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A5F1V7 (CDD_VIBC3) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 47. 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:VC0395_A0852, VC395_1350
OrganismVibrio cholerae serotype O1 (strain ATCC 39541 / Classical Ogawa 395 / O395) [Complete proteome] [HAMAP]
Taxonomic identifier345073 [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_1000073582

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
A5F1V7 [UniParc].

Last modified June 12, 2007. Version 1.
Checksum: EAE80602103E48C9

FASTA29531,989
        10         20         30         40         50         60 
MRNRIEQALQ QMPASFAPYL RELVLAKDFD ATFSAEQYQQ LLTLSGMEDS 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]Heidelberg J.
Submitted (MAR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 39541 / Classical Ogawa 395 / O395.
[2]"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: ATCC 39541 / Classical Ogawa 395 / O395.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000627 Genomic DNA. Translation: ABQ21759.1.
CP001235 Genomic DNA. Translation: ACP09358.1.
RefSeqYP_001216798.1. NC_009457.1.
YP_002819594.1. NC_012582.1.

3D structure databases

ProteinModelPortalA5F1V7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING345073.VC0395_A0852.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ21759; ABQ21759; VC0395_A0852.
ACP09358; ACP09358; VC395_1350.
GeneID5137396.
7775276.
KEGGvco:VC0395_A0852.
vcr:VC395_1350.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0295.
HOGENOMHOG000218617.
KOK01489.
OMANRSHAPY.
ProtClustDBPRK09027.

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_VIBC3
AccessionPrimary (citable) accession number: A5F1V7
Secondary accession number(s): C3LZZ2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: June 12, 2007
Last modified: April 16, 2014
This is version 47 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