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Search results 101 to 196 out of 196 for Nags

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Type Details Score
GXD Expression
GXD Expression
     
Probe: MGI:4417367
Assay Type: RNA in situ
Annotation Date: 2012-06-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:3287422
Stage: TS22
Assay Id: MGI:5421970
Age: embryonic day 14.5
Specimen Label: ES2285; Specimen S884
Detected: false
Specimen Num: 1
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GXD Expression
GXD Expression
     
Probe: MGI:4417367
Assay Type: RNA in situ
Annotation Date: 2012-06-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:3266022
Stage: TS22
Assay Id: MGI:5421970
Age: embryonic day 14.5
Specimen Label: ES2285; Specimen S884
Detected: false
Specimen Num: 1
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•
GXD Expression
GXD Expression
   
Probe: MGI:4417367
Assay Type: RNA in situ
Annotation Date: 2012-06-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:1624622
Stage: TS22
Assay Id: MGI:5421970
Age: embryonic day 14.5
Note: Expression was not detected in the digestive system.
Specimen Label: ES2285; Specimen S884
Detected: false
Specimen Num: 1
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•
GXD Expression
GXD Expression
     
Probe: MGI:4417367
Assay Type: RNA in situ
Annotation Date: 2012-06-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:1721422
Stage: TS22
Assay Id: MGI:5421970
Age: embryonic day 14.5
Specimen Label: ES2285; Specimen S884
Detected: false
Specimen Num: 1
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•
GXD Expression
GXD Expression
     
Probe: MGI:4417367
Assay Type: RNA in situ
Annotation Date: 2012-06-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:1646922
Stage: TS22
Assay Id: MGI:5421970
Age: embryonic day 14.5
Specimen Label: ES2285; Specimen S884
Detected: false
Specimen Num: 1
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•
GXD Expression
GXD Expression
     
Probe: MGI:4417367
Assay Type: RNA in situ
Annotation Date: 2012-06-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:1736222
Stage: TS22
Assay Id: MGI:5421970
Age: embryonic day 14.5
Specimen Label: ES2285; Specimen S884
Detected: false
Specimen Num: 1
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•
GXD Expression
GXD Expression
     
Probe: MGI:4417367
Assay Type: RNA in situ
Annotation Date: 2012-06-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:1683322
Stage: TS22
Assay Id: MGI:5421970
Age: embryonic day 14.5
Specimen Label: ES2285; Specimen S884
Detected: false
Specimen Num: 1
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•
GXD Expression
GXD Expression
     
Probe: MGI:4417367
Assay Type: RNA in situ
Annotation Date: 2012-06-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:1700022
Stage: TS22
Assay Id: MGI:5421970
Age: embryonic day 14.5
Specimen Label: ES2285; Specimen S884
Detected: false
Specimen Num: 1
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•
GXD Expression
GXD Expression
     
Probe: MGI:4417367
Assay Type: RNA in situ
Annotation Date: 2012-06-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:1832122
Stage: TS22
Assay Id: MGI:5421970
Age: embryonic day 14.5
Specimen Label: ES2285; Specimen S884
Detected: false
Specimen Num: 1
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•
GXD Expression
GXD Expression
   
Probe: MGI:4417367
Assay Type: RNA in situ
Annotation Date: 2012-06-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:1876522
Stage: TS22
Assay Id: MGI:5421970
Age: embryonic day 14.5
Note: Expression was not detected in the immune system.
Specimen Label: ES2285; Specimen S884
Detected: false
Specimen Num: 1
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•
GXD Expression
GXD Expression
     
Probe: MGI:4417367
Assay Type: RNA in situ
Annotation Date: 2012-06-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:1741222
Stage: TS22
Assay Id: MGI:5421970
Age: embryonic day 14.5
Specimen Label: ES2285; Specimen S884
Detected: false
Specimen Num: 1
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•
GXD Expression
GXD Expression
     
Probe: MGI:4417367
Assay Type: RNA in situ
Annotation Date: 2012-06-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:1754022
Stage: TS22
Assay Id: MGI:5421970
Age: embryonic day 14.5
Specimen Label: ES2285; Specimen S884
Detected: false
Specimen Num: 1
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•
GXD Expression
GXD Expression
     
Probe: MGI:4417367
Assay Type: RNA in situ
Annotation Date: 2012-06-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:3599822
Stage: TS22
Assay Id: MGI:5421970
Age: embryonic day 14.5
Specimen Label: ES2285; Specimen S884
Detected: false
Specimen Num: 1
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•
GXD Expression
GXD Expression
     
Probe: MGI:4417367
Assay Type: RNA in situ
Annotation Date: 2012-06-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:3280922
Stage: TS22
Assay Id: MGI:5421970
Age: embryonic day 14.5
Specimen Label: ES2285; Specimen S884
Detected: false
Specimen Num: 1
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•
GXD Expression
GXD Expression
     
Probe: MGI:4417367
Assay Type: RNA in situ
Annotation Date: 2012-06-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:1833322
Stage: TS22
Assay Id: MGI:5421970
Age: embryonic day 14.5
Specimen Label: ES2285; Specimen S884
Detected: false
Specimen Num: 1
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•
GXD Expression
GXD Expression
     
Probe: MGI:4417367
Assay Type: RNA in situ
Annotation Date: 2012-06-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:3287022
Stage: TS22
Assay Id: MGI:5421970
Age: embryonic day 14.5
Specimen Label: ES2285; Specimen S884
Detected: false
Specimen Num: 1
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GXD Expression
GXD Expression
     
