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Q5QWC6 (PYRC_IDILO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 42. 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:
Dihydroorotase
Short name=DHOase
EC=3.5.2.3
Gene names
Name:pyrC
Ordered Locus Names:IL0362
OrganismIdiomarina loihiensis (strain ATCC BAA-735 / DSM 15497 / L2-TR) [Complete proteome] [HAMAP]
Taxonomic identifier283942 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Alteromonadales › Idiomarinaceae › Idiomarina

Protein attributes

Sequence length344 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate. HAMAP MF_00219

Cofactor

Binds 2 zinc ions per subunit By similarity. HAMAP MF_00219

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. HAMAP MF_00219

Subunit structure

Homodimer By similarity. HAMAP MF_00219

Sequence similarities

Belongs to the DHOase family. Type 1 subfamily.

Ontologies

Keywords
   Biological processPyrimidine biosynthesis
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processpyrimidine base biosynthetic process

Inferred from electronic annotation. Source: InterPro

pyrimidine nucleotide biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functiondihydroorotase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 344344Dihydroorotase HAMAP MF_00219
PRO_1000024018

Sites

Metal binding131Zinc 1 By similarity
Metal binding151Zinc 1 By similarity
Metal binding991Zinc 1; via carbamate group By similarity
Metal binding991Zinc 2; via carbamate group By similarity
Metal binding1361Zinc 2 By similarity
Metal binding1741Zinc 2 By similarity
Metal binding2471Zinc 1 By similarity

Amino acid modifications

Modified residue991N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5QWC6 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: 0524427E85F4BD41

FASTA34437,656
        10         20         30         40         50         60 
MQSLTIPRPD DWHLHLRDGA MLQTTVPATA AVFHRAVVMP NLVPPVTTVA AAMEYRERIL 

        70         80         90        100        110        120 
AEIPAGMSFN PLMALYLTAD TTPAEIAEAA ANEHVIGFKL YPSGATTNSA AGVKSVEALA 

       130        140        150        160        170        180 
PVLAAMQEHQ VPLLVHGEVT DSDIDIFDRE RVFIERHLIP ITERFPQLKL VLEHITTADA 

       190        200        210        220        230        240 
VKFVENANSN VAATMTPQHL LMNRNDLLVG GIRPHNYCLP ILKRRSHQQA LQQAALSGNP 

       250        260        270        280        290        300 
KFFLGTDSAP HVQANKETAC GCAGCYSAPA AIELYAEFFS QHNALDKLAN FASVFGADFY 

       310        320        330        340 
QLPRNTETIE LVQQPWTVAE TVDTATGPMV PYWAGSDLQW KLRG

« Hide

References

[1]"Genome sequence of the deep-sea gamma-proteobacterium Idiomarina loihiensis reveals amino acid fermentation as a source of carbon and energy."
Hou S., Saw J.H., Lee K.S., Freitas T.A., Belisle C., Kawarabayasi Y., Donachie S.P., Pikina A., Galperin M.Y., Koonin E.V., Makarova K.S., Omelchenko M.V., Sorokin A., Wolf Y.I., Li Q.X., Keum Y.S., Campbell S., Denery J. expand/collapse author list , Aizawa S., Shibata S., Malahoff A., Alam M.
Proc. Natl. Acad. Sci. U.S.A. 101:18036-18041(2004) [PubMed: 15596722] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-735 / DSM 15497 / L2-TR.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE017340 Genomic DNA. Translation: AAV81205.1.
RefSeqYP_154754.1. NC_006512.1.

3D structure databases

HSSPHSSP built from PDB template 1J79 based on UniProtKB P05020.
ProteinModelPortalQ5QWC6.
SMRQ5QWC6. Positions 2-343.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3172502.
GenomeReviewsGene locus IL0362 in contig AE017340_GR.
KEGGilo:IL0362.
NMPDRfig|283942.3.peg.446.
PATRIC22138745. VBIIdiLoi21852_0364.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG628648.
OMACLPVAKR.
ProtClustDBPRK05451.

Enzyme and pathway databases

BioCycILOI283942:IL0362-MONOMER.

Family and domain databases

HAMAPMF_00219. PyrC_type1.
[Tree]
InterProIPR006680. Amidohydro_1.
IPR004721. DHOdimr.
IPR002195. Dihydroorotase_CS.
[Graphical view]
KOK01465.
PfamPF01979. Amidohydro_1. 1 hit.
[Graphical view]
PIRSFPIRSF001237. DHOdimr. 1 hit.
TIGRFAMsTIGR00856. PyrC_dimer. 1 hit.
PROSITEPS00482. DIHYDROOROTASE_1. 1 hit.
PS00483. DIHYDROOROTASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRC_IDILO
AccessionPrimary (citable) accession number: Q5QWC6
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: January 4, 2005
Last modified: January 25, 2012
This is version 42 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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