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Reviewed, UniProtKB/Swiss-Prot Q3AC01 (PYRC_CARHZ)

Last modified November 3, 2009. Version 26. 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:
    Dihydroorotase
      Short name=DHOase
    EC=3.5.2.3
Gene names
Name: pyrC
Ordered Locus Names: CHY_1501
OrganismCarboxydothermus hydrogenoformans (strain Z-2901 / DSM 6008) [Complete proteome] [HAMAP]
Taxonomic identifier246194 [NCBI]
Taxonomic lineageBacteriaFirmicutesClostridiaThermoanaerobacteralesThermoanaerobacteriaceaeCarboxydothermus

Protein attributes

Sequence length430 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Catalytic activity

(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate. HAMAP MF_00220

Cofactor

Binds 2 zinc ions per subunit By similarity.

Pathway

Pyrimidine metabolism; UMP biosynthesis via de novo pathway; (S)-dihydroorotate from bicarbonate: step 3/3. HAMAP MF_00220

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the DHOase family. Type 2 subfamily.

Ontologies

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

Inferred from electronic annotation. Source: HAMAP

   Molecular functiondihydroorotase activity

Inferred from electronic annotation. Source: HAMAP

zinc ion binding

Inferred from electronic annotation. Source: HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 430430Dihydroorotase HAMAP MF_00220
PRO_1000024079

Sites

Metal binding601Zinc 1 By similarity
Metal binding621Zinc 1 By similarity
Metal binding1411Zinc 1; via carbamate group By similarity
Metal binding1411Zinc 2; via carbamate group By similarity
Metal binding1781Zinc 2 By similarity
Metal binding2311Zinc 2 By similarity
Metal binding3041Zinc 1 By similarity

Amino acid modifications

Modified residue1411N6-carboxylysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3AC01-1 [UniParc].

Last modified November 22, 2005. Version 1.
Checksum: 0CA0F06BA9EB2890

FASTA43047,093
        10         20         30         40         50         60 
MGMLIKNGNV VMVEDGKIRK MDVLIDKGII VEISPEINRS DVEVIDIEGK FLIPGLIDMH 

        70         80         90        100        110        120 
VHFRDPGYTH KEDIHSGSNA ALAGGFTGVL MMPNTDPPPD NATVIYYWKE KSKSIPLNIL 

       130        140        150        160        170        180 
FSGCITKNRA GKELSKFYEL KEAGAVAITD DGNWVADGAV FRHAMEYAAA LDLLVITHPE 

       190        200        210        220        230        240 
EPTIANRGVI NEGYWSTVLG LRGIPKAAEN IAIYRDIEIA KMTGAKLHVA HLSTAEGVRL 

       250        260        270        280        290        300 
VAAAKKLGLK VTAEVTPHHL VLTDEALAGY DTNLKVNPPL REAEEQKALL KGLLEGVIDV 

       310        320        330        340        350        360 
IATDHAPHAS YEKNVEFNDA PFGIEGLETA FPVLYTELVL KKKITLEKLL LKMTVNPAKI 

       370        380        390        400        410        420 
LQLPKQGDIK KGNYANLTVI DPKLTLKVSE ELLVGKSKNN PFLGRTLTGW PVMTVYQGIV 

       430 
AYQRLLKGVQ 

« Hide

References

[1]"Life in hot carbon monoxide: the complete genome sequence of Carboxydothermus hydrogenoformans Z-2901."
Wu M., Ren Q., Durkin A.S., Daugherty S.C., Brinkac L.M., Dodson R.J., Madupu R., Sullivan S.A., Kolonay J.F., Nelson W.C., Tallon L.J., Jones K.M., Ulrich L.E., Gonzalez J.M., Zhulin I.B., Robb F.T., Eisen J.A.
PLoS Genet. 1:563-574(2005) [PubMed: 16311624] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000141 Genomic DNA. Translation: ABB14270.1.
RefSeqYP_360333.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ3AC01.

Genome annotation databases

GeneID3728542.
GenomeReviewsGene locus CHY_1501 in contig CP000141_GR.
KEGGchy:CHY_1501.
NMPDRfig|246194.3.peg.61.
TIGRCHY_1501.

Phylogenomic databases

HOGENOMQ3AC01.
OMAGIFAEKE.

Enzyme and pathway databases

BioCycCHYD246194:CHY_1501-MON.

Family and domain databases

HAMAPMF_00220.
[Tree]
InterProIPR006680. Amidohydro_1.
IPR004722. DHOmult.
IPR002195. Dihydroorotase_CS.
[Graphical view]
PfamPF01979. Amidohydro_1. 1 hit.
[Graphical view]
TIGRFAMsTIGR00857. pyrC_multi. 1 hit.
PROSITEPS00482. DIHYDROOROTASE_1. 1 hit.
PS00483. DIHYDROOROTASE_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePYRC_CARHZ
AccessionPrimary (citable) accession number: Q3AC01
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 22, 2005
Last modified: November 3, 2009
This is version 26 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