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A4SME2 (PYRD_AERS4) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 51. 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 (quinone)
EC=1.3.5.2
Alternative name(s):
DHOdehase
Short name=DHOD
Short name=DHODase
Dihydroorotate oxidase
Gene names
Name:pyrD
Ordered Locus Names:ASA_1993
OrganismAeromonas salmonicida (strain A449) [Complete proteome] [HAMAP]
Taxonomic identifier382245 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Aeromonadales › Aeromonadaceae › Aeromonas ›

Protein attributes

Sequence length336 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of dihydroorotate to orotate with quinone as electron acceptor By similarity. HAMAP-Rule MF_00225

Catalytic activity

(S)-dihydroorotate + a quinone = orotate + a quinol. HAMAP-Rule MF_00225

Cofactor

Binds 1 FMN per subunit By similarity.

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; orotate from (S)-dihydroorotate (quinone route): step 1/1. HAMAP-Rule MF_00225

Subunit structure

Monomer By similarity.

Subcellular location

Cell membrane; Peripheral membrane protein By similarity HAMAP-Rule MF_00225.

Sequence similarities

Belongs to the dihydroorotate dehydrogenase family. Type 2 subfamily.

Ontologies

Keywords
   Biological processPyrimidine biosynthesis
   Cellular componentCell membrane
Membrane
   LigandFMN
Flavoprotein
   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_componentplasma membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functiondihydroorotate oxidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 336336Dihydroorotate dehydrogenase (quinone) HAMAP-Rule MF_00225
PRO_1000024148

Regions

Nucleotide binding62 – 665FMN By similarity
Nucleotide binding318 – 3192FMN By similarity
Region111 – 1155Substrate binding By similarity
Region246 – 2472Substrate binding By similarity

Sites

Active site1751Nucleophile By similarity
Binding site661Substrate By similarity
Binding site861FMN; via amide nitrogen By similarity
Binding site1391FMN By similarity
Binding site1721FMN By similarity
Binding site1721Substrate By similarity
Binding site1771Substrate By similarity
Binding site2171FMN By similarity
Binding site2451FMN; via carbonyl oxygen By similarity
Binding site2681FMN; via amide nitrogen By similarity
Binding site2971FMN; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
A4SME2 [UniParc].

Last modified May 15, 2007. Version 1.
Checksum: EC003C32D9230911

FASTA33636,411
        10         20         30         40         50         60 
MLYPLARHFL FKFNPEQAHD LSIKYLPRLL GTPLDCFFRH SLPKRPVTVM GLYFANPVGL 

        70         80         90        100        110        120 
AAGLDKDGEC IDAFGAMGFG FIEVGTVTPK PQSGNDKPRL FRVIPAEGII NRMGFNNKGV 

       130        140        150        160        170        180 
DHLVAQVKKA KYQGVIGINI GKNKDTPIEQ GKDDYLICMD KVYDHAGYIA VNISSPNTPG 

       190        200        210        220        230        240 
LRSLQYGDAL DELLAALKVR QQELAAQYKK YVPLAVKIAP DLSLDEINQV AASLIKNGID 

       250        260        270        280        290        300 
GVIATNTTLD REMIYDMPHA GEAGGLSGRP LQHKSTEVIR QLAKALDGAL PIIGVGGIDS 

       310        320        330 
AMAAREKLAA GASLVQIYSG FIYKGPSLVK EIVTHI

« Hide

References

[1]"The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into the evolution of a fish pathogen."
Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J., Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C., Brown L.L.
BMC Genomics 9:427-427(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: A449.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000644 Genomic DNA. Translation: ABO90064.1.
RefSeqYP_001141812.1. NC_009348.1.

3D structure databases

ProteinModelPortalA4SME2.
SMRA4SME2. Positions 1-336.
ModBaseSearch...

Protein-protein interaction databases

STRING382245.ASA_1993.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABO90064; ABO90064; ASA_1993.
GeneID4996284.
KEGGasa:ASA_1993.
PATRIC20790364. VBIAerSal2987_1978.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0167.
HOGENOMHOG000225103.
KOK00226.
OMAALNRMGF.
ProtClustDBPRK05286.

Enzyme and pathway databases

BioCycASAL382245:GJJN-1984-MONOMER.
UniPathwayUPA00070; UER00946.

Family and domain databases

Gene3D3.20.20.70. 1 hit.
HAMAPMF_00225. DHO_dh_type2.
InterProIPR013785. Aldolase_TIM.
IPR012135. Dihydroorotate_DH_1_2.
IPR005719. Dihydroorotate_DH_2.
IPR001295. Dihydroorotate_DH_CS.
[Graphical view]
PfamPF01180. DHO_dh. 1 hit.
[Graphical view]
PIRSFPIRSF000164. DHO_oxidase. 1 hit.
TIGRFAMsTIGR01036. pyrD_sub2. 1 hit.
PROSITEPS00911. DHODEHASE_1. 1 hit.
PS00912. DHODEHASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRD_AERS4
AccessionPrimary (citable) accession number: A4SME2
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 15, 2007
Last modified: May 1, 2013
This is version 51 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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