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Protein

Cytidine deaminase

Gene

cdd

Organism
Sporosarcina psychrophila (Bacillus psychrophilus)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.By similarity

Catalytic activityi

Cytidine + H2O = uridine + NH3.
2'deoxycytidine + H2O = 2'-deoxyuridine + NH3.

Cofactori

Zn2+By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi53 – 531Zinc; catalyticBy similarity
Active sitei55 – 551Proton donorBy similarity
Metal bindingi86 – 861Zinc; catalyticBy similarity
Metal bindingi89 – 891Zinc; catalyticBy similarity

GO - Molecular functioni

  1. cytidine deaminase activity Source: UniProtKB-EC
  2. zinc ion binding Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.5.4.5. 685.

Names & Taxonomyi

Protein namesi
Recommended name:
Cytidine deaminase (EC:3.5.4.5)
Short name:
CDA
Alternative name(s):
Cytidine aminohydrolase
Gene namesi
Name:cdd
OrganismiSporosarcina psychrophila (Bacillus psychrophilus)
Taxonomic identifieri1476 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesPlanococcaceaeSporosarcina

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 136136Cytidine deaminasePRO_0000171677Add
BLAST

Structurei

3D structure databases

ProteinModelPortaliQ9S3M0.
SMRiQ9S3M0. Positions 1-130.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 128128CMP/dCMP-type deaminasePROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni42 – 443Substrate bindingBy similarity

Sequence similaritiesi

Contains 1 CMP/dCMP-type deaminase domain.PROSITE-ProRule annotation

Family and domain databases

InterProiIPR002125. CMP_dCMP_Zn-bd.
IPR006262. Cyt_deam_tetra.
IPR016193. Cytidine_deaminase-like.
[Graphical view]
PfamiPF00383. dCMP_cyt_deam_1. 1 hit.
[Graphical view]
SUPFAMiSSF53927. SSF53927. 1 hit.
TIGRFAMsiTIGR01354. cyt_deam_tetra. 1 hit.
PROSITEiPS51747. CYT_DCMP_DEAMINASES_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9S3M0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDVEKLIAES KKAREQAYVP YSKFPVGAAL LAEDGTIYHG CNIENSAYSM
60 70 80 90 100
TNCAERTAFF KAVSDGVRSF KALAVVADTE GPVSPCGACR QVIAEFCNGS
110 120 130
MPVYLTNLKG DIEETTVAKL LPGAFSKEDL SYAAEQ
Length:136
Mass (Da):14,600
Last modified:May 1, 2000 - v1
Checksum:i323DDC0450EC3E62
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ237978 Genomic DNA. Translation: CAB51906.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ237978 Genomic DNA. Translation: CAB51906.1.

3D structure databases

ProteinModelPortaliQ9S3M0.
SMRiQ9S3M0. Positions 1-130.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Enzyme and pathway databases

BRENDAi3.5.4.5. 685.

Family and domain databases

InterProiIPR002125. CMP_dCMP_Zn-bd.
IPR006262. Cyt_deam_tetra.
IPR016193. Cytidine_deaminase-like.
[Graphical view]
PfamiPF00383. dCMP_cyt_deam_1. 1 hit.
[Graphical view]
SUPFAMiSSF53927. SSF53927. 1 hit.
TIGRFAMsiTIGR01354. cyt_deam_tetra. 1 hit.
PROSITEiPS51747. CYT_DCMP_DEAMINASES_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Cytidine deaminase from two extremophilic bacteria: cloning, expression and comparison of their structural stability."
    Cambi A., Vincenzetti S., De Sanctis G., Neuhard J., Natalini P., Vita A.
    Protein Eng. 14:807-813(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Entry informationi

Entry nameiCDD_SPOPS
AccessioniPrimary (citable) accession number: Q9S3M0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 13, 2002
Last sequence update: May 1, 2000
Last modified: April 1, 2015
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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 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.