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Protein

Probable dCTP deaminase

Gene

dcd

Organism
Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Status
Reviewed-Annotation score: Annotation score: 2 out of 5-Protein inferred from homologyi

Functioni

Catalytic activityi

dCTP + H2O = dUTP + NH3.UniRule annotation

Pathwayi: dUMP biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes dUMP from dCTP (dUTP route).UniRule annotation
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Probable dCTP deaminase (dcd)
  2. Probable deoxyuridine 5'-triphosphate nucleotidohydrolase (dut)
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 (dUTP route), 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

Enzyme and pathway databases

UniPathwayiUPA00610; UER00665.

Names & Taxonomyi

Protein namesi
Recommended name:
Probable dCTP deaminaseUniRule annotation (EC:3.5.4.13UniRule annotation)
Alternative name(s):
Deoxycytidine triphosphate deaminaseUniRule annotation
Gene namesi
Name:dcdUniRule annotation
Ordered Locus Names:MTH_1847
OrganismiMethanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum)
Taxonomic identifieri187420 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter
Proteomesi
  • UP000005223 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001560321 – 197Probable dCTP deaminaseAdd BLAST197

Interactioni

Protein-protein interaction databases

STRINGi187420.MTH1847.

Structurei

3D structure databases

ProteinModelPortaliO27875.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the dCTP deaminase family.UniRule annotation

Phylogenomic databases

eggNOGiarCOG04048. Archaea.
COG0717. LUCA.
KOiK01494.
OMAiNIPCIHP.

Family and domain databases

CDDicd07557. trimeric_dUTPase. 1 hit.
Gene3Di2.70.40.10. 1 hit.
HAMAPiMF_00146. dCTP_deaminase. 1 hit.
InterProiIPR011962. dCTP_deam.
IPR010550. dCTP_deam_bac.
IPR029054. dUTPase-like.
IPR008180. dUTPase/dCTP_deaminase.
IPR033704. dUTPase_trimeric.
[Graphical view]
PfamiPF06559. DCD. 1 hit.
PF00692. dUTPase. 1 hit.
[Graphical view]
SUPFAMiSSF51283. SSF51283. 1 hit.
TIGRFAMsiTIGR02274. dCTP_deam. 1 hit.

Sequencei

Sequence statusi: Complete.

O27875-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAILSDRDIK RYIEEGLITI DPLDDPERQI QPSSVDLRIG NEFKGFRVIR
60 70 80 90 100
KPCIDPKDPS DIESYMETFH VEDGPFIIHP GEFALATTHE YIALPEDLVA
110 120 130 140 150
RVEGRSSIGR LGITMHVTAG YIDPGFHGRI TLEISNIGKM PVALYPRQRV
160 170 180 190
CQIVFETMTS PAERPYGHPS RDSKYIGQTR PQTSRIKDDY EIRNSRL
Length:197
Mass (Da):22,427
Last modified:December 1, 2000 - v2
Checksum:i96A019F9DBA3528F
GO

Sequence cautioni

The sequence AAB86313 differs from that shown. Reason: Erroneous initiation.Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000666 Genomic DNA. Translation: AAB86313.1. Different initiation.
PIRiA69114.
RefSeqiWP_048061156.1. NC_000916.1.

Genome annotation databases

EnsemblBacteriaiAAB86313; AAB86313; MTH_1847.
GeneIDi1470932.
KEGGimth:MTH_1847.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE000666 Genomic DNA. Translation: AAB86313.1. Different initiation.
PIRiA69114.
RefSeqiWP_048061156.1. NC_000916.1.

3D structure databases

ProteinModelPortaliO27875.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi187420.MTH1847.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB86313; AAB86313; MTH_1847.
GeneIDi1470932.
KEGGimth:MTH_1847.

Phylogenomic databases

eggNOGiarCOG04048. Archaea.
COG0717. LUCA.
KOiK01494.
OMAiNIPCIHP.

Enzyme and pathway databases

UniPathwayiUPA00610; UER00665.

Family and domain databases

CDDicd07557. trimeric_dUTPase. 1 hit.
Gene3Di2.70.40.10. 1 hit.
HAMAPiMF_00146. dCTP_deaminase. 1 hit.
InterProiIPR011962. dCTP_deam.
IPR010550. dCTP_deam_bac.
IPR029054. dUTPase-like.
IPR008180. dUTPase/dCTP_deaminase.
IPR033704. dUTPase_trimeric.
[Graphical view]
PfamiPF06559. DCD. 1 hit.
PF00692. dUTPase. 1 hit.
[Graphical view]
SUPFAMiSSF51283. SSF51283. 1 hit.
TIGRFAMsiTIGR02274. dCTP_deam. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiDCD_METTH
AccessioniPrimary (citable) accession number: O27875
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: December 1, 2000
Last modified: November 30, 2016
This is version 99 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. 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.