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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)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi135 – 1351D → N: Loss of activity. 1 Publication
Mutagenesisi145 – 1451E → Q: Loss of dCTP deaminase activity, but retains 25% dUTP pyrophosphatase activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 204204dCTP deaminase, dUMP-formingPRO_0000156029Add
BLAST

Interactioni

Subunit structurei

Homohexamer.

Protein-protein interaction databases

STRINGi243232.MJ_0430.

Structurei

Secondary structure

1
204
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi5 – 139Combined sources
Beta strandi16 – 216Combined sources
Helixi24 – 263Combined sources
Beta strandi32 – 365Combined sources
Beta strandi38 – 436Combined sources
Beta strandi45 – 473Combined sources
Beta strandi56 – 605Combined sources
Beta strandi62 – 687Combined sources
Helixi76 – 8611Combined sources
Beta strandi89 – 946Combined sources
Beta strandi96 – 10510Combined sources
Beta strandi110 – 1167Combined sources
Helixi118 – 1214Combined sources
Turni122 – 1243Combined sources
Beta strandi125 – 1273Combined sources
Beta strandi139 – 15113Combined sources
Beta strandi153 – 1564Combined sources
Beta strandi160 – 1689Combined sources
Beta strandi176 – 1805Combined sources
Helixi196 – 1983Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-182.
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.

Genome annotation databases

EnsemblBacteriaiAAB98415; AAB98415; MJ_0430.
KEGGimja:MJ_0430.

Cross-referencesi

Sequence databases

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 1-182.
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.
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: September 7, 2016
This is version 126 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.