Probe: MGI:4417367
Assay Type: RNA in situ
Annotation Date: 2012-06-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:1752522
Stage: TS22
Assay Id: MGI:5421970
Age: embryonic day 14.5
Specimen Label: ES2285; Specimen S884
Detected: false
Specimen Num: 1
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GXD Expression
GXD Expression
     
Probe: MGI:4417367
Assay Type: RNA in situ
Annotation Date: 2012-06-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:1821522
Stage: TS22
Assay Id: MGI:5421970
Age: embryonic day 14.5
Specimen Label: ES2285; Specimen S884
Detected: false
Specimen Num: 1
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GXD Expression
GXD Expression
     
Probe: MGI:4417367
Assay Type: RNA in situ
Annotation Date: 2012-06-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:3557722
Stage: TS22
Assay Id: MGI:5421970
Age: embryonic day 14.5
Specimen Label: ES2285; Specimen S884
Detected: false
Specimen Num: 1
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GXD Expression
GXD Expression
     
Probe: MGI:4417367
Assay Type: RNA in situ
Annotation Date: 2012-06-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:1702122
Stage: TS22
Assay Id: MGI:5421970
Age: embryonic day 14.5
Specimen Label: ES2285; Specimen S884
Detected: false
Specimen Num: 1
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•
GXD Expression
GXD Expression
     
Probe: MGI:4417367
Assay Type: RNA in situ
Annotation Date: 2012-06-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:1756322
Stage: TS22
Assay Id: MGI:5421970
Age: embryonic day 14.5
Specimen Label: ES2285; Specimen S884
Detected: false
Specimen Num: 1
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•
GXD Expression
GXD Expression
     
Probe: MGI:4417367
Assay Type: RNA in situ
Annotation Date: 2012-06-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:1668822
Stage: TS22
Assay Id: MGI:5421970
Age: embryonic day 14.5
Specimen Label: ES2285; Specimen S884
Detected: false
Specimen Num: 1
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GXD Expression
GXD Expression
     
Probe: MGI:4417367
Assay Type: RNA in situ
Annotation Date: 2012-06-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:1757722
Stage: TS22
Assay Id: MGI:5421970
Age: embryonic day 14.5
Specimen Label: ES2285; Specimen S884
Detected: false
Specimen Num: 1
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GXD Expression
GXD Expression
     
Probe: MGI:4417367
Assay Type: RNA in situ
Annotation Date: 2012-06-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:1757522
Stage: TS22
Assay Id: MGI:5421970
Age: embryonic day 14.5
Specimen Label: ES2285; Specimen S884
Detected: false
Specimen Num: 1
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•
GXD Expression
GXD Expression
     
Probe: MGI:4417367
Assay Type: RNA in situ
Annotation Date: 2012-06-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:1738322
Stage: TS22
Assay Id: MGI:5421970
Age: embryonic day 14.5
Specimen Label: ES2285; Specimen S884
Detected: false
Specimen Num: 1
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GXD Expression
GXD Expression
     
Probe: MGI:4417367
Assay Type: RNA in situ
Annotation Date: 2012-06-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:1802422
Stage: TS22
Assay Id: MGI:5421970
Age: embryonic day 14.5
Specimen Label: ES2285; Specimen S884
Detected: false
Specimen Num: 1
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GXD Expression
GXD Expression
   
Probe: MGI:4417367
Assay Type: RNA in situ
Annotation Date: 2012-06-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:1768022
Stage: TS22
Assay Id: MGI:5421970
Age: embryonic day 14.5
Note: Expression was not detected in the skull (base and vault).
Specimen Label: ES2285; Specimen S884
Detected: false
Specimen Num: 1
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GXD Expression
GXD Expression
   
Probe: MGI:4417367
Assay Type: RNA in situ
Annotation Date: 2012-06-12
Strength: Absent
Sex: Not Specified
Emaps: EMAPS:2672022
Stage: TS22
Assay Id: MGI:5421970
Age: embryonic day 14.5
Note: Expression was not detected in whisker follicle.
Specimen Label: ES2285; Specimen S884
Detected: false
Specimen Num: 1
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Publication
- | J:79826
   
First Author: Eckhardt M
Year: 2002
Journal: GenBank Submission
Title: Mus musculus mRNA for amino-acid N-acetyltransferase (argA gene)
Pages: AJ489814
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Publication
18614015 | J:151002
First Author: Pagliarini DJ
Year: 2008
Journal: Cell
Title: A mitochondrial protein compendium elucidates complex I disease biology.
Volume: 134
Issue: 1
Pages: 112-23
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Publication
- | J:342601
       
First Author: UniProt-GOA
Year: 2012
Title: Gene Ontology annotation based on UniPathway vocabulary mapping
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Publication
- | J:77000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: MGC Data curation in Mouse Genome Informatics
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Publication
14681479 | J:122989
First Author: Visel A
Year: 2004
Journal: Nucleic Acids Res
Title: GenePaint.org: an atlas of gene expression patterns in the mouse embryo.
Volume: 32
Issue: Database issue
Pages: D552-6
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Publication
- | J:57656
     
First Author: Lennon G
Year: 1999
Journal: Database Download
Title: WashU-HHMI Mouse EST Project
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Publication
- | J:136110
     
First Author: Velocigene
Year: 2008
Journal: MGI Direct Data Submission
Title: Alleles produced for the KOMP project by Velocigene (Regeneron Pharmaceuticals)
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Publication
- | J:157065
     
