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A7GRK9 (PYRDB_BACCN) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 42. 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):
Dihydrdoorotate oxidase B
Orotate reductase (NADH)
Gene names
Name:pyrD
Ordered Locus Names:Bcer98_2533
OrganismBacillus cereus subsp. cytotoxis (strain NVH 391-98) [Complete proteome] [HAMAP]
Taxonomic identifier315749 [NCBI]
Taxonomic lineageBacteria › Firmicutes › 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 MF_00224

Catalytic activity

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

Cofactor

Binds 1 FMN per subunit By similarity. HAMAP MF_00224

Pathway

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

Subunit structure

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

Subcellular location

Cytoplasm By similarity HAMAP MF_00224.

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' pyrimidine base biosynthetic process

Inferred from electronic annotation. Source: InterPro

UMP 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 MF_00224
PRO_1000078152

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
A7GRK9 [UniParc].

Last modified September 11, 2007. Version 1.
Checksum: 8BB2E789FFF10419

FASTA30932,931
        10         20         30         40         50         60 
MNRLQVELPG LSLKNPIIPA SGCFGFGREY AQFYDLNVLG SIMIKATTEQ PRYGNPTPRV 

        70         80         90        100        110        120 
AETPGGMLNA IGLQNPGLEK VMGSELPWLE QFDLPIIANV AGSQVEDYVA VAKKISKAPN 

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

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

       250        260        270        280        290        300 
GMGGIESAED VIEFFYAGAS AVAVGTANFV DPLVCPTIIE ELPSLLDELG FGHISECQGR 


SWKQVCQSR

« Hide

References

[1]"Extending the Bacillus cereus group genomics to putative food-borne pathogens of different toxicity."
Lapidus A., Goltsman E., Auger S., Galleron N., Segurens B., Dossat C., Land M.L., Broussolle V., Brillard J., Guinebretiere M.-H., Sanchis V., Nguen-the C., Lereclus D., Richardson P., Wincker P., Weissenbach J., Ehrlich S.D., Sorokin A.
Chem. Biol. Interact. 171:236-249(2008) [PubMed: 17434157] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: NVH 391-98.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000764 Genomic DNA. Translation: ABS22767.1.
RefSeqYP_001375762.1. NC_009674.1.

3D structure databases

ProteinModelPortalA7GRK9.
SMRA7GRK9. Positions 2-288.
ModBaseSearch...

Protein-protein interaction databases

STRINGA7GRK9.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBACT00000037183; EBBACP00000036234; EBBACG00000037174.
GeneID5343666.
GenomeReviewsGene locus Bcer98_2533 in contig CP000764_GR.
KEGGbcy:Bcer98_2533.
PATRIC18933664. VBIBacCyt128034_2676.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0167.
GeneTreeEBGT00050000001544.
HOGENOMHBG472415.
OMAVALRMVW.
ProtClustDBPRK07259.

Enzyme and pathway databases

BioCycBCER315749:BCER98_2533-MONOMER.

Family and domain databases

HAMAPMF_00224. DHO_dh_type1.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR005720. Dihydroorotate_DH.
IPR024920. Dihydroorotate_DH_1.
IPR012135. Dihydroorotate_DH_1_2.
IPR001295. Dihydroorotate_DH_CS.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
KOK00226.
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_BACCN
AccessionPrimary (citable) accession number: A7GRK9
Entry history
Integrated into UniProtKB/Swiss-Prot: May 20, 2008
Last sequence update: September 11, 2007
Last modified: January 25, 2012
This is version 42 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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