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Reviewed, UniProtKB/Swiss-Prot Q1R9T0 (CDD_ECOUT)

Last modified June 16, 2009. Version 23. 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: UTI89_C2416
OrganismEscherichia coli (strain UTI89 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier364106 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

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_1000068952

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
Q1R9T0-1 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: 69B5CD68AB145D6C

FASTA29431,567
        10         20         30         40         50         60 
MHPRFQTAFA QLADNLQSAL EPILADKYFP ALLTGEQVSS LKSATGLDED ALAFALLPLA 

        70         80         90        100        110        120 
AACARTPLSN FNVGAIARGV SGTWYFGANM EFIGATMQQT VHAEQSAISH AWLSGEKALA 

       130        140        150        160        170        180 
AITVNYTPCG HCRQFMNELN SGLDLRIHLP GREAHALRDY LPDAFGPKDL EIKTLLMDEQ 

       190        200        210        220        230        240 
DHGYALTGDA LSQAAIAAAN RSHMPYSKSP SGVALECKDG RIFSGSYAEN AAFNPTLPPL 

       250        260        270        280        290 
QGALILLNLK GYDYPDIQRA VLAEKADAPL IQWDATSATL KALGCHNIDR VLLA 

« Hide

References

[1]"Identification of genes subject to positive selection in uropathogenic strains of Escherichia coli: a comparative genomics approach."
Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J., Gordon J.I.
Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006) [PubMed: 16585510] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000243 Genomic DNA. Translation: ABE07884.1.
RefSeqYP_541415.1.

3D structure databases

SMRQ1R9T0. Positions 1-294.
ModBaseSearch...

Genome annotation databases

GeneID3990463.
GenomeReviewsGene locus UTI89_C2416 in contig CP000243_GR.
KEGGeci:UTI89_C2416.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ1R9T0.
OMAQ1R9T0. FSPCGHC.

Enzyme and pathway databases

BioCycECOL364106:UTI89_C2416-MON.

Family and domain databases

HAMAPMF_01558.
[Tree]
InterProIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn_bd.
IPR006263. Cyt_deam_dimer.
IPR013171. dC_C_deam_Zn_bd.
[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_ECOUT
AccessionPrimary (citable) accession number: Q1R9T0
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: May 16, 2006
Last modified: June 16, 2009
This is version 23 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