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Q0I4X6 (CDD_HISS1) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 58. 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:HS_1257
OrganismHistophilus somni (strain 129Pt) (Haemophilus somnus) [Complete proteome] [HAMAP]
Taxonomic identifier205914 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHistophilus

Protein attributes

Sequence length303 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 – 303303Cytidine deaminase HAMAP-Rule MF_01558
PRO_0000318623

Regions

Domain69 – 15183CMP/dCMP deaminase zinc-binding
Region98 – 1003Substrate binding By similarity

Sites

Active site1131Proton donor By similarity
Metal binding1111Zinc; catalytic By similarity
Metal binding1381Zinc; catalytic By similarity
Metal binding1411Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
Q0I4X6 [UniParc].

Last modified October 3, 2006. Version 1.
Checksum: 16CDCC47C9A6B43F

FASTA30334,347
        10         20         30         40         50         60 
MTHHSLKHIS DRIKQALNQI ENRNLAQDLW YILGEQNFQG FLPAFTVNHF CEKYHMTDKE 

        70         80         90        100        110        120 
LALILLPVSA CYANPTISHF SVGAIAKGES GSFYFGANQE FCTTNIQQTV HAEQSAISHA 

       130        140        150        160        170        180 
WMRRESKITE ITVNYTPCGH CRQFMNELNS AETLRIHLPH SQDNLLHHYL PDAFGPHNLQ 

       190        200        210        220        230        240 
IDNRLFDKKA HNLFFVTEDP LIQAALDAAN QSHAPYSKTY SGIALQLQDQ QIFQGSYAEN 

       250        260        270        280        290        300 
AAFNPSLPPL QTALNYLLLN GNEVENIARA VLVEQPFRLS YRGMTEELLA YLGDIPLDYI 


QVS 

« Hide

References

[1]"Complete genome sequence of Haemophilus somnus (Histophilus somni) strain 129Pt and comparison to Haemophilus ducreyi 35000HP and Haemophilus influenzae Rd."
Challacombe J.F., Duncan A.J., Brettin T.S., Bruce D., Chertkov O., Detter J.C., Han C.S., Misra M., Richardson P., Tapia R., Thayer N., Xie G., Inzana T.J.
J. Bacteriol. 189:1890-1898(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 129Pt.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000436 Genomic DNA. Translation: ABI25532.1.
RefSeqYP_719469.1. NC_008309.1.

3D structure databases

ProteinModelPortalQ0I4X6.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING205914.HS_1257.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABI25532; ABI25532; HS_1257.
GeneID4240768.
KEGGhso:HS_1257.
PATRIC20282599. VBIHaeSom53361_1320.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0295.
HOGENOMHOG000218617.
KOK01489.
OrthoDBEOG6XDH25.

Enzyme and pathway databases

BioCycHSOM205914:GJ7V-1312-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_HISS1
AccessionPrimary (citable) accession number: Q0I4X6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: October 3, 2006
Last modified: May 14, 2014
This is version 58 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