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Reviewed, UniProtKB/Swiss-Prot Q1LT62 (PYRD_BAUCH)

Last modified November 25, 2008. Version 25. 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: BCI_0409
OrganismBaumannia cicadellinicola subsp. Homalodisca coagulata [Complete proteome] [HAMAP]
Taxonomic identifier374463 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaCandidatus Baumannia

Protein attributes

Sequence length336 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

Homodimer By similarity.

Subcellular location

Cell membrane; Peripheral membrane proteinBy similarity.

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

oxidation reduction

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular componentplasma membrane

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 – 336336Dihydroorotate dehydrogenase
PRO_1000024153

Sites

Active site1751Nucleophile By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1LT62-1 [UniParc].

Last modified May 30, 2006. Version 1.
Checksum: B00B0E763B82D580

FASTA33636,873
        10         20         30         40         50         60 
MLYPLIRQFL FQLDPEKAHE LTIQQLKRIA GTPLEYLVRQ SVPTKAVTCM GIAFKNPLGL 

        70         80         90        100        110        120 
AAGLDKNGEC IDALGAMGFG FIEVGTVTPH AQIGNEKPRL FRLTKAYGLI NRMGFNNKGV 

       130        140        150        160        170        180 
DNLVNNIQKS HFGGVLGINI GKNKDTPIEQ GKDDYLICME KVYPYANYIA VNISSPNTPQ 

       190        200        210        220        230        240 
LTTLQSGEIL DDLLRAIKDK QAKLQEYHHK YVPIAVKITP DMTESELIQM ADLLVQHKID 

       250        260        270        280        290        300 
GIIATNTTTS RELVHGLDHS SQSGGLSGRP LQLMSTEVIR ILSSKLQGKL PIIGVGGIDS 

       310        320        330 
LISAREKMAA GATLIQIYSS FIFHGPRLIK DIISDL 

« Hide

References

[1]"Metabolic complementarity and genomics of the dual bacterial symbiosis of sharpshooters."
Wu D., Daugherty S.C., Van Aken S.E., Pai G.H., Watkins K.L., Khouri H., Tallon L.J., Zaborsky J.M., Dunbar H.E., Tran P.L., Moran N.A., Eisen J.A.
PLoS Biol. 4:1079-1092(2006) [PubMed: 16729848] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000238 Genomic DNA. Translation: ABF14134.1.
RefSeqYP_588852.1.

3D structure databases

SMRQ1LT62. Positions 1-336.
ModBaseSearch...

Genome annotation databases

GeneID4056320.
GenomeReviewsGene locus BCI_0409 in contig CP000238_GR.
KEGGbci:BCI_0409.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ1LT62.

Family and domain databases

HAMAPMF_00225.
[Tree]
InterProIPR013785. Aldolase_TIM.
IPR012135. DHO_DHase_1_2.
IPR005719. DHO_DHase_2.
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.
TIGRFAMsTIGR01036. pyrD_sub2. 1 hit.
PROSITEPS00911. DHODEHASE_1. 1 hit.
PS00912. DHODEHASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRD_BAUCH
AccessionPrimary (citable) accession number: Q1LT62
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 30, 2006
Last modified: November 25, 2008
This is version 25 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