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Q9CP11 (CDD_PASMU) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 76. 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:PM0259
OrganismPasteurella multocida (strain Pm70) [Complete proteome] [HAMAP]
Taxonomic identifier272843 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaePasteurella

Protein attributes

Sequence length294 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 – 294294Cytidine deaminase HAMAP-Rule MF_01558
PRO_0000171656

Regions

Domain61 – 14282CMP/dCMP deaminase zinc-binding
Region90 – 923Substrate binding By similarity

Sites

Active site1051Proton donor By similarity
Metal binding1031Zinc; catalytic By similarity
Metal binding1301Zinc; catalytic By similarity
Metal binding1331Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9CP11 [UniParc].

Last modified June 1, 2001. Version 1.
Checksum: B490DEDF9BF351CA

FASTA29432,994
        10         20         30         40         50         60 
MSEKIRKTLS LIESQQLAQD VWHILQEQHF KGMLPYFTVE HLCTKHQLTP QQLALKLLPI 

        70         80         90        100        110        120 
AAAYSLAPIS QFHVGAIAIG QRGAYYFGAN LEFASTHIQQ TVHAEQSAIS HAWMNHESAI 

       130        140        150        160        170        180 
TDVVVNYTPC GHCRQFMNEL KTAPQLKIHL PHSQNNLLHS YLPDAFGPAD LDIQHFLLDA 

       190        200        210        220        230        240 
QNNQLTYETQ DPVMLTALEC ANAAHAPYSK SYHGIAIETK DKQIYRGSYA ENAAFNPSLP 

       250        260        270        280        290 
ALQVALNHLL LSGDTLQNIQ RIVMIEKANH LCYRHMAEDL VANLVDIPLD YIAL 

« Hide

References

[1]"Complete genomic sequence of Pasteurella multocida Pm70."
May B.J., Zhang Q., Li L.L., Paustian M.L., Whittam T.S., Kapur V.
Proc. Natl. Acad. Sci. U.S.A. 98:3460-3465(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Pm70.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE004439 Genomic DNA. Translation: AAK02343.1.
RefSeqNP_245196.1. NC_002663.1.

3D structure databases

ProteinModelPortalQ9CP11.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272843.PM0259.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAK02343; AAK02343; PM0259.
GeneID1243606.
KEGGpmu:PM0259.
PATRIC22869670. VBIPasMul88067_0267.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0295.
HOGENOMHOG000218617.
KOK01489.
OMANRSHAPY.
OrthoDBEOG6XDH25.

Enzyme and pathway databases

BioCycPMUL272843:GC8W-263-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_PASMU
AccessionPrimary (citable) accession number: Q9CP11
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: June 1, 2001
Last modified: May 14, 2014
This is version 76 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