First Author: Helmholtz Zentrum Muenchen GmbH
Year: 2010
Journal: MGI Direct Data Submission
Title: Alleles produced for the EUCOMM and EUCOMMTools projects by the Helmholtz Zentrum Muenchen GmbH (Hmgu)
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Publication
- | J:342604
       
First Author: UniProt-GOA
Year: 2012
Title: Gene Ontology annotation based on UniProtKB/Swiss-Prot Subcellular Location vocabulary mapping, accompanied by conservative changes to GO terms applied by UniProt
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Publication
16602821 | J:162220
First Author: Magdaleno S
Year: 2006
Journal: PLoS Biol
Title: BGEM: an in situ hybridization database of gene expression in the embryonic and adult mouse nervous system.
Volume: 4
Issue: 4
Pages: e86
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Publication
- | J:85000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2003
Title: MGI Sequence Curation Reference
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Publication
- | J:78475
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Chromosome assignment of mouse genes using the Mouse Genome Sequencing Consortium (MGSC) assembly and the ENSEMBL Database
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Publication
11217851 | J:65060
First Author: Kawai J
Year: 2001
Journal: Nature
Title: Functional annotation of a full-length mouse cDNA collection.
Volume: 409
Issue: 6821
Pages: 685-90
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Publication
- | J:293217
       
First Author: GemPharmatech
Year: 2020
Title: GemPharmatech Website.
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Publication
- | J:326541
       
First Author: Cyagen Biosciences Inc.
Year: 2022
Title: Cyagen Biosciences Website.
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Publication
- | J:60000
       
First Author: UniProt-GOA
Year: 2012
Title: Gene Ontology annotation based on UniProtKB/Swiss-Prot keyword mapping
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Publication
- | J:68900
     
First Author: The Jackson Laboratory Mouse Radiation Hybrid Database
Year: 2004
Journal: Database Release
Title: Mouse T31 Radiation Hybrid Data Load
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Publication
12466851 | J:80000
First Author: Okazaki Y
Year: 2002
Journal: Nature
Title: Analysis of the mouse transcriptome based on functional annotation of 60,770 full-length cDNAs.
Volume: 420
Issue: 6915
Pages: 563-73
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Publication
- | J:164563
       
First Author: The Gene Ontology Consortium
Year: 2010
Title: Automated transfer of experimentally-verified manual GO annotation data to mouse-human orthologs
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Publication
21267068 | J:153498
First Author: Diez-Roux G
Year: 2011
Journal: PLoS Biol
Title: A high-resolution anatomical atlas of the transcriptome in the mouse embryo.
Volume: 9
Issue: 1
Pages: e1000582
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Publication
- | J:57747
     
First Author: MGI Genome Annotation Group and UniGene Staff
Year: 2015
Journal: Database Download
Title: MGI-UniGene Interconnection Effort
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Publication
- | J:161428
       
First Author: Marc Feuermann, Huaiyu Mi, Pascale Gaudet, Dustin Ebert, Anushya Muruganujan, Paul Thomas
Year: 2010
Title: Annotation inferences using phylogenetic trees
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Publication
- | J:63103
     
First Author: Mouse Genome Database and National Center for Biotechnology Information
Year: 2000
Journal: Database Release
Title: Entrez Gene Load
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Publication
- | J:262123
     
First Author: Allen Institute for Brain Science
Year: 2004
Journal: Allen Institute
Title: Allen Brain Atlas: mouse riboprobes
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Publication
- | J:144086
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Gene 1.0 ST Array Platform
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Publication
- | J:155721
     
First Author: Mouse Genome Informatics (MGI) and The National Center for Biotechnology Information (NCBI)
Year: 2010
Journal: Database Download
Title: Consensus CDS project
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Publication
- | J:85324
     
First Author: Mouse Genome Informatics Group
Year: 2003
Journal: Database Procedure
Title: Automatic Encodes (AutoE) Reference
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Publication
- | J:53168
     
First Author: Bairoch A
Year: 1999
Journal: Database Release
Title: SWISS-PROT Annotated protein sequence database
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Publication
- | J:91388
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and Loading Genome Assembly Coordinates from Ensembl Annotations
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Publication
- | J:155221
     
