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Q9V0Y6 (PYRDB_PYRAB) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 90. 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:PYRAB06530
ORF Names:PAB1936
OrganismPyrococcus abyssi (strain GE5 / Orsay) [Complete proteome] [HAMAP]
Taxonomic identifier272844 [NCBI]
Taxonomic lineageArchaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus

Protein attributes

Sequence length303 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 – 303303Dihydroorotate dehydrogenase B (NAD(+)), catalytic subunit HAMAP MF_00224
PRO_0000148412

Regions

Nucleotide binding47 – 482FMN By similarity
Nucleotide binding241 – 2422FMN By similarity
Nucleotide binding263 – 2642FMN By similarity
Region71 – 755Substrate binding By similarity
Region190 – 1912Substrate binding By similarity

Sites

Active site1281Nucleophile
Binding site231FMN By similarity
Binding site471Substrate By similarity
Binding site1251FMN By similarity
Binding site1251Substrate By similarity
Binding site1631FMN By similarity
Binding site1891FMN; via carbonyl oxygen By similarity
Binding site2151FMN; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9V0Y6 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 2C28CBB50E2D9F32

FASTA30332,619
        10         20         30         40         50         60 
MVRGMLEVNL FGIKFKNPLI LASGVVDMTP ELLRRAHREG AGGVVTKSIG MEPRKGYENP 

        70         80         90        100        110        120 
TIVELPYGLI NAMGLPNPGW EAFLEEFRKE KFDFPVIVSI FGGTPEEFAF LAEKLGEVAD 

       130        140        150        160        170        180 
AFELNLSCPH AKGYGMEIGQ KPENVYEVVK AVKDVTDKPV IAKLTPNVSD IRELGLAAEK 

       190        200        210        220        230        240 
AGADGVSAIN TVKAIAIDIY AKRPILSNKF GGYSGPGVKP IALRAVYDLA SSLDIPVIGI 

       250        260        270        280        290        300 
GGITTWQDAV EFLLAGASAL QIGTAVYLRG FSVFREIAEG ISRYLKEEGY SSVKEIIGLA 


LKV

« Hide

References

[1]"An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi."
Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O., Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P.
Mol. Microbiol. 47:1495-1512(2003) [PubMed: 12622808] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GE5 / Orsay.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AJ248285 Genomic DNA. Translation: CAB49566.1.
PIRE75106.
RefSeqNP_126335.1. NC_000868.1.

3D structure databases

ProteinModelPortalQ9V0Y6.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBPYRT00000002872; EBPYRP00000002803; EBPYRG00000002872.
GeneID1495551.
GenomeReviewsGene locus PYRAB06530 in contig AL096836_GR.
KEGGpab:PAB1936.
NMPDRfig|272844.1.peg.675.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000023023.
HOGENOMHBG472415.
OMAHAKGYGM.
PhylomeDBQ9V0Y6.
ProtClustDBPRK07259.

Enzyme and pathway databases

BioCycPABY272844:PAB1936-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_PYRAB
AccessionPrimary (citable) accession number: Q9V0Y6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: May 1, 2000
Last modified: January 25, 2012
This is version 90 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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