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Protein

Cytidine deaminase

Gene

cdd

Organism
Shigella flexneri
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:SF2228, S2357
OrganismiShigella flexneri
Taxonomic identifieri623 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeShigella
ProteomesiUP000002673 Componenti: Chromosome UP000001006 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 294294Cytidine deaminasePRO_0000171667Add
BLAST

Proteomic databases

PaxDbiP0ABF7.
PRIDEiP0ABF7.

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi198214.SF2228.

Structurei

3D structure databases

SMRiP0ABF7. Positions 1-294.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini48 – 168121CMP/dCMP-type deaminase 1PROSITE-ProRule annotationAdd
BLAST
Domaini186 – 294109CMP/dCMP-type deaminase 2PROSITE-ProRule annotationAdd
BLAST

Region

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

Sequence similaritiesi

Belongs to the cytidine and deoxycytidylate deaminase family.UniRule annotation
Contains 2 CMP/dCMP-type deaminase domains.PROSITE-ProRule 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. 1 hit.
PS51747. CYT_DCMP_DEAMINASES_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0ABF7-1 [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 KALGCHSIDR VLLA
Length:294
Mass (Da):31,540
Last modified:October 24, 2005 - v1
Checksum:iF0B5CD68AB145D7D
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005674 Genomic DNA. Translation: AAN43750.1.
AE014073 Genomic DNA. Translation: AAP17567.1.
RefSeqiNP_708043.1. NC_004337.2.
NP_837758.1. NC_004741.1.

Genome annotation databases

EnsemblBacteriaiAAN43750; AAN43750; SF2228.
AAP17567; AAP17567; S2357.
GeneIDi1025385.
1078648.
KEGGisfl:SF2228.
sfx:S2357.
PATRICi18706267. VBIShiFle31049_2610.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE005674 Genomic DNA. Translation: AAN43750.1.
AE014073 Genomic DNA. Translation: AAP17567.1.
RefSeqiNP_708043.1. NC_004337.2.
NP_837758.1. NC_004741.1.

3D structure databases

SMRiP0ABF7. Positions 1-294.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi198214.SF2228.

Proteomic databases

PaxDbiP0ABF7.
PRIDEiP0ABF7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAN43750; AAN43750; SF2228.
AAP17567; AAP17567; S2357.
GeneIDi1025385.
1078648.
KEGGisfl:SF2228.
sfx:S2357.
PATRICi18706267. VBIShiFle31049_2610.

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. 1 hit.
PS51747. CYT_DCMP_DEAMINASES_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Genome sequence of Shigella flexneri 2a: insights into pathogenicity through comparison with genomes of Escherichia coli K12 and O157."
    Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J., Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L., Xue Y.
    , Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H., Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.
    Nucleic Acids Res. 30:4432-4441(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 301 / Serotype 2a.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700930 / 2457T / Serotype 2a.

Entry informationi

Entry nameiCDD_SHIFL
AccessioniPrimary (citable) accession number: P0ABF7
Secondary accession number(s): P13652
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 24, 2005
Last sequence update: October 24, 2005
Last modified: March 31, 2015
This is version 73 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.