First Author: Mouse Genome Informatics
Year: 2010
Journal: Database Release
Title: Protein Ontology Association Load.
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Publication
- | J:90438
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2005
Title: Obtaining and loading genome assembly coordinates from NCBI annotations
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Publication
- | J:144087
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2009
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome 430 2.0 Array Platform
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DO Term
DOID:0112258 | N-acetylglutamate synthase deficiency
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Protein Domain
IPR006855 | Vertebrate-like_GNAT_dom
Type: Domain
Description: The N-acetyltransferases (NAT) (EC 2.3.1.-) are enzymes that use acetylcoenzyme A (CoA) to transfer an acetyl group to a substrate, a reactionimplicated in various functions from bacterial antibiotic resistance tomammalian circadian rhythm and chromatin remodeling. The Gcn5-relatedN-acetyltransferases (GNAT) catalyze the transfer of the acetyl from the CoAdonor to a primary amine of the acceptor. The GNAT proteins share a domaincomposed of four conserved sequence motifs A-D [, ]. This GNAT domain isnamed after yeast GCN5 (from General Control Nonrepressed) and related histoneacetyltransferases (HATs) like Hat1 and PCAF. HATs acetylate lysine residuesof amino terminal histone tails, resulting in transcription activation.Another category of GNAT, the aminoglycoside N-acetyltransferases, conferantibiotic resistance by catalyzing the acetylation of amino groups inaminoglycoside antibiotics []. GNAT proteins can also have anabolic andcatabolic functions in both prokaryotes and eukaryotes [, , , , ].The acetyltransferase/GNAT domain forms a structurally conserved fold of 6 to7 beta strands (B) and 4 helices (H) in the topologyB1-H1-H2-B2-B3-B4-H3-B5-H4-B6, followed by a C-terminal strand which may befrom the same monomer or contributed by another [, ]. MotifsD (B2-B3), A (B4-H3) and B (B5-H4) are collectively called the HAT core[, , ], while the N-terminal motif C (B1-H1) is less conserved.This entry represents the vertebrate-likeNAGS-type GNAT domain [].
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Protein
Q8R4H7
Organism: Mus musculus/domesticus
Length: 527  
Fragment?: false
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Publication
23894642 | -
First Author: Zhao G
Year: 2013
Journal: PLoS One
Title: Crystal structure of the N-acetyltransferase domain of human N-acetyl-L-glutamate synthase in complex with N-acetyl-L-glutamate provides insights into its catalytic and regulatory mechanisms.
Volume: 8
Issue: 7
Pages: e70369
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Publication
12527305 | -
First Author: He H
Year: 2003
Journal: J Mol Biol
Title: Crystal structure of tabtoxin resistance protein complexed with acetyl coenzyme A reveals the mechanism for beta-lactam acetylation.
Volume: 325
Issue: 5
Pages: 1019-30
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Publication
15581578 | -
First Author: Vetting MW
Year: 2005
Journal: Arch Biochem Biophys
Title: Structure and functions of the GNAT superfamily of acetyltransferases.
Volume: 433
Issue: 1
Pages: 212-26
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Publication
12592013 | -
First Author: Burk DL
Year: 2003
Journal: Protein Sci
Title: X-ray structure of the AAC(6')-Ii antibiotic resistance enzyme at 1.8 A resolution; examination of oligomeric arrangements in GNAT superfamily members.
Volume: 12
Issue: 3
Pages: 426-37
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Publication
10940244 | -
 
