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Q0AFI1 (PYRC_NITEC) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Dihydroorotase

Short name=DHOase
EC=3.5.2.3
Gene names
Name:pyrC
Ordered Locus Names:Neut_1659
OrganismNitrosomonas eutropha (strain C91) [Complete proteome] [HAMAP]
Taxonomic identifier335283 [NCBI]
Taxonomic lineageBacteriaProteobacteriaBetaproteobacteriaNitrosomonadalesNitrosomonadaceaeNitrosomonas

Protein attributes

Sequence length345 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Catalytic activity

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

Cofactor

Binds 2 zinc ions per subunit By similarity. HAMAP-Rule MF_00219

Pathway

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

Subunit structure

Homodimer By similarity. HAMAP-Rule 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_process'de novo' UMP biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-UniPathway

pyrimidine nucleobase biosynthetic process

Inferred from electronic annotation. Source: InterPro

   Molecular_functiondihydroorotase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 345345Dihydroorotase HAMAP-Rule MF_00219
PRO_1000024025

Sites

Metal binding141Zinc 1 By similarity
Metal binding161Zinc 1 By similarity
Metal binding1021Zinc 1; via carbamate group By similarity
Metal binding1021Zinc 2; via carbamate group By similarity
Metal binding1391Zinc 2 By similarity
Metal binding1771Zinc 2 By similarity
Metal binding2501Zinc 1 By similarity

Amino acid modifications

Modified residue1021N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0AFI1 [UniParc].

Last modified October 17, 2006. Version 1.
Checksum: 0AD34C94361246F8

FASTA34538,476
        10         20         30         40         50         60 
MTNKLTFTRP DDWHLHLRDG KAMQSVLPDT ARRFARAMIM PNLKLPVVTT EQAAAYRARI 

        70         80         90        100        110        120 
LSALPQELVG QFEPLMTLYL TDTTTPEEIS RAKASGIVQA VKLYPAGATT HSDAGVTDID 

       130        140        150        160        170        180 
RCKATLAMME KLDMPLLVHG EVVDPAVDIF DREKIFIDRV LIPLLQRFPG LRVVFEHITT 

       190        200        210        220        230        240 
REAVEFVQSI SNRIAATITA HHLMLNRNAL FTGGLQPHHY CLPVLKREIH RQALVAAATS 

       250        260        270        280        290        300 
GHSRFFLGTD SAPHPLKDKE SACGCAGIYS AHAAIEFYAE IFEQAGRLDR LEAFASFYGP 

       310        320        330        340 
DFYGLPRNTD QISLSKESWQ IPGEVEFGGD RLVPLRAGEQ VCWRL 

« Hide

References

[1]"Whole-genome analysis of the ammonia-oxidizing bacterium, Nitrosomonas eutropha C91: implications for niche adaptation."
Stein L.Y., Arp D.J., Berube P.M., Chain P.S., Hauser L., Jetten M.S., Klotz M.G., Larimer F.W., Norton J.M., Op den Camp H.J.M., Shin M., Wei X.
Environ. Microbiol. 9:2993-3007(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: C91.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000450 Genomic DNA. Translation: ABI59901.1.
RefSeqYP_747866.1. NC_008344.1.

3D structure databases

ProteinModelPortalQ0AFI1.
SMRQ0AFI1. Positions 2-345.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING335283.Neut_1659.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI59901; ABI59901; Neut_1659.
GeneID4273812.
KEGGnet:Neut_1659.
PATRIC22720754. VBINitEut7577_2030.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0418.
HOGENOMHOG000256259.
KOK01465.
OMAVAFEPLM.
OrthoDBEOG6TFCMH.

Enzyme and pathway databases

BioCycNEUT335283:GHT6-1692-MONOMER.
UniPathwayUPA00070; UER00117.

Family and domain databases

HAMAPMF_00219. PyrC_type1.
InterProIPR006680. Amidohydro_1.
IPR004721. DHOdimr.
IPR002195. Dihydroorotase_CS.
[Graphical view]
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_NITEC
AccessionPrimary (citable) accession number: Q0AFI1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: October 17, 2006
Last modified: May 14, 2014
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways