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Protein

Dihydroorotase

Gene

pyrC

Organism
Synechococcus sp. (strain CC9902)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

(S)-dihydroorotate + H2O = N-carbamoyl-L-aspartate.UniRule annotation

Cofactori

Zn2+UniRule annotationNote: Binds 2 Zn2+ ions per subunit.UniRule annotation

Pathway:iUMP biosynthesis via de novo pathway

This protein is involved in step 3 of the subpathway that synthesizes (S)-dihydroorotate from bicarbonate.UniRule annotation
Proteins known to be involved in the 3 steps of the subpathway in this organism are:
  1. Carbamoyl-phosphate synthase (glutamine-hydrolyzing) (Syncc9902_0836), Carbamoyl-phosphate synthase small chain (carA)
  2. Aspartate carbamoyltransferase (pyrB)
  3. Dihydroorotase (pyrC)
This subpathway is part of the pathway UMP biosynthesis via de novo pathway, which is itself part of Pyrimidine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes (S)-dihydroorotate from bicarbonate, the pathway UMP biosynthesis via de novo pathway and in Pyrimidine metabolism.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi14 – 141Zinc 1; via tele nitrogenUniRule annotation
Metal bindingi16 – 161Zinc 1; via tele nitrogenUniRule annotation
Metal bindingi100 – 1001Zinc 1; via carbamate groupUniRule annotation
Metal bindingi100 – 1001Zinc 2; via carbamate groupUniRule annotation
Metal bindingi137 – 1371Zinc 2; via pros nitrogenUniRule annotation
Metal bindingi175 – 1751Zinc 2; via tele nitrogenUniRule annotation
Metal bindingi248 – 2481Zinc 1UniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Pyrimidine biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciSSP316279:GJCI-903-MONOMER.
UniPathwayiUPA00070; UER00117.

Names & Taxonomyi

Protein namesi
Recommended name:
DihydroorotaseUniRule annotation (EC:3.5.2.3UniRule annotation)
Short name:
DHOaseUniRule annotation
Gene namesi
Name:pyrCUniRule annotation
Ordered Locus Names:Syncc9902_0892
OrganismiSynechococcus sp. (strain CC9902)
Taxonomic identifieri316279 [NCBI]
Taxonomic lineageiBacteriaCyanobacteriaOscillatoriophycideaeChroococcalesSynechococcus
ProteomesiUP000002712 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 343343DihydroorotasePRO_1000024069Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei100 – 1001N6-carboxylysineUniRule annotation

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi316279.Syncc9902_0892.

Structurei

3D structure databases

ProteinModelPortaliQ3AYG9.
SMRiQ3AYG9. Positions 2-340.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the DHOase family. Type 1 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0418.
HOGENOMiHOG000256259.
KOiK01465.
OMAiYAEAFEQ.
OrthoDBiEOG6TFCMH.

Family and domain databases

HAMAPiMF_00219. PyrC_type1.
InterProiIPR006680. Amidohydro_1.
IPR004721. DHOdimr.
IPR002195. Dihydroorotase_CS.
[Graphical view]
PANTHERiPTHR11647:SF59. PTHR11647:SF59. 1 hit.
PfamiPF01979. Amidohydro_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001237. DHOdimr. 1 hit.
TIGRFAMsiTIGR00856. pyrC_dimer. 1 hit.
PROSITEiPS00482. DIHYDROOROTASE_1. 1 hit.
PS00483. DIHYDROOROTASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q3AYG9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSDQIQLIAP DDWHVHLRDG EMLKQVVPYT AQMFRRAIVM PNLRPPVVTV
60 70 80 90 100
EAAKAYRDQI VAACHPNWGF TPLMTAYLTD DIAPEEIERG FHEGVFTAAK
110 120 130 140 150
LYPANATTNS AAGVTELRHI HGVLLVMERI GMPLLIHGEV TDVDVDVFDR
160 170 180 190 200
EAVFIERSLK PIRDRYPGLK VVLEHITTEQ AVDFVGSADQ NLAATITPHH
210 220 230 240 250
LHINRNAMFA GGLRSDFYCL PVAKRERHRL ALRRAAMSGD RRFFLGTDSA
260 270 280 290 300
PHARPGKESS CGCAGIFNAP HALESYAMAF AQDDKLDKLE AFASLHGPAF
310 320 330 340
YGLPVNEGIV TLQRDDKLVP NVVNGLVPFH AGETLPWRLQ PCT
Length:343
Mass (Da):38,057
Last modified:November 22, 2005 - v1
Checksum:i8479D756696FD2CE
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000097 Genomic DNA. Translation: ABB25858.1.
RefSeqiWP_011359695.1. NC_007513.1.

Genome annotation databases

EnsemblBacteriaiABB25858; ABB25858; Syncc9902_0892.
KEGGisye:Syncc9902_0892.
PATRICi23799033. VBISynSp76179_0979.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000097 Genomic DNA. Translation: ABB25858.1.
RefSeqiWP_011359695.1. NC_007513.1.

3D structure databases

ProteinModelPortaliQ3AYG9.
SMRiQ3AYG9. Positions 2-340.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi316279.Syncc9902_0892.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABB25858; ABB25858; Syncc9902_0892.
KEGGisye:Syncc9902_0892.
PATRICi23799033. VBISynSp76179_0979.

Phylogenomic databases

eggNOGiCOG0418.
HOGENOMiHOG000256259.
KOiK01465.
OMAiYAEAFEQ.
OrthoDBiEOG6TFCMH.

Enzyme and pathway databases

UniPathwayiUPA00070; UER00117.
BioCyciSSP316279:GJCI-903-MONOMER.

Family and domain databases

HAMAPiMF_00219. PyrC_type1.
InterProiIPR006680. Amidohydro_1.
IPR004721. DHOdimr.
IPR002195. Dihydroorotase_CS.
[Graphical view]
PANTHERiPTHR11647:SF59. PTHR11647:SF59. 1 hit.
PfamiPF01979. Amidohydro_1. 1 hit.
[Graphical view]
PIRSFiPIRSF001237. DHOdimr. 1 hit.
TIGRFAMsiTIGR00856. pyrC_dimer. 1 hit.
PROSITEiPS00482. DIHYDROOROTASE_1. 1 hit.
PS00483. DIHYDROOROTASE_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Complete sequence of Synechococcus sp. CC9902."
    Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Martinez M., Schmutz J., Larimer F., Land M., Kyrpides N., Ivanova N., Richardson P.
    Submitted (AUG-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: CC9902.

Entry informationi

Entry nameiPYRC_SYNS9
AccessioniPrimary (citable) accession number: Q3AYG9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 22, 2005
Last modified: July 22, 2015
This is version 61 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.