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Protein

Cytidine deaminase

Gene

cdd

Organism
Escherichia coli O17:K52:H18 (strain UMN026 / ExPEC)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.UniRule annotation

Catalytic activityi

Cytidine + H2O = uridine + NH3.UniRule annotation
2'deoxycytidine + H2O = 2'-deoxyuridine + NH3.UniRule annotation

Cofactori

Zn2+UniRule annotationNote: Binds 1 zinc ion.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi102 – 1021Zinc; catalyticUniRule annotation
Active sitei104 – 1041Proton donorUniRule annotation
Metal bindingi129 – 1291Zinc; catalyticUniRule annotation
Metal bindingi132 – 1321Zinc; catalyticUniRule annotation

GO - Molecular functioni

  1. cytidine deaminase activity Source: UniProtKB-HAMAP
  2. zinc ion binding Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Cytidine deaminaseUniRule annotation (EC:3.5.4.5UniRule annotation)
Alternative name(s):
Cytidine aminohydrolaseUniRule annotation
Short name:
CDAUniRule annotation
Gene namesi
Name:cddUniRule annotation
Ordered Locus Names:ECUMN_2476
OrganismiEscherichia coli O17:K52:H18 (strain UMN026 / ExPEC)
Taxonomic identifieri585056 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
ProteomesiUP000007097: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 294294Cytidine deaminasePRO_1000147100Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi585056.ECUMN_2476.

Structurei

3D structure databases

ProteinModelPortaliB7NCH2.
SMRiB7NCH2. Positions 1-294.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini56 – 13984CMP/dCMP deaminase zinc-bindingAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni89 – 913Substrate bindingUniRule annotation

Sequence similaritiesi

Belongs to the cytidine and deoxycytidylate deaminase family.UniRule annotation

Phylogenomic databases

eggNOGiCOG0295.
HOGENOMiHOG000218617.
KOiK01489.
OMAiSHAPYSK.
OrthoDBiEOG6XDH25.

Family and domain databases

HAMAPiMF_01558. Cyt_deam.
InterProiIPR016192. 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]
PfamiPF00383. dCMP_cyt_deam_1. 1 hit.
PF08211. dCMP_cyt_deam_2. 1 hit.
[Graphical view]
PIRSFiPIRSF006334. Cdd_plus_pseudo. 1 hit.
SUPFAMiSSF53927. SSF53927. 2 hits.
TIGRFAMsiTIGR01355. cyt_deam_dimer. 1 hit.
PROSITEiPS00903. CYT_DCMP_DEAMINASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B7NCH2-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MHPRFQTAFA QLADNLQSAL EPILADKYFP ALLTGEQVSS LKSATGLDED
60 70 80 90 100
ALAFALLPLA AACARTPLSN FNVGAIARGV SGTWYFGANM EFIGATMQQT
110 120 130 140 150
VHAEQSAISH AWLSGEKALA AITVNYTPCG HCRQFMNELN SGLDLRIHLP
160 170 180 190 200
GREAHALRDY LPDAFGPKDL EIKTLLMDEQ DHGYALTGDA LSQAAIAAAN
210 220 230 240 250
RSHMPYSKSP SGVALECKDG RIFSGSYAEN AAFNPTLPPL QGALILLNLK
260 270 280 290
GYDYPDIQRA VLAEKADAPL IQWDATSATL KALGCHNIDR VLLA
Length:294
Mass (Da):31,567
Last modified:March 24, 2009 - v1
Checksum:i69B5CD68AB145D6C
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU928163 Genomic DNA. Translation: CAR13662.1.
RefSeqiYP_002413190.1. NC_011751.1.

Genome annotation databases

EnsemblBacteriaiCAR13662; CAR13662; ECUMN_2476.
GeneIDi7159562.
KEGGieum:ECUMN_2476.
PATRICi18444205. VBIEscCol32010_2656.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CU928163 Genomic DNA. Translation: CAR13662.1.
RefSeqiYP_002413190.1. NC_011751.1.

3D structure databases

ProteinModelPortaliB7NCH2.
SMRiB7NCH2. Positions 1-294.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi585056.ECUMN_2476.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiCAR13662; CAR13662; ECUMN_2476.
GeneIDi7159562.
KEGGieum:ECUMN_2476.
PATRICi18444205. VBIEscCol32010_2656.

Phylogenomic databases

eggNOGiCOG0295.
HOGENOMiHOG000218617.
KOiK01489.
OMAiSHAPYSK.
OrthoDBiEOG6XDH25.

Family and domain databases

HAMAPiMF_01558. Cyt_deam.
InterProiIPR016192. 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]
PfamiPF00383. dCMP_cyt_deam_1. 1 hit.
PF08211. dCMP_cyt_deam_2. 1 hit.
[Graphical view]
PIRSFiPIRSF006334. Cdd_plus_pseudo. 1 hit.
SUPFAMiSSF53927. SSF53927. 2 hits.
TIGRFAMsiTIGR01355. cyt_deam_dimer. 1 hit.
PROSITEiPS00903. CYT_DCMP_DEAMINASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: UMN026 / ExPEC.

Entry informationi

Entry nameiCDD_ECOLU
AccessioniPrimary (citable) accession number: B7NCH2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 14, 2009
Last sequence update: March 24, 2009
Last modified: January 7, 2015
This is version 41 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.