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Protein

dCTP deaminase, dUMP-forming

Gene

dcd

Organism
Bacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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 annotation1 Publication

Catalytic activityi

dCTP + 2 H2O = dUMP + diphosphate + NH3.UniRule annotation1 Publication

Cofactori

Mg2+1 Publication

Enzyme regulationi

Inhibited by dTTP.1 Publication

Pathwayi: dUMP biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes dUMP from dCTP.UniRule annotationCurated
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
Binding sitei110dCTP1 Publication1
Sitei112 – 113Important for bifunctional activityUniRule annotation2
Active sitei125Proton donor/acceptorUniRule annotationBy similarity1
Binding sitei144dCTPUniRule annotation1 Publication1
Binding sitei164dCTPUniRule annotation1 Publication1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi98 – 103dCTP bindingUniRule annotation1 Publication6
Nucleotide bindingi115 – 118dCTP binding1 Publication4
Nucleotide bindingi123 – 125dCTP bindingUniRule annotation1 Publication3
Nucleotide bindingi157 – 160dCTP binding1 Publication4

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase
Biological processNucleotide metabolism
LigandMagnesium, Nucleotide-binding

Enzyme and pathway databases

BioCyciBHAL272558:G1G3A-421-MONOMER
UniPathwayiUPA00610; UER00667

Names & Taxonomyi

Protein namesi
Recommended name:
dCTP deaminase, dUMP-formingUniRule annotationCurated (EC:3.5.4.30UniRule annotation1 Publication)
Alternative name(s):
Bifunctional dCTP deaminase:dUTPaseUniRule annotation
DCD-DUTUniRule annotation
Gene namesi
Name:dcdUniRule annotation
Synonyms:dcdB1 Publication
Ordered Locus Names:BH0368
OrganismiBacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
Taxonomic identifieri272558 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001258 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001559641 – 177dCTP deaminase, dUMP-formingAdd BLAST177

Expressioni

Inductioni

Repressed by both deoxycytidine and thymidine.1 Publication

Interactioni

Subunit structurei

Homotrimer.UniRule annotation1 Publication

Protein-protein interaction databases

STRINGi272558.BH0368

Structurei

Secondary structure

1177
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 13Combined sources9
Beta strandi16 – 21Combined sources6
Helixi24 – 26Combined sources3
Beta strandi32 – 36Combined sources5
Beta strandi38 – 43Combined sources6
Turni45 – 47Combined sources3
Beta strandi49 – 51Combined sources3
Beta strandi53 – 55Combined sources3
Beta strandi59 – 63Combined sources5
Beta strandi66 – 71Combined sources6
Beta strandi76 – 86Combined sources11
Beta strandi91 – 97Combined sources7
Helixi99 – 102Combined sources4
Turni103 – 105Combined sources3
Beta strandi106 – 108Combined sources3
Beta strandi112 – 114Combined sources3
Beta strandi119 – 128Combined sources10
Beta strandi130 – 132Combined sources3
Beta strandi134 – 137Combined sources4
Beta strandi140 – 152Combined sources13
Turni160 – 163Combined sources4
Helixi172 – 174Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4XJCX-ray2.35A/B/C/D/E/F1-177[»]
ProteinModelPortaliQ9KFV3
SMRiQ9KFV3
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the dCTP deaminase family.UniRule annotation

Phylogenomic databases

eggNOGiENOG4105DHP Bacteria
COG0717 LUCA
KOiK01494
OMAiGQLCLFR
OrthoDBiPOG091H02A6

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.

Q9KFV3-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MILSGKTISE KLTEKELEIT PLTEEQIQPA SVDLRLGPHF VTIDDSKEAV
60 70 80 90 100
ISFERPIRYR EWTTSDETIV LPPHTFLLAT TMETVKLPNH LTAFVEGRSS
110 120 130 140 150
VGRLGLFIQN AGWVDPGFNG QITLELFNAN RLPIELPIGR RICQLVFAEV
160 170
TGEVAPYQGK YLFQKGATMS EIYKDAF
Length:177
Mass (Da):19,897
Last modified:October 1, 2000 - v1
Checksum:iD15AE75387847E2B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000004 Genomic DNA Translation: BAB04087.1
PIRiH83695
RefSeqiWP_010896547.1, NC_002570.2

Genome annotation databases

EnsemblBacteriaiBAB04087; BAB04087; BAB04087
KEGGibha:BH0368

Similar proteinsi

Entry informationi

Entry nameiDCDB_BACHD
AccessioniPrimary (citable) accession number: Q9KFV3
Entry historyiIntegrated into UniProtKB/Swiss-Prot: January 10, 2003
Last sequence update: October 1, 2000
Last modified: May 23, 2018
This is version 97 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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