HAMAP rule MF_01211
General rule information
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Accession | MF_01211 |
Dates | 17-JUN-2002 (Created)
19-NOV-2022 (Last updated, Version 46) |
Name | DHODB_Fe_S_bind |
Scope(s) |
Bacteria Archaea |
Template(s) | P56968 (PYRK_LACLM); P25983 (PYRK_BACSU); P0DH76 (PYRK_ENTFA); [ Recover all ] |
Triggered by |
HAMAP; MF_01211 (Get profile general information and statistics) |
Propagated annotation
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Identifier, protein and gene names
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Identifier | PYRK |
case <OC:Bacteria> | |
Protein name | RecName: Full=Dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit; AltName: Full=Dihydroorotate oxidase B, electron transfer subunit; |
end case | |
case <OC:Archaea> | |
Protein name | RecName: Full=Probable dihydroorotate dehydrogenase B (NAD(+)), electron transfer subunit; AltName: Full=Dihydroorotate oxidase B, electron transfer subunit; |
end case | |
Gene name | Name=pyrK; |
Comments
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FUNCTION | Responsible for channeling the electrons from the oxidation of dihydroorotate from the FMN redox center in the PyrD type B subunit to the ultimate electron acceptor NAD(+). |
COFACTOR | Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135; Note=Binds 1 [2Fe-2S] cluster per subunit.; |
COFACTOR | Name=FAD; Xref=ChEBI:CHEBI:57692; Note=Binds 1 FAD per subunit.; |
PATHWAY | Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1. |
SUBUNIT | Heterotetramer of 2 PyrK and 2 PyrD type B subunits. |
SIMILARITY | Belongs to the PyrK family. |
Keywords
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Pyrimidine biosynthesis |
Transport |
Electron transport |
Metal-binding |
Iron |
Iron-sulfur |
2Fe-2S |
Flavoprotein |
FAD |
Gene Ontology
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GO:0009055; Molecular function:electron transfer activity |
GO:0006221; Biological process:pyrimidine nucleotide biosynthetic process |
Cross-references
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Pfam | PF10418; DHODB_Fe-S_bind; 1; |
Pfam | PF00970; FAD_binding_6; 1; |
Pfam | PF00175; NAD_binding_1; 1; |
PIRSF | PIRSF006816; Cyc3_hyd_g; 1; |
PRINTS | PR00409; PHDIOXRDTASE; 1; |
PROSITE | PS00197; 2FE2S_FER_1; 0-1; |
PROSITE | PS51384; FAD_FR; 1; |
Features
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From: PYRK_LACLM (P56968) | ||||||||||||
Key | From | To | Description | Tag | Condition | FTGroup | ||||||
case <OC:Bacteria> | ||||||||||||
BINDING | 53 | 56 | /ligand="FAD" /ligand_id="ChEBI:CHEBI:57692" |
R-P-x-S | ||||||||
BINDING | 70 | 72 | /ligand="FAD" /ligand_id="ChEBI:CHEBI:57692" |
[LIV]-x-[RQ] | ||||||||
BINDING | 79 | 80 | /ligand="FAD" /ligand_id="ChEBI:CHEBI:57692" |
G-T | ||||||||
end case | ||||||||||||
BINDING | 226 | 226 | /ligand="[2Fe-2S] cluster" /ligand_id="ChEBI:CHEBI:190135" |
C | ||||||||
BINDING | 231 | 231 | /ligand="[2Fe-2S] cluster" /ligand_id="ChEBI:CHEBI:190135" |
C | ||||||||
BINDING | 234 | 234 | /ligand="[2Fe-2S] cluster" /ligand_id="ChEBI:CHEBI:190135" |
C | ||||||||
BINDING | 249 | 249 | /ligand="[2Fe-2S] cluster" /ligand_id="ChEBI:CHEBI:190135" |
C |
Additional information
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Size range | 232-266 amino acids |
Related rules |
None |
Fusion | Nter: None Cter: None |
Comments | Divergent THEMA and THEP1, annotated as "atypical" since they are quite divergent from the family profile, but can be thought to be PyrK proteins as the gene is adjacent to pyrD. |