First Author: Dyda F
Year: 2000
Journal: Annu Rev Biophys Biomol Struct
Title: GCN5-related N-acetyltransferases: a structural overview.
Volume: 29
Pages: 81-103
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Publication
9175471 | -
First Author: Neuwald AF
Year: 1997
Journal: Trends Biochem Sci
Title: GCN5-related histone N-acetyltransferases belong to a diverse superfamily that includes the yeast SPT10 protein.
Volume: 22
Issue: 5
Pages: 154-5
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Publication
8939437 | -
First Author: Yu YG
Year: 1996
Journal: Mol Microbiol
Title: Acetylglutamate synthase from Neurospora crassa: structure and regulation of expression.
Volume: 22
Issue: 3
Pages: 545-54
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Protein Domain
IPR037528 | ArgB
Type: Family
Description: N -Acetylglutamate (NAG) fulfils distinct biological roles in lower and higher organisms. In prokaryotes, lower eukaryotes and plants it is the first intermediate in the biosynthesis of arginine, whereas in ureotelic (excreting nitrogen mostly in the form of urea) vertebrates, it is an essential allosteric cofactor for carbamyl phosphate synthetase I (CPSI), the first enzyme of the urea cycle. The pathway that leads from glutamate to arginine in lower organisms employs eight steps, starting with the acetylation of glutamate to form NAG. In these species, NAG can be produced by two enzymatic reactions: one catalysed by NAG synthase (NAGS) and the other by ornithine acetyltransferase (OAT). In ureotelic species, NAG is produced exclusively by NAGS. In lower organisms, NAGS is feedback-inhibited by L-arginine, whereas mammalian NAGS activity is significantly enhanced by this amino acid. The NAGS genes of bacteria, fungi and mammals are more diverse than other arginine-biosynthesis and urea-cycle genes. The evolutionary relationship between the distinctly different roles of NAG and its metabolism in lower and higher organisms remains to be determined [].The pathway from glutamate to arginine is: NAGS; N-acetylglutamate synthase () (glutamate to N-acetylglutamate)NAGK; N-acetylglutamate kinase () (N-acetylglutamate to N-acetylglutamate-5P)N-acetyl-gamma-glutamyl-phosphate reductase () (N-acetylglutamate-5P to N-acetylglumate semialdehyde)Acetylornithine aminotransferase () (N-acetylglumate semialdehyde to N-acetylornithine)Acetylornithine deacetylase () (N-acetylornithine to ornithine)Arginase () (ornithine to arginine)This family represents acetylglutamate kinase ArgB ().
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Protein Domain
IPR004662 | AcgluKinase_fam
Type: Family
Description: N -Acetylglutamate (NAG) fulfils distinct biological roles in lower and higher organisms. In prokaryotes, lower eukaryotes and plants it is the first intermediate in the biosynthesis of arginine, whereas in ureotelic (excreting nitrogen mostly in the form of urea) vertebrates, it is an essential allosteric cofactor for carbamyl phosphate synthetase I (CPSI), the first enzyme of the urea cycle. The pathway that leads from glutamate to arginine in lower organisms employs eight steps, starting with the acetylation of glutamate to form NAG. In these species, NAG can be produced by two enzymatic reactions: one catalysed by NAG synthase (NAGS) and the other by ornithine acetyltransferase (OAT). In ureotelic species, NAG is produced exclusively by NAGS. In lower organisms, NAGS is feedback-inhibited by L-arginine, whereas mammalian NAGS activity is significantly enhanced by this amino acid. The NAGS genes of bacteria, fungi and mammals are more diverse than other arginine-biosynthesis and urea-cycle genes. The evolutionary relationship between the distinctly different roles of NAG and its metabolism in lower and higher organisms remains to be determined [].The pathway from glutamate to arginine is: NAGS; N-acetylglutamate synthase () (glutamate to N-acetylglutamate)NAGK; N-acetylglutamate kinase () (N-acetylglutamate to N-acetylglutamate-5P)N-acetyl-gamma-glutamyl-phosphate reductase () (N-acetylglutamate-5P to N-acetylglumate semialdehyde)Acetylornithine aminotransferase () (N-acetylglumate semialdehyde to N-acetylornithine)Acetylornithine deacetylase () (N-acetylornithine to ornithine)Arginase () (ornithine to arginine)This family includes acetylglutamate kinase and related enzymes [LysW]-aminoadipate/[LysW]-glutamate kinase (LysZ), which is involved both in the biosynthesis of lysine and arginine [], and [LysW]-aminoadipate kinase [].
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Protein Domain
IPR011242 | ArgB_GNAT
Type: Family
Description: N -Acetylglutamate (NAG) fulfils distinct biological roles in lower and higher organisms. In prokaryotes, lower eukaryotes and plants it is the first intermediate in the biosynthesis of arginine, whereas in ureotelic (excreting nitrogen mostly in the form of urea) vertebrates, it is an essential allosteric cofactor for carbamyl phosphate synthetase I (CPSI), the first enzyme of the urea cycle. The pathway that leads from glutamate to arginine in lower organisms employs eight steps, starting with the acetylation of glutamate to form NAG. In these species, NAG can be produced by two enzymatic reactions: one catalysed by NAG synthase (NAGS) and the other by ornithine acetyltransferase (OAT). In ureotelic species, NAG is produced exclusively by NAGS. In lower organisms, NAGS is feedback-inhibited by L-arginine, whereas mammalian NAGS activity is significantly enhanced by this amino acid. The NAGS genes of bacteria, fungi and mammals are more diverse than other arginine-biosynthesis and urea-cycle genes. The evolutionary relationship between the distinctly different roles of NAG and its metabolism in lower and higher organisms remains to be determined [].The pathway from glutamate to arginine is: NAGS; N-acetylglutamate synthase () (glutamate to N-acetylglutamate)NAGK; N-acetylglutamate kinase () (N-acetylglutamate to N-acetylglutamate-5P)N-acetyl-gamma-glutamyl-phosphate reductase () (N-acetylglutamate-5P to N-acetylglumate semialdehyde)Acetylornithine aminotransferase () (N-acetylglumate semialdehyde to N-acetylornithine)Acetylornithine deacetylase () (N-acetylornithine to ornithine)Arginase () (ornithine to arginine)This entry represents N-acetylglutamate kinase (NAGK) with a C-terminal GNAT domain. Majority of proteins in this entry are from bacteria, including argB from Xylella fastidiosa (UniProt:Q9PEM7).
