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Q3IBX5 (CDD_PSEHT) Reviewed, UniProtKB/Swiss-Prot

Last modified August 10, 2010. Version 36. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
Customize displayNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·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:PSHAb0315
OrganismPseudoalteromonas haloplanktis (strain TAC 125) [Complete proteome] [HAMAP]
Taxonomic identifier326442 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesPseudoalteromonadaceaePseudoalteromonas

Protein attributes

Sequence length309 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 MF_01558

Catalytic activity

Cytidine + H2O = uridine + NH3. HAMAP MF_01558

Cofactor

Binds 1 zinc ion By similarity. HAMAP MF_01558

Subunit structure

Homodimer By similarity. HAMAP MF_01558

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: EC

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 309309Cytidine deaminase HAMAP MF_01558
PRO_0000171659

Regions

Region100 – 1023Substrate binding By similarity

Sites

Active site1151Proton donor By similarity
Metal binding1131Zinc; catalytic By similarity
Metal binding1401Zinc; catalytic By similarity
Metal binding1431Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
Q3IBX5-1 [UniParc].

Last modified November 8, 2005. Version 1.
Checksum: 5B3D57E86EF87DC8

FASTA30933,242
        10         20         30         40         50         60 
MASATFLVQA NTALSNTHIS LSVAQTQALR SQLKTQRGIL NANNINQLCA QLNVTNDALL 

        70         80         90        100        110        120 
QGLVPLASEF AVAPVSNFHV GAIVKALDES GEVNFYFGAN AEFNRQALSL VVHAEQSAIN 

       130        140        150        160        170        180 
NAWLNGAKKI LKIAISDAPC GYCRQFMNEL ADAREFDILL PEQQFKLADL LPHSFGPTDL 

       190        200        210        220        230        240 
GNQYSLFNPA PQARSFNNTE VEQQLAAYAL AAYVPYSQNY SAVKITTFNN GDFYGSYAEN 

       250        260        270        280        290        300 
AAYSPSLSPL QSALSQLFLA GLSFDQHTVK GITLLETAGH ENQAGVAQAV LASFVNLPPL 


ELISAPLSE 

« Hide

References

[1]"Coping with cold: the genome of the versatile marine Antarctica bacterium Pseudoalteromonas haloplanktis TAC125."
Medigue C., Krin E., Pascal G., Barbe V., Bernsel A., Bertin P.N., Cheung F., Cruveiller S., D'Amico S., Duilio A., Fang G., Feller G., Ho C., Mangenot S., Marino G., Nilsson J., Parrilli E., Rocha E.P.C. expand/collapse author list , Rouy Z., Sekowska A., Tutino M.L., Vallenet D., von Heijne G., Danchin A.
Genome Res. 15:1325-1335(2005) [PubMed: 16169927] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CR954247 Genomic DNA. Translation: CAI89355.1.
RefSeqYP_341801.1.

3D structure databases

ProteinModelPortalQ3IBX5.
SMRQ3IBX5. Positions 25-303.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ3IBX5.

Genome annotation databases

GeneID3711463.
GenomeReviewsGene locus PSHAb0315 in contig CR954247_GR.
KEGGpha:PSHAb0315.
NMPDRfig|326442.4.peg.3244.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0295.
OMANRSHAPY.
PhylomeDBQ3IBX5.
ProtClustDBPRK09027.

Enzyme and pathway databases

BioCycPHAL326442:PSHAB0315-MONOMER.

Family and domain databases

HAMAPMF_01558. Cyt_deam.
[Tree]
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. Cytidine_deaminase-like. 2 hits.
PROSITEPS00903. CYT_DCMP_DEAMINASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCDD_PSEHT
AccessionPrimary (citable) accession number: Q3IBX5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: November 8, 2005
Last modified: August 10, 2010
This is version 36 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