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Q9S3M0 (CDD_SPOPS) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 60. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cytidine deaminase

Short name=CDA
EC=3.5.4.5
Alternative name(s):
Cytidine aminohydrolase
Gene names
Name:cdd
OrganismSporosarcina psychrophila (Bacillus psychrophilus)
Taxonomic identifier1476 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacilliBacillalesPlanococcaceaeSporosarcina

Protein attributes

Sequence length136 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

Catalytic activity

Cytidine + H2O = uridine + NH3.

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

Cofactor

Zinc By similarity.

Sequence similarities

Belongs to the cytidine and deoxycytidylate deaminase family.

Contains 1 CMP/dCMP deaminase zinc-binding domain.

Ontologies

Keywords
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Gene Ontology (GO)
   Molecular_functioncytidine deaminase activity

Inferred from electronic annotation. Source: UniProtKB-EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 136136Cytidine deaminase
PRO_0000171677

Regions

Domain3 – 9795CMP/dCMP deaminase zinc-binding
Region42 – 443Substrate binding By similarity

Sites

Active site551Proton donor By similarity
Metal binding531Zinc; catalytic By similarity
Metal binding861Zinc; catalytic By similarity
Metal binding891Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9S3M0 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 323DDC0450EC3E62

FASTA13614,600
        10         20         30         40         50         60 
MDVEKLIAES KKAREQAYVP YSKFPVGAAL LAEDGTIYHG CNIENSAYSM TNCAERTAFF 

        70         80         90        100        110        120 
KAVSDGVRSF KALAVVADTE GPVSPCGACR QVIAEFCNGS MPVYLTNLKG DIEETTVAKL 

       130 
LPGAFSKEDL SYAAEQ 

« Hide

References

[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(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ237978 Genomic DNA. Translation: CAB51906.1.

3D structure databases

ProteinModelPortalQ9S3M0.
SMRQ9S3M0. Positions 1-130.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA3.5.4.5. 685.

Family and domain databases

InterProIPR002125. CMP_dCMP_Zn-bd.
IPR006262. Cyt_deam_tetra.
IPR016193. Cytidine_deaminase-like.
[Graphical view]
PfamPF00383. dCMP_cyt_deam_1. 1 hit.
[Graphical view]
SUPFAMSSF53927. SSF53927. 1 hit.
TIGRFAMsTIGR01354. cyt_deam_tetra. 1 hit.
ProtoNetSearch...

Entry information

Entry nameCDD_SPOPS
AccessionPrimary (citable) accession number: Q9S3M0
Entry history
Integrated into UniProtKB/Swiss-Prot: August 13, 2002
Last sequence update: May 1, 2000
Last modified: February 19, 2014
This is version 60 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families