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C3LLS7 (CDD_VIBCM) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 34. 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

EC=3.5.4.5
Alternative name(s):
Cytidine aminohydrolase
Short name=CDA
Gene names
Name:cdd
Ordered Locus Names:VCM66_1186
OrganismVibrio cholerae serotype O1 (strain M66-2) [Complete proteome] [HAMAP]
Taxonomic identifier579112 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length295 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. HAMAP-Rule MF_01558

Catalytic activity

Cytidine + H2O = uridine + NH3. HAMAP-Rule MF_01558

2'deoxycytidine + H2O = 2'-deoxyuridine + NH3. HAMAP-Rule MF_01558

Cofactor

Binds 1 zinc ion By similarity. HAMAP-Rule MF_01558

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_01558

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
   Technical termComplete proteome
Gene Ontology (GO)
   Molecular_functioncytidine deaminase activity

Inferred from electronic annotation. Source: UniProtKB-HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-HAMAP

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 295295Cytidine deaminase HAMAP-Rule MF_01558
PRO_1000185419

Regions

Domain60 – 14081CMP/dCMP deaminase zinc-binding
Region89 – 913Substrate binding By similarity

Sites

Active site1041Proton donor By similarity
Metal binding1021Zinc; catalytic By similarity
Metal binding1291Zinc; catalytic By similarity
Metal binding1321Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
C3LLS7 [UniParc].

Last modified June 16, 2009. Version 1.
Checksum: 7AA766021089D736

FASTA29531,955
        10         20         30         40         50         60 
MRNRIEQALQ QMPASFAPYL RELVLAKDFD ATFSAEQYQQ LLTLSGLEDA DLRVALLPIA 

        70         80         90        100        110        120 
AAYSYAPISE FYVGAIVRGI SGRLYLGANM EFTGAQLGQT VHAEQCAISH AWMKGEKGVA 

       130        140        150        160        170        180 
DITINFSPCG HCRQFMNELT TASSLKIQLP KRAAKTLQEY LPESFGPADL GIDSGLMSPV 

       190        200        210        220        230        240 
NHGKTSDDDE ELIQQALRAM NISHSPYTQN FSGVALKMRS GAIYLGAYAE NAAFNPSLPP 

       250        260        270        280        290 
LQVALAQAMM MGESFEDIEA AALVESATGK ISHLADTQAT LEVINPDIPL SYLSL 

« Hide

References

[1]"A recalibrated molecular clock and independent origins for the cholera pandemic clones."
Feng L., Reeves P.R., Lan R., Ren Y., Gao C., Zhou Z., Ren Y., Cheng J., Wang W., Wang J., Qian W., Li D., Wang L.
PLoS ONE 3:E4053-E4053(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: M66-2.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001233 Genomic DNA. Translation: ACP05503.1.
RefSeqYP_002809954.1. NC_012578.1.

3D structure databases

ProteinModelPortalC3LLS7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING579112.VCM66_1186.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACP05503; ACP05503; VCM66_1186.
GeneID7772464.
KEGGvcm:VCM66_1186.
PATRIC20066157. VBIVibCho108967_1129.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0295.
HOGENOMHOG000218617.
KOK01489.
OMANRSHAPY.
OrthoDBEOG6XDH25.
ProtClustDBPRK09027.

Enzyme and pathway databases

BioCycVCHO579112:GJAW-1252-MONOMER.

Family and domain databases

HAMAPMF_01558. Cyt_deam.
InterProIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn-bd.
IPR013171. Cyd/dCyd_deaminase_Zn-bd.
IPR006263. Cyt_deam_dimer.
IPR016193. Cytidine_deaminase-like.
IPR020797. Cytidine_deaminase_bacteria.
[Graphical view]
PfamPF00383. dCMP_cyt_deam_1. 1 hit.
PF08211. dCMP_cyt_deam_2. 1 hit.
[Graphical view]
PIRSFPIRSF006334. Cdd_plus_pseudo. 1 hit.
SUPFAMSSF53927. SSF53927. 2 hits.
TIGRFAMsTIGR01355. cyt_deam_dimer. 1 hit.
PROSITEPS00903. CYT_DCMP_DEAMINASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCDD_VIBCM
AccessionPrimary (citable) accession number: C3LLS7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: June 16, 2009
Last modified: February 19, 2014
This is version 34 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