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Protein Domain
IPR011243 | GlcNAc_Synth_met
Type: Family
Description: N -Acetylglutamate (NAG) fulfils distinct biological roles in lower and higher organisms. In prokaryotes, lower eukaryotes and plants it is the first intermediate in the biosynthesis of arginine, whereas in ureotelic (excreting nitrogen mostly inthe form of urea) vertebrates, it is an essential allosteric cofactor for carbamyl phosphate synthetase I (CPSI), the first enzyme of the urea cycle. The pathway that leads from glutamate to arginine in lower organisms employs eight steps, starting with the acetylation of glutamate to form NAG. In these species, NAG can be produced by two enzymatic reactions: one catalysed by NAG synthase (NAGS) and the other by ornithine acetyltransferase (OAT). In ureotelic species, NAG is produced exclusively by NAGS. In lower organisms, NAGS is feedback-inhibited by L-arginine, whereas mammalian NAGS activity is significantly enhanced by this amino acid. The NAGS genes of bacteria, fungi and mammals are more diverse than other arginine-biosynthesis and urea-cycle genes. The evolutionary relationship between the distinctly different roles of NAG and its metabolism in lower and higher organisms remains to be determined [].The pathway from glutamate to arginine is: NAGS; N-acetylglutamate synthase () (glutamate to N-acetylglutamate)NAGK; N-acetylglutamate kinase () (N-acetylglutamate to N-acetylglutamate-5P)N-acetyl-gamma-glutamyl-phosphate reductase () (N-acetylglutamate-5P to N-acetylglumate semialdehyde)Acetylornithine aminotransferase () (N-acetylglumate semialdehyde to N-acetylornithine)Acetylornithine deacetylase () (N-acetylornithine to ornithine)Arginase () (ornithine to arginine)This group represents a N-acetylglutamate synthase, animal type [].
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Protein Domain
IPR011190 | GlcNAc_Synth_fun
Type: Family
Description: N -Acetylglutamate (NAG) fulfils distinct biological roles in lower and higher organisms. In prokaryotes, lower eukaryotes and plants it is the first intermediate in the biosynthesis of arginine, whereas in ureotelic (excreting nitrogen mostly in the form of urea) vertebrates, it is an essential allosteric cofactor for carbamyl phosphate synthetase I (CPSI), the first enzyme of the urea cycle. The pathway that leads from glutamate to arginine in lower organisms employs eight steps, starting with the acetylation of glutamate to form NAG. In these species, NAG can be produced by two enzymatic reactions: one catalysed by NAG synthase (NAGS) and the other by ornithine acetyltransferase (OAT). In ureotelic species, NAG is produced exclusively by NAGS. In lower organisms, NAGS is feedback-inhibited by L-arginine, whereas mammalian NAGS activity is significantly enhanced by this amino acid. The NAGS genes of bacteria, fungi and mammals are more diverse than other arginine-biosynthesis and urea-cycle genes. The evolutionary relationship between the distinctly different roles of NAG and its metabolism in lower and higher organisms remains to be determined [].The pathway from glutamate to arginine is: NAGS; N-acetylglutamate synthase () (glutamate to N-acetylglutamate)NAGK; N-acetylglutamate kinase () (N-acetylglutamate to N-acetylglutamate-5P)N-acetyl-gamma-glutamyl-phosphate reductase () (N-acetylglutamate-5P to N-acetylglumate semialdehyde)Acetylornithine aminotransferase () (N-acetylglumate semialdehyde to N-acetylornithine)Acetylornithine deacetylase () (N-acetylornithine to ornithine)Arginase () (ornithine to arginine)This group represents a N-acetylglutamate synthase, belonging to the Ascomycetes [, ].
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Publication
12633501 | -
First Author: Caldovic L
Year: 2003
Journal: Biochem J
Title: N-acetylglutamate and its changing role through evolution.
Volume: 372
Issue: Pt 2
Pages: 279-90
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Publication
25392000 | -
First Author: Yoshida A
Year: 2015
Journal: J Biol Chem
Title: Structural insight into amino group-carrier protein-mediated lysine biosynthesis: crystal structure of the LysZ·LysW complex from Thermus thermophilus.
Volume: 290
Issue: 1
Pages: 435-47
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Publication
11553611 | -
First Author: Abadjieva A
Year: 2001
Journal: J Biol Chem
Title: A new yeast metabolon involving at least the two first enzymes of arginine biosynthesis: acetylglutamate synthase activity requires complex formation with acetylglutamate kinase.
Volume: 276
Issue: 46
Pages: 42869-80
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Publication
1406250 | -
First Author: Floriano B
Year: 1992
Journal: Mol Microbiol
Title: Isolation of arginine auxotrophs, cloning by mutant complementation, and sequence analysis of the argC gene from the cyanobacterium Anabaena species PCC 7120.
Volume: 6
Issue: 15
Pages: 2085-94
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Publication
17316682 | -
First Author: Cherney LT
Year: 2007
Journal: J Mol Biol
Title: Crystal structure of N-acetyl-gamma-glutamyl-phosphate reductase from Mycobacterium tuberculosis in complex with NADP(+).
Volume: 367
Issue: 5
Pages: 1357-69
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Protein Domain
IPR023013 | AGPR_AS
Type: Active_site
Description: N -Acetylglutamate (NAG) fulfils distinct biological roles in lower and higher organisms. In prokaryotes, lower eukaryotes and plants it is the first intermediate in the biosynthesis of arginine, whereas in ureotelic (excreting nitrogen mostly in the form of urea) vertebrates, it is an essential allosteric cofactor for carbamyl phosphate synthetase I (CPSI), the first enzyme of the urea cycle. The pathway that leads from glutamate to arginine in lower organisms employs eight steps, starting with the acetylation of glutamate to form NAG. In these species, NAG can be produced by two enzymatic reactions: one catalysed by NAG synthase (NAGS) and the other by ornithine acetyltransferase (OAT). In ureotelic species, NAG is produced exclusively by NAGS. In lower organisms, NAGS is feedback-inhibited by L-arginine, whereas mammalian NAGS activity is significantly enhanced by this amino acid. The NAGS genes of bacteria, fungi and mammals are more diverse than other arginine-biosynthesis and urea-cycle genes. The evolutionary relationship between the distinctly