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Reviewed, UniProtKB/Swiss-Prot Q8A9C3 (PYRD_BACTN)

Last modified November 25, 2008. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Dihydroorotate dehydrogenase
    EC=1.3.3.1
Alternative name(s):
    Dihydroorotate oxidase
    DHOdehase
      Short name=DHODase
      Short name=DHOD
Gene names
Name: pyrD
Ordered Locus Names: BT_0892
OrganismBacteroides thetaiotaomicron [Complete proteome] [HAMAP]
Taxonomic identifier818 [NCBI]
Taxonomic lineageBacteriaBacteroidetesBacteroidiaBacteroidalesBacteroidaceaeBacteroides

Protein attributes

Sequence length303 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

(S)-dihydroorotate + O(2) = orotate + H(2)O(2).

Cofactor

Binds 1 FMN per subunit By similarity.

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; UMP from HCO(3)(-): step 4/6.

Subunit structure

Heterotetramer of 2 pyrK and 2 pyrD subunits By similarity.

Subcellular location

CytoplasmBy similarity.

Sequence similarities

Belongs to the dihydroorotate dehydrogenase family. Type 1 subfamily.

Ontologies

Keywords

   Biological processPyrimidine biosynthesis
   Cellular componentCytoplasm
   LigandFMN
Flavoprotein
   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

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentcytoplasm

Inferred from electronic annotation. Source: HAMAP

   Molecular functiondihydroorotate oxidase activity

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 303303Dihydroorotate dehydrogenase
PRO_1000024131

Sites

Active site1301Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8A9C3-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: B51FAAF443050485

FASTA30332,296
        10         20         30         40         50         60 
MADLSVNIGE LQMKNPVMTA SGTFGYGEEF SDFIDIARIG GIIVKGTTLH KREGNPYPRM 

        70         80         90        100        110        120 
AETPSGMLNA VGLQNKGVDY FVEQIYPRIK DIQTNMIVNV SGSAIEDYVK TAEIINELDK 

       130        140        150        160        170        180 
IPAIELNISC PNVKQGGMAF GVSAKGASEV VKAVRAAYKK TLIVKLSPNV TDITEIARAA 

       190        200        210        220        230        240 
EESGADSVSL INTLLGMAID AERKRPILST VTGGMSGAAV KPIALRMVWQ VAKAVNIPVI 

       250        260        270        280        290        300 
GLGGIMNWKD AVEFMLAGAS AIQIGTANFI DPAVTIKVED GINNYLERHG CKSVKEIIGA 


LEV 

« Hide

References

[1]"A genomic view of the human-Bacteroides thetaiotaomicron symbiosis."
Xu J., Bjursell M.K., Himrod J., Deng S., Carmichael L.K., Chiang H.C., Hooper L.V., Gordon J.I.
Science 299:2074-2076(2003) [PubMed: 12663928] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 29148 / DSM 2079 / NCTC 10582 / E50 / VPI-5482.

Cross-references

Sequence databases

AE015928 Genomic DNA. Translation: AAO75999.1.
RefSeqNP_809805.1.

3D structure databases

HSSPHSSP built from PDB template 1EP2 based on UniProtKB P54322.
ModBaseSearch...

Genome annotation databases

GeneID1074664.
GenomeReviewsGene locus BT_0892 in contig AE015928_GR.
KEGGbth:BT_0892.
NMPDRfig|226186.1.peg.892.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ8A9C3.

Enzyme and pathway databases

BioCycBTHE226186:BT_0892-MON.

Family and domain databases

HAMAPMF_00224.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR012135. DHO_DHase_1_2.
IPR005720. DHO_DHase_1_core.
IPR001295. Dihydroorotate_DHase_core.
[Graphical view]
Gene3DG3DSA:3.20.20.70. Aldolase_TIM. 1 hit.
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 namePYRD_BACTN
AccessionPrimary (citable) accession number: Q8A9C3
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: June 1, 2003
Last modified: November 25, 2008
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents