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Protein

dCTP deaminase, dUMP-forming

Gene

dcd

Organism
Mycobacterium bovis (strain BCG / Tokyo 172 / ATCC 35737 / TMC 1019)
Status
Reviewed-Annotation score: -Protein inferred from homologyi

Functioni

Bifunctional enzyme that catalyzes both the deamination of dCTP to dUTP and the hydrolysis of dUTP to dUMP without releasing the toxic dUTP intermediate.UniRule annotation

Catalytic activityi

dCTP + 2 H2O = dUMP + diphosphate + NH3.UniRule annotation

Pathwayi: dUMP biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes dUMP from dCTP.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. dCTP deaminase, dUMP-forming (dcd)
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, the pathway dUMP biosynthesis and in Pyrimidine metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sitei116 – 117Important for bifunctional activityUniRule annotation2
Binding sitei119dCTPUniRule annotation1
Active sitei129Proton donor/acceptorUniRule annotation1
Binding sitei148dCTPUniRule annotation1
Binding sitei162dCTPUniRule annotation1
Binding sitei170dCTPUniRule annotation1
Binding sitei174dCTPUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi101 – 106dCTP bindingUniRule annotation6
Nucleotide bindingi127 – 129dCTP bindingUniRule annotation3

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase
Biological processNucleotide metabolism
LigandNucleotide-binding

Enzyme and pathway databases

UniPathwayiUPA00610; UER00667

Names & Taxonomyi

Protein namesi
Recommended name:
dCTP deaminase, dUMP-formingUniRule annotation (EC:3.5.4.30UniRule annotation)
Alternative name(s):
Bifunctional dCTP deaminase:dUTPaseUniRule annotation
DCD-DUTUniRule annotation
Gene namesi
Name:dcdUniRule annotation
Ordered Locus Names:JTY_0331
OrganismiMycobacterium bovis (strain BCG / Tokyo 172 / ATCC 35737 / TMC 1019)
Taxonomic identifieri561275 [NCBI]
Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesMycobacteriaceaeMycobacteriumMycobacterium tuberculosis complex

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10001231521 – 190dCTP deaminase, dUMP-formingAdd BLAST190

Interactioni

Subunit structurei

Homotrimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliC1AJZ9
SMRiC1AJZ9
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the dCTP deaminase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000228601
KOiK01494
OMAiGQLCLFR

Family and domain databases

CDDicd07557 trimeric_dUTPase, 1 hit
Gene3Di2.70.40.10, 1 hit
HAMAPiMF_00146 dCTP_deaminase, 1 hit
InterProiView protein in InterPro
IPR011962 dCTP_deaminase
IPR029054 dUTPase-like
IPR036157 dUTPase-like_sf
IPR033704 dUTPase_trimeric
PfamiView protein in Pfam
PF00692 dUTPase, 1 hit
SUPFAMiSSF51283 SSF51283, 1 hit
TIGRFAMsiTIGR02274 dCTP_deam, 1 hit

Sequencei

Sequence statusi: Complete.

C1AJZ9-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLLSDRDLRA EISSGRLGID PFDDTLVQPS SIDVRLDCLF RVFNNTRYTH
60 70 80 90 100
IDPAKQQDEL TSLVQPVDGE PFVLHPGEFV LGSTLELFTL PDNLAGRLEG
110 120 130 140 150
KSSLGRLGLL THSTAGFIDP GFSGHITLEL SNVANLPITL WPGMKIGQLC
160 170 180 190
MLRLTSPSEH PYGSSRAGSK YQGQRGPTPS RSCQNFIRST
Length:190
Mass (Da):20,810
Last modified:May 26, 2009 - v1
Checksum:i7609329810B64794
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AP010918 Genomic DNA Translation: BAH24628.1
RefSeqiWP_003401638.1, NZ_CP014566.1

Genome annotation databases

EnsemblBacteriaiBAH24628; BAH24628; JTY_0331
KEGGimbt:JTY_0331

Similar proteinsi

Entry informationi

Entry nameiDCDB_MYCBT
AccessioniPrimary (citable) accession number: C1AJZ9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: May 26, 2009
Last modified: April 25, 2018
This is version 56 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health