different roles of NAG and its metabolism in lower and higher organisms remains to be determined [].The pathway from glutamate to arginine is: NAGS; N-acetylglutamate synthase () (glutamate to N-acetylglutamate)NAGK; N-acetylglutamate kinase () (N-acetylglutamate to N-acetylglutamate-5P)N-acetyl-gamma-glutamyl-phosphate reductase () (N-acetylglutamate-5P to N-acetylglumate semialdehyde)Acetylornithine aminotransferase () (N-acetylglumate semialdehyde to N-acetylornithine)Acetylornithine deacetylase () (N-acetylornithine to ornithine)Arginase () (ornithine to arginine)N-acetyl-gamma-glutamyl-phosphate reductase () (AGPR) [, ]is the enzyme that catalyzes the third step in the biosynthesis of arginine from glutamate, the NADP-dependent reduction of N-acetyl-5-glutamyl phosphate into N-acetylglutamate 5-semialdehyde. In bacteria it is a monofunctional protein of 35 to 38kDa (gene argC) while in fungi it is part of a bifunctional mitochondrial enzyme (gene ARG5,6, arg11 or arg-6) which contains a N-terminal acetylglutamate kinase (() domain and a C-terminal AGPR domain. In the Mycobacterium tuberculosis enzyme, a cysteine has been shown to be implicated in the catalytic activity; the region around this residue is well conserved and is used as a signature pattern for the proteins in this entry [, ].
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Publication
16122935 | -
First Author: Slocum RD
Year: 2005
Journal: Plant Physiol Biochem
Title: Genes, enzymes and regulation of arginine biosynthesis in plants.
Volume: 43
Issue: 8
Pages: 729-45
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Protein Domain
IPR033719 | NAGS_kin
Type: Domain
Description: This is the N-acetylglutamate (NAG) kinase-like domain of the NAG Synthase (NAGS) of the arginine-biosynthesis pathway (ABP) found in gamma- and beta-proteobacteria and higher plant chloroplasts. The domain architecture of these NAGS consists of an N-terminal NAG kinase-like (ArgB) domain and a C-terminal NAG synthase, acetyltransferase (ArgA) domain. Both bacterial and plant sequences have a conserved N-terminal extension; a similar sequence in the NAG kinases of the cyclic arginine-biosynthesis pathway has been implicated in feedback inhibition sensing. Plant sequences also have an N-terminal chloroplast transit peptide and an insert (approx. 70 residues) in the C-terminal region of ArgB [, ].
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HT Experiment
E-GEOD-30017 | Widespread regulated alternative splicing of single codons accelerates proteome evolution
Series Id: GSE30017
Experiment Type: RNA-Seq
Study Type: Baseline
Source: ArrayExpress
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Publication
1339424 | -
First Author: Ludovice M
Year: 1992
Journal: J Bacteriol
Title: Characterization of the Streptomyces clavuligerus argC gene encoding N-acetylglutamyl-phosphate reductase: expression in Streptomyces lividans and effect on clavulanic acid production.
Volume: 174
Issue: 14
Pages: 4606-13
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Publication
7907589 | -
First Author: Gessert SF
Year: 1994
Journal: J Biol Chem
Title: A polyprotein precursor of two mitochondrial enzymes in Neurospora crassa. Gene structure and precursor processing.
Volume: 269
Issue: 11
Pages: 8189-203
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Protein Domain
IPR010136 | AGPR_type-2
Type: Family
Description: N -Acetylglutamate (NAG) fulfils distinct biological roles in lower and higher organisms. In prokaryotes, lower eukaryotes and plants it is the first intermediate in the biosynthesis of arginine, whereas in ureotelic (excreting nitrogen mostly in the form of urea) vertebrates, it is an essential allosteric cofactor for carbamyl phosphate synthetase I (CPSI), the first enzyme of the urea cycle. The pathway that leads from glutamate to arginine in lower organisms employs eight steps, starting with the acetylation of glutamate to formNAG. In these species, NAG can be produced by two enzymatic reactions: one catalysed by NAG synthase (NAGS) and the other by ornithine acetyltransferase (OAT). In ureotelic species, NAG is produced exclusively by NAGS. In lower organisms, NAGS is feedback-inhibited by L-arginine, whereas mammalian NAGS activity is significantly enhanced by this amino acid. The NAGS genes of bacteria, fungi and mammals are more diverse than other arginine-biosynthesis and urea-cycle genes. The evolutionary relationship between the distinctly different roles of NAG and its metabolism in lower and higher organisms remains to be determined [].The pathway from glutamate to arginine is: NAGS; N-acetylglutamate synthase () (glutamate to N-acetylglutamate)NAGK; N-acetylglutamate kinase () (N-acetylglutamate to N-acetylglutamate-5P)N-acetyl-gamma-glutamyl-phosphate reductase () (N-acetylglutamate-5P to N-acetylglumate semialdehyde)Acetylornithine aminotransferase () (N-acetylglumate semialdehyde to N-acetylornithine)Acetylornithine deacetylase () (N-acetylornithine to ornithine)Arginase () (ornithine to arginine)N-acetyl-gamma-glutamyl-phosphate reductase () (AGPR, NAGSA dehydrogenase) [, ]is the enzyme that catalyses the third step in the biosynthesis of arginine from glutamate, the NADP-dependent reduction of N-acetyl-5-glutamyl phosphate into N-acetylglutamate 5-semialdehyde. In bacteria it is a monofunctional protein of 35 to 38kDa (gene argC), while in fungi it is part of a bifunctional mitochondrial enzyme (gene ARG5,6, arg11 or arg-6) which contains a N-terminal acetylglutamate kinase () domain and a C-terminal AGPR domain. In the Escherichia coli enzyme, a cysteine has been shown to be implicated in the catalytic activity, and the region around this residue is well conserved.This entry represents the less common of two related families of N-acetyl-gamma-glutamyl-phosphate reductase, an enzyme catalyzing the third step or Arg biosynthesis from Glu. The two families differ by phylogeny, similarity clustering, and gap architecture in a multiple sequence alignment.
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Publication
17933574 | J:130077
First Author: Deignan JL
Year: 2008
Journal: Mol Genet Metab
Title: Contrasting features of urea cycle disorders in human patients and knockout mouse models.
Volume: 93
Issue: 1
Pages: 7-14
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Publication
21757002 | J:180347
First Author: Renga B
Year: 2011
Journal: Biochim Biophys Acta
