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Protein

dCTP deaminase, dUMP-forming

Gene

dcd

Organism
Leptospira borgpetersenii serovar Hardjo-bovis (strain L550)
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
Sitei108 – 109Important for bifunctional activityUniRule annotation2
Binding sitei111dCTPUniRule annotation1
Active sitei121Proton donor/acceptorUniRule annotation1
Binding sitei138dCTPUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi93 – 98dCTP bindingUniRule annotation6
Nucleotide bindingi119 – 121dCTP 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:LBL_3016
OrganismiLeptospira borgpetersenii serovar Hardjo-bovis (strain L550)
Taxonomic identifieri355276 [NCBI]
Taxonomic lineageiBacteriaSpirochaetesLeptospiralesLeptospiraceaeLeptospira

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10001179781 – 173dCTP deaminase, dUMP-formingAdd BLAST173

Interactioni

Subunit structurei

Homotrimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliQ04X69
SMRiQ04X69
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the dCTP deaminase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4107S9R Bacteria
COG0717 LUCA
HOGENOMiHOG000228601
KOiK01494
OMAiGWIDAGF
OrthoDBiPOG091H021I

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
IPR036157 dUTPase-like_sf
IPR033704 dUTPase_trimeric
SUPFAMiSSF51283 SSF51283, 1 hit
TIGRFAMsiTIGR02274 dCTP_deam, 1 hit

Sequencei

Sequence statusi: Complete.

Q04X69-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MILTGKEIQK RIGKDIIITP YSEKQLNPNS YNLRLHEELL IYTELPLDMK
60 70 80 90 100
KPNLTKKQII PESGLLLKPG ILYLGRTLEF TETHHLVPML EGRSSIGRLG
110 120 130 140 150
MLVHVTAGFG DVGFKGFWTL EISVIQPLIV YPGVEVCQIF YHTLEGQITE
160 170
YTSGKYQANQ GIQPSMLYQD FEK
Length:173
Mass (Da):19,695
Last modified:November 14, 2006 - v1
Checksum:i5B8427DA0A80D4C2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000348 Genomic DNA Translation: ABJ80326.1
RefSeqiWP_011671221.1, NC_008508.1

Genome annotation databases

EnsemblBacteriaiABJ80326; ABJ80326; LBL_3016
GeneIDi4405966
KEGGilbl:LBL_3016

Similar proteinsi

Entry informationi

Entry nameiDCDB_LEPBL
AccessioniPrimary (citable) accession number: Q04X69
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: November 14, 2006
Last modified: April 25, 2018
This is version 70 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