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A8HZX8 (PYRD_AZOC5) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. 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 (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:AZC_4640
OrganismAzorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / ORS 571) [Complete proteome] [HAMAP]
Taxonomic identifier438753 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Xanthobacteraceae › Azorhizobium

Protein attributes

Sequence length356 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 MF_00225

Catalytic activity

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

Cofactor

Binds 1 FMN per subunit By similarity. HAMAP MF_00225

Pathway

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

Subunit structure

Monomer By similarity. HAMAP MF_00225

Subcellular location

Cell membrane; Peripheral membrane protein By similarity HAMAP 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' pyrimidine base biosynthetic process

Inferred from electronic annotation. Source: InterPro

UMP 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 – 356356Dihydroorotate dehydrogenase (quinone) HAMAP MF_00225
PRO_1000071765

Regions

Nucleotide binding60 – 645FMN By similarity
Nucleotide binding317 – 3182FMN By similarity
Region109 – 1135Substrate binding By similarity
Region245 – 2462Substrate binding By similarity

Sites

Active site1741Nucleophile By similarity
Binding site641Substrate By similarity
Binding site841FMN; via amide nitrogen By similarity
Binding site1401FMN By similarity
Binding site1711FMN By similarity
Binding site1711Substrate By similarity
Binding site1761Substrate By similarity
Binding site2161FMN By similarity
Binding site2441FMN; via carbonyl oxygen By similarity
Binding site2671FMN; via amide nitrogen By similarity
Binding site2961FMN; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
A8HZX8 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: 291AF104984E9FA6

FASTA35637,501
        10         20         30         40         50         60 
MDLYPLVRPF LPLFTPEQAH GLSIRALKKG LVPADRSPAD PVLRTRVWNI DFPNPVGLAA 

        70         80         90        100        110        120 
GFDKDAEIID PLLSLGFGFV EAGSVTPRPQ PGNPKPRLFR LDEDEGVINR FGFNSQGLAP 

       130        140        150        160        170        180 
FIYQLGKRKA AGLPGIVGAN VGKNKETEDA SEDYVAGVSA TCRLADYIVC NVSSPNTPGL 

       190        200        210        220        230        240 
RLLQARTEMS ALIGAALSAR NDSLPDAATR PPLLVKVAPD LDDAGLEAVA EVTLELGVDG 

       250        260        270        280        290        300 
IIMGNTTISR PDSLRSRHKG ETGGLSGAPL FTLSTERLGA LYRLVRGRIP LVGAGGIASG 

       310        320        330        340        350 
ADAYAKIRAG ASLVQLYSAL VFHGPALVPR IKADLAARLK ADGFRSVADA VGADIR

« Hide

References

[1]"Complete genome sequence of the nitrogen-fixing bacterium Azorhizobium caulinodans ORS571."
Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T., Kaneko T., Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B., Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M., Oyaizu H.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43989 / DSM 5975 / ORS 571.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP009384 Genomic DNA. Translation: BAF90638.1.
RefSeqYP_001527556.1. NC_009937.1.

3D structure databases

ProteinModelPortalA8HZX8.
ModBaseSearch...

Protein-protein interaction databases

STRINGA8HZX8.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5687762.
GenomeReviewsGene locus AZC_4640 in contig AP009384_GR.
KEGGazc:AZC_4640.
PATRIC21026229. VBIAzoCau17976_4837.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG351027.
OMAAALNRMG.
ProtClustDBPRK05286.

Enzyme and pathway databases

BioCycACAU438753:AZC_4640-MONOMER.

Family and domain databases

HAMAPMF_00225. DHO_dh_type2.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR012135. Dihydroorotate_DH_1_2.
IPR005719. Dihydroorotate_DH_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.
TIGRFAMsTIGR01036. PyrD_sub2. 1 hit.
PROSITEPS00911. DHODEHASE_1. 1 hit.
PS00912. DHODEHASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRD_AZOC5
AccessionPrimary (citable) accession number: A8HZX8
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: December 4, 2007
Last modified: January 25, 2012
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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