Title: The nuclear receptor FXR regulates hepatic transport and metabolism of glutamine and glutamate.
Volume: 1812
Issue: 11
Pages: 1522-31
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Publication
19620981 | -
First Author: Horie A
Year: 2009
Journal: Nat Chem Biol
Title: Discovery of proteinaceous N-modification in lysine biosynthesis of Thermus thermophilus.
Volume: 5
Issue: 9
Pages: 673-9
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Publication
26966182 | -
First Author: Shimizu T
Year: 2016
Journal: J Biol Chem
Title: Crystal Structure of the LysY·LysW Complex from Thermus thermophilus.
Volume: 291
Issue: 19
Pages: 9948-59
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Protein Domain
IPR000706 | AGPR_type-1
Type: Family
Description: N -Acetylglutamate (NAG) fulfils distinct biological roles in lower and higher organisms. In prokaryotes, lower eukaryotes and plants it is the first intermediate in the biosynthesis of arginine, whereas in ureotelic (excreting nitrogen mostly in the form of urea) vertebrates, it is an essential allosteric cofactor for carbamyl phosphate synthetase I (CPSI), the first enzyme of the urea cycle. The pathway that leads from glutamate to arginine in lower organisms employs eight steps, starting with the acetylation of glutamate to form NAG. In these species, NAG can be produced by two enzymatic reactions: one catalysed by NAG synthase (NAGS) and the other by ornithine acetyltransferase (OAT). In ureotelic species, NAG is produced exclusively by NAGS. In lower organisms, NAGS is feedback-inhibited by L-arginine, whereas mammalian NAGS activity is significantly enhanced by this amino acid. The NAGS genes of bacteria, fungi and mammals are more diverse than other arginine-biosynthesis and urea-cycle genes. The evolutionary relationship between the distinctly different roles of NAG and its metabolism in lower and higher organisms remains to be determined [].The pathway from glutamate to arginine is: NAGS; N-acetylglutamate synthase () (glutamate to N-acetylglutamate)NAGK; N-acetylglutamate kinase () (N-acetylglutamate to N-acetylglutamate-5P)N-acetyl-gamma-glutamyl-phosphate reductase () (N-acetylglutamate-5P to N-acetylglumate semialdehyde)Acetylornithine aminotransferase () (N-acetylglumate semialdehyde to N-acetylornithine)Acetylornithine deacetylase () (N-acetylornithine to ornithine)Arginase () (ornithine to arginine)N-acetyl-gamma-glutamyl-phosphate reductase () (AGPR, NAGSA dehydrogenase) [, ]is the enzyme that catalyses the third step in the biosynthesis of arginine from glutamate, the NADP-dependent reduction of N-acetyl-5-glutamyl phosphate into N-acetylglutamate 5-semialdehyde. In bacteria it is a monofunctional protein of 35 to 38kDa (gene argC), while in fungi it is part of a bifunctional mitochondrial enzyme (gene ARG5,6, arg11 or arg-6) which contains a N-terminal acetylglutamate kinase () domain and a C-terminal AGPR domain. In the Escherichia coli enzyme, a cysteine has been shown to be implicated in the catalytic activity, and the region around this residue is well conserved.This entry represents the more common of two related families of N-acetyl-gamma-glutamyl-phosphate reductase, an enzyme catalyzing the third step or Arg biosynthesis from Glu. The two families differ by phylogeny, similarity clustering, and the gap architecture in a multiple sequence alignment. Bacterial members of this family tend to be found within Arg biosynthesis operons. This family also includes LysY (LysW-L-2-aminoadipate/LysW-L-glutamate phosphate reductase), which is involved in both the arginine and lysine biosynthetic pathways. Several bacteria and archaea utilize the amino group-carrier protein, LysW, for lysine biosynthesis from alpha-aminoadipate (AAA). In some cases, such as Sulfolobus, LysW is also used to protect the amino group of glutamate in arginine biosynthesis. After LysW modification, AAA and glutamate are converted to lysine and ornithine, respectively, by a single set of enzymes with dual functions []. LysY is the third enzyme in lysine biosynthesis from AAA []. LysY shows high sequence identity and functional similarities with ArgC, and they are considered to have evolved from a common ancestor [, ].
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Publication
23434852 | -
First Author: Ouchi T
Year: 2013
Journal: Nat Chem Biol
Title: Lysine and arginine biosyntheses mediated by a common carrier protein in Sulfolobus.
Volume: 9
Issue: 4
Pages: 277-83
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Publication
22235189 | J:356906
First Author: Bradley RK
Year: 2012
Journal: PLoS Biol
Title: Alternative splicing of RNA triplets is often regulated and accelerates proteome evolution.
Volume: 10
Issue: 1
Pages: e1001229
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Publication
10613839 | -
First Author: Nishida H
Year: 1999
Journal: Genome Res
Title: A prokaryotic gene cluster involved in synthesis of lysine through the amino adipate pathway: a key to the evolution of amino acid biosynthesis.
Volume: 9
Issue: 12
Pages: 1175-83
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Publication
32174131 | J:309973
First Author: Galsgaard KD
Year: 2020
Journal: Am J Physiol Gastrointest Liver Physiol
Title: Glucagon receptor signaling is not required for N-carbamoyl glutamate- and l-citrulline-induced ureagenesis in mice.
Volume: 318
Issue: 5
Pages: G912-G927
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MouseMine is a collaboration between MGI at The Jackson Laboratory and the InterMine project at the Cambridge Systems Biology Centre. MouseMine is funded through a grant from the NIH/NHGRI.The Jackson Laboratory makes no representation about the suitability or accuracy of this software or data for any purpose, and makes no warranties, either express or implied, including merchantability and fitness for a particular purpose or that the use of this software or data will not infringe any third party patents, copyrights, trademarks, or other rights. the software and data are provided "as is". This software and data are provided to enhance knowledge and encourage progress in the scientific community and are to be used only for research and educational purposes. Any reproduction or use for commercial purpose is prohibited without the prior express written permission of the Jackson Laboratory.

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