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Search results 201 to 234 out of 234 for Ppox

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Type Details Score
Publication
- | J:342605
       
First Author: GOA curators
Year: 2016
Title: Automatic transfer of experimentally verified manual GO annotation data to orthologs using Ensembl Compara
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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
- | J:75000
       
First Author: Mouse Genome Informatics Scientific Curators
Year: 2002
Title: Mouse Genome Informatics Computational Sequence to Gene Associations
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Publication
- | J:157972
     
First Author: Mouse Genome Informatics Scientific Curators
Year: 2010
Journal: Database Download
Title: Mouse Microarray Data Integration in Mouse Genome Informatics, the Affymetrix GeneChip Mouse Genome U74 Array Platform (A, B, C v2).
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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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Protein
O55241
Organism: Mus musculus/domesticus
Length: 130  
Fragment?: false
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Publication
23621493 | -
First Author: Wang P
Year: 2013
Journal: J Am Chem Soc
Title: Uncovering the enzymes that catalyze the final steps in oxytetracycline biosynthesis.
Volume: 135
Issue: 19
Pages: 7138-41
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Protein Domain
IPR024031 | MSMEG_5819/OxyR
Type: Family
Description: F420 (or 8-hydroxy-5-deazaflavin) is a coenzyme involved in redox reactions in methanogens. A Genome Properties metabolic reconstruction for F420 biosynthesis shows that slightly over 10 percent of all prokaryotes with fully sequenced genomes, including about two thirds of the Actinomycetales, make F420. This subfamily within the PPOX family occurs in at least 19 distinct species of F420 producers and is likely to bind F420 rather than FMN (flavin mononucleotide or riboflavin-5'-phosphate). The member OxyR was shown in Streptomyces rimosusto use F420 to catalyze a C5a-C11a reduction in tetracycline or oxytetracycline biosynthesis [, ], and OxyR is also known as 5a,11a-dehydrotetracycline/5a,11a-dehydrooxytetracycline reductase.
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Protein Domain
IPR019966 | F420-dep_enz_PPOX_Rv3369
Type: Family
Description: A Genome Properties metabolic reconstruction for F420 biosynthesis shows that slightly over 10 percent of all prokaryotes with fully sequenced genomes, including about two thirds of the Actinomycetales, make F420. A variant of the Partial Phylogenetic Profiling algorithm, SIMBAL, shows that this protein likely binds F420 in a cleft similar to that in which the homologous enzyme pyridoxamine phosphate oxidase (PPOX) binds FMN [].
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Protein Domain
IPR019967 | F420-dep_enz_PPOX_Rv0121
Type: Family
Description: A Genome Properties metabolic reconstruction for F420 biosynthesis shows that slightly over 10 percent of all prokaryotes with fully sequenced genomes, including about two thirds of the Actinomycetales, make F420. A variant of the Partial Phylogenetic Profiling algorithm, SIMBAL, shows that this protein likely binds F420 in a cleft similar to that in which the homologous enzyme pyridoxamine phosphate oxidase (PPOX) binds FMN [].
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Protein Domain
IPR019965 | PPOX_F420-dep_Rv2061_put
Type: Family
Description: A Genome Properties metabolic reconstruction for F420 biosynthesis shows that slightly over 10 percent of all prokaryotes with fully sequenced genomes, including about two thirds of the Actinomycetales, make F420. A variant of the Partial Phylogenetic Profiling algorithm, SIMBAL, shows that this protein likely binds F420 in a cleft similar to that in which the homologous enzyme pyridoxamine phosphate oxidase (PPOX) binds FMN [].
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Publication
20675471 | -
First Author: Selengut JD
Year: 2010
Journal: J Bacteriol
Title: Unexpected abundance of coenzyme F(420)-dependent enzymes in Mycobacterium tuberculosis and other actinobacteria.
Volume: 192
Issue: 21
Pages: 5788-98
