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A5UEI7 (CDD_HAEIG) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 45. 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:CGSHiGG_00395
OrganismHaemophilus influenzae (strain PittGG) [Complete proteome] [HAMAP]
Taxonomic identifier374931 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length292 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-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 – 292292Cytidine deaminase HAMAP-Rule MF_01558
PRO_1000068956

Regions

Domain51 – 13989CMP/dCMP deaminase zinc-binding
Region88 – 903Substrate binding By similarity

Sites

Active site1031Proton donor By similarity
Metal binding1011Zinc; catalytic By similarity
Metal binding1281Zinc; catalytic By similarity
Metal binding1311Zinc; catalytic By similarity

Sequences

Sequence LengthMass (Da)Tools
A5UEI7 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 62F0DCBF015F5DB3

FASTA29232,597
        10         20         30         40         50         60 
MQELIKRTLP QDDALNQAIV NELRSQNWAG FLNYSQVQQL CHNFELTTLK LAMHLLPLAA 

        70         80         90        100        110        120 
SYSHTAISHF NVGAIAIGEQ GDFYFGANQE FANSAIQQTI HAEQSAISHA WLRNERRISD 

       130        140        150        160        170        180 
MVVNYTPCGH CRQFMNELHG AEKISIHLPH SQNNPLHSYL PDAFGPKDLD IAAHLLAEEN 

       190        200        210        220        230        240 
HDLVADHQDD LVNQAILAAN QSHCPYSNSP HGIAILFKNG DVVTGRYAEN AAFNPSLPAL 

       250        260        270        280        290 
QTALNFAYLN DRKLSDIERI VMAEKALKLS HKTMAETLLS TLTSVELEYY SL 

« Hide

References

[1]"Characterization and modeling of the Haemophilus influenzae core and supragenomes based on the complete genomic sequences of Rd and 12 clinical nontypeable strains."
Hogg J.S., Hu F.Z., Janto B., Boissy R., Hayes J., Keefe R., Post J.C., Ehrlich G.D.
Genome Biol. 8:R103.1-R103.18(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PittGG.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000672 Genomic DNA. Translation: ABQ99192.1.
RefSeqYP_001291576.1. NC_009567.1.

3D structure databases

ProteinModelPortalA5UEI7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING374931.CGSHiGG_00395.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABQ99192; ABQ99192; CGSHiGG_00395.
GeneID5227876.
KEGGhiq:CGSHiGG_00395.
PATRIC20184295. VBIHaeInf102487_0080.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0295.
HOGENOMHOG000218617.
KOK01489.
OMANRSHAPY.
OrthoDBEOG6XDH25.
ProtClustDBPRK09027.

Enzyme and pathway databases

BioCycHINF374931:GJA4-67-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_HAEIG
AccessionPrimary (citable) accession number: A5UEI7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: July 10, 2007
Last modified: February 19, 2014
This is version 45 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