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Protein

Deoxycytidine triphosphate deaminase

Gene

dcd

Organism
Campylobacter curvus (strain 525.92)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

dCTP + H2O = dUTP + NH3.UniRule annotation

Pathway: dUMP biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes dUMP from dCTP (dUTP route).UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Deoxycytidine triphosphate deaminase (dcd)
  2. no protein annotated in this organism
This subpathway is part of the pathway dUMP biosynthesis, which is itself part of Pyrimidine metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes dUMP from dCTP (dUTP route), the pathway dUMP biosynthesis and in Pyrimidine metabolism.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Nucleotide metabolism

Enzyme and pathway databases

BioCyciCCUR360105:GJ9P-1820-MONOMER.
UniPathwayiUPA00610; UER00665.

Names & Taxonomyi

Protein namesi
Recommended name:
Deoxycytidine triphosphate deaminaseUniRule annotation (EC:3.5.4.13UniRule annotation)
Short name:
dCTP deaminaseUniRule annotation
Gene namesi
Name:dcdUniRule annotation
Ordered Locus Names:Ccur92_16580
ORF Names:CCV52592_0559
OrganismiCampylobacter curvus (strain 525.92)
Taxonomic identifieri360105 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeCampylobacter
ProteomesiUP000006380 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 186186Deoxycytidine triphosphate deaminasePRO_1000009699Add
BLAST

Interactioni

Protein-protein interaction databases

STRINGi360105.CCV52592_0559.

Structurei

3D structure databases

ProteinModelPortaliA7H0H0.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the dCTP deaminase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0717.
HOGENOMiHOG000228600.
KOiK01494.
OMAiMEYFRIP.
OrthoDBiEOG67DPKR.

Family and domain databases

Gene3Di2.70.40.10. 1 hit.
HAMAPiMF_00146. dCTP_deaminase.
InterProiIPR011962. dCTP_deam.
IPR029054. dUTPase-like.
IPR008180. dUTPase/dCTP_deaminase.
[Graphical view]
PfamiPF00692. dUTPase. 1 hit.
[Graphical view]
SUPFAMiSSF51283. SSF51283. 1 hit.
TIGRFAMsiTIGR02274. dCTP_deam. 1 hit.

Sequencei

Sequence statusi: Complete.

A7H0H0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGLKSDAWIR KMSHEKAMIV PFAEEQVGRG VVSYGVSSYG YDIRVGDEFK
60 70 80 90 100
IFTNIGGTVV DPKNFDEKNV VDFKGDVCIV PPNSFALART IEYFNMPDNV
110 120 130 140 150
LAICLGKSTY ARCGIIVNVT PFEPGFKGHI TIEISNTTPL PAKIYANEGI
160 170 180
AQVLFIEGDE PCEVTYADKK GKYQAQEGIT LPRILK
Length:186
Mass (Da):20,520
Last modified:September 11, 2007 - v1
Checksum:i1E0156C61A49ABC9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000767 Genomic DNA. Translation: EAU01415.1.
RefSeqiWP_002948812.1. NC_009715.1.
YP_001408962.1. NC_009715.1.

Genome annotation databases

EnsemblBacteriaiEAU01415; EAU01415; CCV52592_0559.
KEGGiccv:CCV52592_0559.
PATRICi20033927. VBICamCur47627_1748.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000767 Genomic DNA. Translation: EAU01415.1.
RefSeqiWP_002948812.1. NC_009715.1.
YP_001408962.1. NC_009715.1.

3D structure databases

ProteinModelPortaliA7H0H0.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi360105.CCV52592_0559.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiEAU01415; EAU01415; CCV52592_0559.
KEGGiccv:CCV52592_0559.
PATRICi20033927. VBICamCur47627_1748.

Phylogenomic databases

eggNOGiCOG0717.
HOGENOMiHOG000228600.
KOiK01494.
OMAiMEYFRIP.
OrthoDBiEOG67DPKR.

Enzyme and pathway databases

UniPathwayiUPA00610; UER00665.
BioCyciCCUR360105:GJ9P-1820-MONOMER.

Family and domain databases

Gene3Di2.70.40.10. 1 hit.
HAMAPiMF_00146. dCTP_deaminase.
InterProiIPR011962. dCTP_deam.
IPR029054. dUTPase-like.
IPR008180. dUTPase/dCTP_deaminase.
[Graphical view]
PfamiPF00692. dUTPase. 1 hit.
[Graphical view]
SUPFAMiSSF51283. SSF51283. 1 hit.
TIGRFAMsiTIGR02274. dCTP_deam. 1 hit.
ProtoNetiSearch...

Publicationsi

  1. "Genome sequence of Campylobacter curvus 525.92 isolated from human feces."
    Fouts D.E., Mongodin E.F., Puiu D., Sebastian Y., Miller W.G., Mandrell R.E., Lastovica A.J., Nelson K.E.
    Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 525.92.

Entry informationi

Entry nameiDCD_CAMC5
AccessioniPrimary (citable) accession number: A7H0H0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: September 11, 2007
Last modified: May 27, 2015
This is version 46 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, Reference 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.