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Protein

dCTP deaminase, dUMP-forming

Gene

dcd

Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes two consecutive reactions to form dUMP using dCTP as substrate.

Catalytic activityi

dCTP + 2 H2O = dUMP + diphosphate + NH3.

Cofactori

Enzyme regulationi

Inhibited by dTTP.

pH dependencei

Optimum pH is 7.5.

Temperature dependencei

Retains over 70% of its activity after heating at 90 degrees Celsius for 10 min.

Pathwayi: dUMP biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes dUMP from dCTP.
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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Nucleotide metabolism

Keywords - Ligandi

Magnesium

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-17894.
BRENDAi3.5.4.13. 3260.
3.5.4.30. 3260.
3.6.1.23. 3260.
SABIO-RKQ57872.
UniPathwayiUPA00610; UER00667.

Protein family/group databases

MoonProtiQ57872.

Names & Taxonomyi

Protein namesi
Recommended name:
dCTP deaminase, dUMP-forming (EC:3.5.4.30)
Alternative name(s):
Bifunctional deaminase/diphosphatase
MjDCD-DUT
Short name:
DCD/DUT
Gene namesi
Name:dcd
Ordered Locus Names:MJ0430
OrganismiMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Taxonomic identifieri243232 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus
Proteomesi
  • UP000000805 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi135D → N: Loss of activity. 1 Publication1
Mutagenesisi145E → Q: Loss of dCTP deaminase activity, but retains 25% dUTP pyrophosphatase activity. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001560291 – 204dCTP deaminase, dUMP-formingAdd BLAST204

Interactioni

Subunit structurei

Homohexamer.

Protein-protein interaction databases

STRINGi243232.MJ_0430.

Structurei

Secondary structure

1204
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
Beta strandi45 – 47Combined sources3
Beta strandi56 – 60Combined sources5
Beta strandi62 – 68Combined sources7
Helixi76 – 86Combined sources11
Beta strandi89 – 94Combined sources6
Beta strandi96 – 105Combined sources10
Beta strandi110 – 116Combined sources7
Helixi118 – 121Combined sources4
Turni122 – 124Combined sources3
Beta strandi125 – 127Combined sources3
Beta strandi139 – 151Combined sources13
Beta strandi153 – 156Combined sources4
Beta strandi160 – 168Combined sources9
Beta strandi176 – 180Combined sources5
Helixi196 – 198Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OGHX-ray1.88A/B1-204[»]
1PKHX-ray1.42A/B1-204[»]
1PKJX-ray2.10A/B1-204[»]
1PKKX-ray1.77A/B1-204[»]
2HXBX-ray2.55A1-204[»]
2HXDX-ray2.30A1-204[»]
3GF0X-ray2.62A1-204[»]
ProteinModelPortaliQ57872.
SMRiQ57872.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ57872.

Family & Domainsi

Sequence similaritiesi

Belongs to the dCTP deaminase family.Curated

Phylogenomic databases

eggNOGiarCOG04048. Archaea.
COG0717. LUCA.
InParanoidiQ57872.
KOiK09887.
OMAiGWIDAGF.
PhylomeDBiQ57872.

Family and domain databases

CDDicd07557. trimeric_dUTPase. 1 hit.
Gene3Di2.70.40.10. 1 hit.
HAMAPiMF_00146. dCTP_deaminase. 1 hit.
InterProiIPR011962. dCTP_deam.
IPR029054. dUTPase-like.
IPR008180. dUTPase/dCTP_deaminase.
IPR033704. dUTPase_trimeric.
[Graphical view]
PfamiPF00692. dUTPase. 1 hit.
[Graphical view]
SUPFAMiSSF51283. SSF51283. 1 hit.
TIGRFAMsiTIGR02274. dCTP_deam. 1 hit.

Sequencei

Sequence statusi: Complete.

Q57872-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MILSDKDIID YVTSKRIIIK PFNKDFVGPC SYDVTLGDEF IIYDDEVYDL
60 70 80 90 100
SKELNYKRIK IKNSILVCPL NYNLTEEKIN YFKEKYNVDY VVEGGVLGTT
110 120 130 140 150
NEYIELPNDI SAQYQGRSSL GRVFLTSHQT AGWIDAGFKG KITLEIVAFD
160 170 180 190 200
KPVILYKNQR IGQLIFSKLL SPADVGYSER KTSKYAYQKS VMPSLIHLDN

HKKD
Length:204
Mass (Da):23,432
Last modified:November 1, 1996 - v1
Checksum:i1218368057723371
GO

Mass spectrometryi

Molecular mass is 23619±94 Da from positions 1 - 204. Determined by MALDI. 1 Publication

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB98415.1.
PIRiF64353.
RefSeqiWP_010869929.1. NC_000909.1.

Genome annotation databases

EnsemblBacteriaiAAB98415; AAB98415; MJ_0430.
GeneIDi1451290.
KEGGimja:MJ_0430.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB98415.1.
PIRiF64353.
RefSeqiWP_010869929.1. NC_000909.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1OGHX-ray1.88A/B1-204[»]
1PKHX-ray1.42A/B1-204[»]
1PKJX-ray2.10A/B1-204[»]
1PKKX-ray1.77A/B1-204[»]
2HXBX-ray2.55A1-204[»]
2HXDX-ray2.30A1-204[»]
3GF0X-ray2.62A1-204[»]
ProteinModelPortaliQ57872.
SMRiQ57872.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243232.MJ_0430.

Protein family/group databases

MoonProtiQ57872.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB98415; AAB98415; MJ_0430.
GeneIDi1451290.
KEGGimja:MJ_0430.

Phylogenomic databases

eggNOGiarCOG04048. Archaea.
COG0717. LUCA.
InParanoidiQ57872.
KOiK09887.
OMAiGWIDAGF.
PhylomeDBiQ57872.

Enzyme and pathway databases

UniPathwayiUPA00610; UER00667.
BioCyciMetaCyc:MONOMER-17894.
BRENDAi3.5.4.13. 3260.
3.5.4.30. 3260.
3.6.1.23. 3260.
SABIO-RKQ57872.

Miscellaneous databases

EvolutionaryTraceiQ57872.

Family and domain databases

CDDicd07557. trimeric_dUTPase. 1 hit.
Gene3Di2.70.40.10. 1 hit.
HAMAPiMF_00146. dCTP_deaminase. 1 hit.
InterProiIPR011962. dCTP_deam.
IPR029054. dUTPase-like.
IPR008180. dUTPase/dCTP_deaminase.
IPR033704. dUTPase_trimeric.
[Graphical view]
PfamiPF00692. dUTPase. 1 hit.
[Graphical view]
SUPFAMiSSF51283. SSF51283. 1 hit.
TIGRFAMsiTIGR02274. dCTP_deam. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiDCD_METJA
AccessioniPrimary (citable) accession number: Q57872
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: November 2, 2016
This is version 128 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Methanococcus jannaschii
    Methanococcus jannaschii: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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 one 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.