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Protein Domain
IPR026324 | Haem_oxygenase_HugZ
Type: Family
Description: Members of this protein family are HugZ, a class of heme oxygenase that belongs to the PPOX family and lacks homology to the HmuO family. This enzyme releases iron during the conversion of heme to biliverdin [, ].
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Publication
22020097 | -
First Author: Zhang R
Year: 2011
Journal: Biochem Biophys Res Commun
Title: Crystal structure of Campylobacter jejuni ChuZ: a split-barrel family heme oxygenase with a novel heme-binding mode.
Volume: 415
Issue: 1
Pages: 82-7
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Publication
15205415 | -
First Author: Wyckoff EE
Year: 2004
Journal: J Bacteriol
Title: HutZ is required for efficient heme utilization in Vibrio cholerae.
Volume: 186
Issue: 13
Pages: 4142-51
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Publication
22627893 | -
First Author: Uchida T
Year: 2012
Journal: Chem Commun (Camb)
Title: A heme degradation enzyme, HutZ, from Vibrio cholerae.
Volume: 48
Issue: 53
Pages: 6741-3
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Publication
28481076 | -
First Author: Uchida T
Year: 2017
Journal: Biochemistry
Title: Heme Proximal Hydrogen Bonding between His170 and Asp132 Plays an Essential Role in the Heme Degradation Reaction of HutZ from Vibrio cholerae.
Volume: 56
Issue: 21
Pages: 2723-2734
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Publication
28607990 | -
First Author: Uchida T
Year: 2017
Journal: Dalton Trans
Title: Reaction intermediates in the heme degradation reaction by HutZ from Vibrio cholerae.
Volume: 46
Issue: 25
Pages: 8104-8109
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Protein Domain
IPR014419 | HutZ
Type: Family
Description: Members of this family are heme utilization proteins, typically designated HutZ. They are members of the PPOX family () and, except for the lack of an N-terminal extension, are closely related to one form of heme oxidase []. Members typically are found in a three-gene operon with radical SAM enzyme HutW and a protein of unknown function, HutX. In Vibrio cholerae, HugZ is involved in heme degradation [, , , ].
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Publication
21030596 | -
First Author: Hu Y
Year: 2011
Journal: J Biol Chem
Title: Crystal structure of HugZ, a novel heme oxygenase from Helicobacter pylori.
Volume: 286
Issue: 2
Pages: 1537-44
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Protein Domain
IPR037119 | Haem_oxidase_HugZ-like_sf
Type: Homologous_superfamily
Description: This entry represents a domain superfamily that can be found in a group of putative haem-iron utilisation proteins, such as HugZ, a class of heme oxygenase that belongs to the PPOX family and lacks homology to the HmuO family. This enzyme releases iron during the conversion of heme to biliverdin [, ]. This domain can also be found at the C terminus of the glutamyl-tRNA reductase-binding (GluTRBP) protein from Arabidopsis []. GluTRBP is involved in the regulation of glutamyl-tRNA reductase (GluTR) which is important for the synthesis and distribution of 5-aminolevulinate, a precursor in heme and chlorophyll biosynthesis []. GluTRBP is necessary for efficient photosynthetic electron transport in chloroplasts [, ].
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Publication
22180625 | -
First Author: Czarnecki O
Year: 2011
Journal: Plant Cell
Title: An Arabidopsis GluTR binding protein mediates spatial separation of 5-aminolevulinic acid synthesis in chloroplasts.
Volume: 23
Issue: 12
Pages: 4476-91
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Publication
20657737 | -
First Author: Jung HS
Year: 2010
Journal: PLoS One
Title: Arabidopsis thaliana PGR7 encodes a conserved chloroplast protein that is necessary for efficient photosynthetic electron transport.
Volume: 5
Issue: 7
Pages: e11688
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Publication
24753615 | -
First Author: Zhao A
Year: 2014
Journal: Proc Natl Acad Sci U S A
Title: Crystal structure of Arabidopsis glutamyl-tRNA reductase in complex with its stimulator protein.
Volume: 111
Issue: 18
Pages: 6630-5
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