Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9KSM5 (CDD_VIBCH) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 79. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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:VC_1231
OrganismVibrio cholerae serotype O1 (strain ATCC 39315 / El Tor Inaba N16961) [Reference proteome] [HAMAP]
Taxonomic identifier243277 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaVibrionalesVibrionaceaeVibrio

Protein attributes

Sequence length295 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

This enzyme scavenges 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 295295Cytidine deaminase HAMAP-Rule MF_01558
PRO_0000171669

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

Secondary structure

..................................................... 295
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q9KSM5 [UniParc].

Last modified October 1, 2000. 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

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE003852 Genomic DNA. Translation: AAF94390.1.
PIRG82226.
RefSeqNP_230876.1. NC_002505.1.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
4EG2X-ray2.20A/B/C/D/E/F/G/H1-295[»]
ProteinModelPortalQ9KSM5.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243277.VC1231.

Protocols and materials databases

DNASU2614668.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAF94390; AAF94390; VC_1231.
GeneID2614668.
KEGGvch:VC1231.
PATRIC20081548. VBIVibCho83274_1173.

Phylogenomic databases

eggNOGCOG0295.
KOK01489.
OMANRSHAPY.
OrthoDBEOG6XDH25.

Enzyme and pathway databases

BioCycVCHO:VC1231-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_VIBCH
AccessionPrimary (citable) accession number: Q9KSM5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: October 1, 2000
Last modified: May 14, 2014
This is version 79 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references