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Protein

Deoxycytidine triphosphate deaminase

Gene

dcd

Organism
Rickettsia rickettsii (strain Sheila Smith)
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. Deoxyuridine 5'-triphosphate nucleotidohydrolase (dut)
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

BioCyciRRIC392021:GIY1-114-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:A1G_00610
OrganismiRickettsia rickettsii (strain Sheila Smith)
Taxonomic identifieri392021 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaAlphaproteobacteriaRickettsialesRickettsiaceaeRickettsieaeRickettsiaspotted fever group

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 188188Deoxycytidine triphosphate deaminasePRO_1000009802Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliA8GQN3.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the dCTP deaminase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0717.
HOGENOMiHOG000228600.
KOiK01494.
OMAiEAGWEGH.
OrthoDBiEOG67DPKR.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

A8GQN3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAIMSDKWIK EAVINHSMIR PFAEKQVRVH NKEKIISYGL SSYGYDARVS
60 70 80 90 100
NEFKIFTNIN STTVDPKNFS EYNLVDREVD VCIIPPNSFA LGRTIEYFKI
110 120 130 140 150
PRDVLVICVG KSTYARCGII VNVTPLEPEW EGHVTLEFSN TTPLPAKIYA
160 170 180
NEGACQFLFL KSDQICDTSY ADRQGKYMKQ VGVTLPLT
Length:188
Mass (Da):21,328
Last modified:November 13, 2007 - v1
Checksum:i34EF8EBA5D3A9257
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000848 Genomic DNA. Translation: ABV75708.1.
RefSeqiWP_004996797.1. NC_009882.1.
YP_001494216.1. NC_009882.1.

Genome annotation databases

EnsemblBacteriaiABV75708; ABV75708; A1G_00610.
GeneIDi928095.
KEGGirri:A1G_00610.
PATRICi17902915. VBIRicRic5337_0129.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000848 Genomic DNA. Translation: ABV75708.1.
RefSeqiWP_004996797.1. NC_009882.1.
YP_001494216.1. NC_009882.1.

3D structure databases

ProteinModelPortaliA8GQN3.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABV75708; ABV75708; A1G_00610.
GeneIDi928095.
KEGGirri:A1G_00610.
PATRICi17902915. VBIRicRic5337_0129.

Phylogenomic databases

eggNOGiCOG0717.
HOGENOMiHOG000228600.
KOiK01494.
OMAiEAGWEGH.
OrthoDBiEOG67DPKR.

Enzyme and pathway databases

UniPathwayiUPA00610; UER00665.
BioCyciRRIC392021:GIY1-114-MONOMER.

Family and domain databases

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

Publicationsi

  1. "Complete genome sequence of Rickettsia rickettsii."
    Madan A., Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., Dasch G., Eremeeva M.
    Submitted (SEP-2007) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Sheila Smith.

Entry informationi

Entry nameiDCD_RICRS
AccessioniPrimary (citable) accession number: A8GQN3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: November 13, 2007
Last modified: June 24, 2015
This is version 45 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.