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P00814

- DCTD_BPT2

UniProt

P00814 - DCTD_BPT2

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Protein

Deoxycytidylate deaminase

Gene

CD

Organism
Enterobacteria phage T2 (Bacteriophage T2)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli

Functioni

Supplies the nucleotide substrate for thymidylate synthetase.

Catalytic activityi

dCMP + H2O = dUMP + NH3.

Cofactori

Binds 2 zinc ions per subunit.By similarity

Enzyme regulationi

Allosteric enzyme whose activity is greatly influenced by the end products of its metabolic pathway, dCTP and dTTP.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi19 – 191Zinc 1; structuralBy similarity
Metal bindingi49 – 491Zinc 1; structuralBy similarity
Metal bindingi94 – 941Zinc 1; structuralBy similarity
Metal bindingi102 – 1021Zinc 2; catalyticBy similarity
Metal bindingi104 – 1041Zinc 2; catalyticBy similarity
Active sitei106 – 1061Proton donorBy similarity
Metal bindingi132 – 1321Zinc 2; catalyticBy similarity
Metal bindingi135 – 1351Zinc 2; catalyticBy similarity

GO - Molecular functioni

  1. dCMP deaminase activity Source: UniProtKB-EC
  2. zinc ion binding Source: InterPro

GO - Biological processi

  1. nucleotide biosynthetic process Source: UniProtKB-KW
  2. pyrimidine nucleotide metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Biological processi

Nucleotide biosynthesis

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Deoxycytidylate deaminase (EC:3.5.4.12)
Alternative name(s):
dCMP deaminase
Gene namesi
Name:CD
OrganismiEnterobacteria phage T2 (Bacteriophage T2)
Taxonomic identifieri10664 [NCBI]
Taxonomic lineageiVirusesdsDNA viruses, no RNA stageCaudoviralesMyoviridaeTevenvirinaeT4likevirus
Virus hostiEscherichia coli [TaxID: 562]

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 188188Deoxycytidylate deaminasePRO_0000171700Add
BLAST

Interactioni

Subunit structurei

Homohexamer.

Structurei

3D structure databases

ProteinModelPortaliP00814.
SMRiP00814. Positions 1-188.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Family and domain databases

InterProiIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn-bd.
IPR016193. Cytidine_deaminase-like.
IPR016473. dCMP_deaminase.
IPR015517. dCMP_deaminase-rel.
[Graphical view]
PANTHERiPTHR11086. PTHR11086. 1 hit.
PfamiPF00383. dCMP_cyt_deam_1. 1 hit.
[Graphical view]
PIRSFiPIRSF006019. dCMP_deaminase. 1 hit.
SUPFAMiSSF53927. SSF53927. 1 hit.
PROSITEiPS00903. CYT_DCMP_DEAMINASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P00814-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MKASTVLQIA YLVSQESKCC SWKVGAVIEK NGRIISTGYN GSPAGGVNCD
60 70 80 90 100
NYAAIEGWLL NKPKHTIIQG HKPECVSFGT SDRFVLAKEH RSAHSEWSSK
110 120 130 140 150
NEIHAELNAI LFAARNGSSI EGATMYVTLS PCPDCAKAIA QSGIKKLVYC
160 170 180
ETYDKNKPGW DDILRNAGIE VFNVPKLNWE NISEFCGE
Length:188
Mass (Da):20,599
Last modified:July 21, 1986 - v1
Checksum:iA13EAF89D5CEB14A
GO

Sequence databases

PIRiA01011. DUBPC2.

Cross-referencesi

Sequence databases

PIRi A01011. DUBPC2.

3D structure databases

ProteinModelPortali P00814.
SMRi P00814. Positions 1-188.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Family and domain databases

InterProi IPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn-bd.
IPR016193. Cytidine_deaminase-like.
IPR016473. dCMP_deaminase.
IPR015517. dCMP_deaminase-rel.
[Graphical view ]
PANTHERi PTHR11086. PTHR11086. 1 hit.
Pfami PF00383. dCMP_cyt_deam_1. 1 hit.
[Graphical view ]
PIRSFi PIRSF006019. dCMP_deaminase. 1 hit.
SUPFAMi SSF53927. SSF53927. 1 hit.
PROSITEi PS00903. CYT_DCMP_DEAMINASES. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

  1. "Complete amino acid sequence of an allosteric enzyme, T2 bacteriophage deoxycytidylate deaminase."
    Maley G.F., Guarino D.U., Maley F.
    J. Biol. Chem. 258:8290-8297(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE.

Entry informationi

Entry nameiDCTD_BPT2
AccessioniPrimary (citable) accession number: P00814
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: July 21, 1986
Last modified: October 29, 2014
This is version 69 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programViral Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Allosteric enzyme, Direct protein sequencing

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3