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C6DDS7 (CDD_PECCP) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 32. 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:PC1_1495
OrganismPectobacterium carotovorum subsp. carotovorum (strain PC1) [Complete proteome] [HAMAP]
Taxonomic identifier561230 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaePectobacterium

Protein attributes

Sequence length296 AA.
Sequence statusComplete.
Protein existenceInferred from homology

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.

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 – 296296Cytidine deaminase HAMAP-Rule MF_01558
PRO_1000215505

Regions

Domain57 – 14084CMP/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
C6DDS7 [UniParc].

Last modified September 1, 2009. Version 1.
Checksum: 44DDC91C25AA3485

FASTA29632,120
        10         20         30         40         50         60 
MHPRFENAFR QLPASLQAAL RPLIDKPDFA AMLTADDVNA VCEASQLDAD ALAFALLPLA 

        70         80         90        100        110        120 
AACAQAPISN FQVGAIAQGL SGNFYFGANM EFSAVQLQQT VHAEQSAVSH AWMRNERGLR 

       130        140        150        160        170        180 
AVTVNYTPCG HCRQFMNELR DAASLRIQLP GRQPATLSHY LPDSFGPVDL QIDTLLMDDI 

       190        200        210        220        230        240 
NHGATLQNMN ALARQALDAA NRSHAPYSKA ISGIVLETSS GNTYTGRYAE NAAFNPSLPP 

       250        260        270        280        290 
LQTALNLMNL AGEDLSTVKH AVVVERRNAV VSHWAISQIM LAELGCTDVE HHFIEE 

« Hide

References

[1]"Complete sequence of Pectobacterium carotovorum subsp. carotovorum PC1."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Tice H., Bruce D., Goodwin L., Pitluck S., Munk A.C., Brettin T., Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N. expand/collapse author list , Balakrishnan V., Glasner J., Perna N.T.
Submitted (JUL-2009) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PC1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001657 Genomic DNA. Translation: ACT12539.1.
RefSeqYP_003017075.1. NC_012917.1.

3D structure databases

ProteinModelPortalC6DDS7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING561230.PC1_1495.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaACT12539; ACT12539; PC1_1495.
GeneID8132436.
KEGGpct:PC1_1495.
PATRIC20487638. VBIPecCar70489_1508.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0295.
HOGENOMHOG000218617.
KOK01489.
OMANRSHAPY.
OrthoDBEOG6XDH25.

Enzyme and pathway databases

BioCycPCAR561230:GKCK-1537-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_PECCP
AccessionPrimary (citable) accession number: C6DDS7
Entry history
Integrated into UniProtKB/Swiss-Prot: September 22, 2009
Last sequence update: September 1, 2009
Last modified: May 14, 2014
This is version 32 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