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Reviewed, UniProtKB/Swiss-Prot Q5PE68 (CDD_SALPA)

Last modified November 3, 2009. Version 34. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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: SPA0668
OrganismSalmonella paratyphi A [Complete proteome] [HAMAP]
Taxonomic identifier54388 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeSalmonella

Protein attributes

Sequence length294 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

This enzyme scavenge exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis By similarity.

Catalytic activity

Cytidine + H2O = uridine + NH3. HAMAP MF_01558

Cofactor

Binds 1 zinc ion By similarity.

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the cytidine and deoxycytidylate deaminase family.

Ontologies

Keywords
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcytidine metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functioncytidine deaminase activity

Inferred from electronic annotation. Source: HAMAP

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 294294Cytidine deaminase HAMAP MF_01558
PRO_0000171661

Regions

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
Q5PE68-1 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: BC695CBDC170A8C8

FASTA29431,718
        10         20         30         40         50         60 
MHPRFQTAFA QLADNLQSAL APILADHHFP AMLTAEQVST LKNTARLDED ALAFALLPLA 

        70         80         90        100        110        120 
AACARTDLSH FNVGAIARGV SGNWYFGANM EFLGATMQQT VHAEQSAISH AWLRGEKGLA 

       130        140        150        160        170        180 
AVTVNYTPCG HCRQFMNELN SGLDLRIHLP GRAPHTLRDY LPDAFGPKDL EIKTLLMDEQ 

       190        200        210        220        230        240 
DHGFTLTGDT LTQAAITAAN KSHMPYSHSP SGVALECKDG RIFTGSYAEN AAFNPTLPPL 

       250        260        270        280        290 
QGALNLLSLN GYDYADIQRA ILAEKGDAAL IQWDATAATL KALGCHNIDR VLLG 

« Hide

References

[1]"Comparison of genome degradation in Paratyphi A and Typhi, human-restricted serovars of Salmonella enterica that cause typhoid."
McClelland M., Sanderson K.E., Clifton S.W., Latreille P., Porwollik S., Sabo A., Meyer R., Bieri T., Ozersky P., McLellan M., Harkins C.R., Wang C., Nguyen C., Berghoff A., Elliott G., Kohlberg S., Strong C., Du F. expand/collapse author list , Carter J., Kremizki C., Layman D., Leonard S., Sun H., Fulton L., Nash W., Miner T., Minx P., Delehaunty K., Fronick C., Magrini V., Nhan M., Warren W., Florea L., Spieth J., Wilson R.K.
Nat. Genet. 36:1268-1274(2004) [PubMed: 15531882] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 9150 / SARB42.

Cross-references

Sequence databases

CP000026 Genomic DNA. Translation: AAV76666.1.
RefSeqYP_149978.1.

3D structure databases

SMRQ5PE68. Positions 1-294.
ModBaseSearch...

Genome annotation databases

GeneID3177937.
GenomeReviewsGene locus SPA0668 in contig CP000026_GR.
KEGGspt:SPA0668.
NMPDRfig|295319.3.peg.1528.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ5PE68.
OMAFSPCGHC.

Enzyme and pathway databases

BioCycSENT295319:SPA0668-MON.

Family and domain databases

HAMAPMF_01558.
[Tree]
InterProIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn_bd.
IPR013171. Cyd/dCyd_deaminase_Zn_bd.
IPR006263. Cyt_deam_dimer.
[Graphical view]
PfamPF00383. dCMP_cyt_deam_1. 1 hit.
PF08211. dCMP_cyt_deam_2. 1 hit.
[Graphical view]
TIGRFAMsTIGR01355. cyt_deam_dimer. 1 hit.
PROSITEPS00903. CYT_DCMP_DEAMINASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCDD_SALPA
AccessionPrimary (citable) accession number: Q5PE68
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: January 4, 2005
Last modified: November 3, 2009
This is version 34 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents