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B6ELD1 (PYRD_ALISL) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 27. 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:VSAL_I1549
OrganismAliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain LFI1238)) [Complete proteome] [HAMAP]
Taxonomic identifier316275 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Vibrionales › Vibrionaceae › Aliivibrio

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 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 – 336336Dihydroorotate dehydrogenase (quinone) HAMAP MF_00225
PRO_1000100246

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
B6ELD1 [UniParc].

Last modified November 25, 2008. Version 1.
Checksum: 694D639C70E2E863

FASTA33637,026
        10         20         30         40         50         60 
MLYRIARAGI FKLDAEKAHD LAIQNFKRFN GTPLDIFYRQ KLVSKPVEVM GIQFKNPIGL 

        70         80         90        100        110        120 
AAGLEKNGEC IEAFGAMGFG FIEVGTVTPR PQAGNDKPRL FRLIEAEGII NRMGFNNLGV 

       130        140        150        160        170        180 
DNLVENVKKA KYDGVIGINI GKNKDTPIEK GTEDYLICME KVYQYAGYIA INISSPNTPG 

       190        200        210        220        230        240 
LRTLQYGEAL DDLLSQLKEK QKELAEKYGK YVPIALKIAP DLDDNELSQI ADSLMKYKID 

       250        260        270        280        290        300 
GVIATNTTLD RSMVEGMKHA EEMGGLSGRP IQTRSTEVVR RLKELLGDSL PIIGVGGVDS 

       310        320        330 
YVAAKEKMVA GADLVQVYSG FIYKGPNLIR DIVNNI

« Hide

References

[1]"The complete genome sequence of the fish pathogen Aliivibrio salmonicida strain LFI1238."
Hjerde E., Lorentzen M.S., Holden M.T.G., Seeger K., Paulsen S., Bason N., Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S., Thurston S., Parkhill J., Willassen N.-P., Thomson N.R.
Submitted (JUN-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: LFI1238.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		FM178379 Genomic DNA. Translation: CAQ79234.1.
RefSeqYP_002262981.1. NC_011312.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGB6ELD1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID6988588.
GenomeReviewsGene locus VSAL_I1549 in contig FM178379_GR.
KEGGvsa:VSAL_I1549.
PATRIC20853384. VBIAliSal95923_1713.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG351027.
OMASYVTVNI.
ProtClustDBPRK05286.

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_ALISL
AccessionPrimary (citable) accession number: B6ELD1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 24, 2009
Last sequence update: November 25, 2008
Last modified: January 25, 2012
This is version 27 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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