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B9IVW1 (PYRDB_BACCQ) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Dihydroorotate dehydrogenase B (NAD(+)), catalytic subunit
Short name=DHOD B
Short name=DHODase B
Short name=DHOdehase B
EC=1.3.1.14
Alternative name(s):
Dihydroorotate oxidase B
Orotate reductase (NADH)
Gene names
Name:pyrD
Ordered Locus Names:BCQ_3670
OrganismBacillus cereus (strain Q1) [Complete proteome] [HAMAP]
Taxonomic identifier361100 [NCBI]
Taxonomic lineageBacteria › Firmicutes › Bacilli › Bacillales › Bacillaceae › Bacillus › Bacillus cereus group ›

Protein attributes

Sequence length309 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of dihydroorotate to orotate with NAD+ as electron acceptor By similarity. HAMAP-Rule MF_00224

Catalytic activity

(S)-dihydroorotate + NAD+ = orotate + NADH. HAMAP-Rule MF_00224

Cofactor

Binds 1 FMN per subunit By similarity.

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (NAD(+) route): step 1/1. HAMAP-Rule MF_00224

Subunit structure

Heterotetramer of 2 PyrK and 2 PyrD type B subunits By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the dihydroorotate dehydrogenase family. Type 1 subfamily.

Ontologies

Keywords
   Biological processPyrimidine biosynthesis
   Cellular componentCytoplasm
   LigandFMN
Flavoprotein
NAD
   Molecular functionOxidoreductase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_process'de novo' UMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

'de novo' pyrimidine nucleobase biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiondihydroorotate oxidase activity

Inferred from electronic annotation. Source: InterPro

orotate reductase (NADH) activity

Inferred from electronic annotation. Source: EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 309309Dihydroorotate dehydrogenase B (NAD(+)), catalytic subunit HAMAP-Rule MF_00224
PRO_1000195046

Regions

Nucleotide binding45 – 462FMN By similarity
Nucleotide binding243 – 2442FMN By similarity
Nucleotide binding265 – 2662FMN By similarity
Region69 – 735Substrate binding By similarity
Region192 – 1932Substrate binding By similarity

Sites

Active site1301Nucleophile
Binding site211FMN By similarity
Binding site451Substrate By similarity
Binding site991FMN By similarity
Binding site1271FMN By similarity
Binding site1271Substrate By similarity
Binding site1651FMN By similarity
Binding site1911FMN; via carbonyl oxygen By similarity
Binding site2171FMN; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
B9IVW1 [UniParc].

Last modified March 24, 2009. Version 1.
Checksum: 70E308F9028EAA27

FASTA30932,990
        10         20         30         40         50         60 
MNRLQVELPG LSLKNPIIPA SGCFGFGREY AQFYDLSVLG SIMIKATTEQ PRYGNPTPRV 

        70         80         90        100        110        120 
AETPGGMLNA IGLQNPGLEK VMNSELPWLE QFDLPIIANV AGSQAEDYVA VAKEISKAPN 

       130        140        150        160        170        180 
VHALELNISC PNVKTGGIAF GTNPEIAADL TKRVKEVSEV PVYVKLSPNV ANIVEIAKAI 

       190        200        210        220        230        240 
ENAGADGLTM INTLLGMRLD LKTAKPILAN RTGGLSGPAI KPVAIRMVHE VSQAVNIPII 

       250        260        270        280        290        300 
GMGGIETAED VIEFFYAGAS AVAVGTANFI DPFVCPTIIE ELPALLDELG FDHISECQGR 


SWKQTCHSR

« Hide

References

[1]"Complete genome sequence of the extremophilic Bacillus cereus strain Q1 with industrial applications."
Xiong Z., Jiang Y., Qi D., Lu H., Yang F., Yang J., Chen L., Sun L., Xu X., Xue Y., Zhu Y., Jin Q.
J. Bacteriol. 191:1120-1121(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Q1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000227 Genomic DNA. Translation: ACM14098.1.
RefSeqYP_002531387.1. NC_011969.1.

3D structure databases

ProteinModelPortalB9IVW1.
SMRB9IVW1. Positions 2-288.
ModBaseSearch...

Protein-protein interaction databases

STRING361100.BCQ_3670.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACM14098; ACM14098; BCQ_3670.
GeneID7375864.
KEGGbcq:BCQ_3670.
PATRIC18915064. VBIBacCer120424_3700.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0167.
HOGENOMHOG000225105.
KOK00226.
OMAKATTANP.
ProtClustDBPRK07259.

Enzyme and pathway databases

BioCycBCER361100:GJ7M-3658-MONOMER.
UniPathwayUPA00070; UER00945.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00224. DHO_dh_type1.
InterProIPR013785. Aldolase_TIM.
IPR005720. Dihydroorotate_DH.
IPR024920. Dihydroorotate_DH_1.
IPR012135. Dihydroorotate_DH_1_2.
IPR001295. Dihydroorotate_DH_CS.
[Graphical view]
PfamPF01180. DHO_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000164. DHO_oxidase. 1 hit.
TIGRFAMsTIGR01037. pyrD_sub1_fam. 1 hit.
PROSITEPS00911. DHODEHASE_1. 1 hit.
PS00912. DHODEHASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRDB_BACCQ
AccessionPrimary (citable) accession number: B9IVW1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 24, 2009
Last modified: May 1, 2013
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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