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Protein

Cytidine deaminase

Gene

cdd

Organism
Shewanella baltica (strain OS223)
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 bindingi101 – 1011Zinc; catalyticUniRule annotation
Active sitei103 – 1031Proton donorUniRule annotation
Metal bindingi128 – 1281Zinc; catalyticUniRule annotation
Metal bindingi131 – 1311Zinc; 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

Enzyme and pathway databases

BioCyciSBAL407976:GJ6Y-2762-MONOMER.

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:Sbal223_2663
OrganismiShewanella baltica (strain OS223)
Taxonomic identifieri407976 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
ProteomesiUP000002507: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 296296Cytidine deaminasePRO_1000185418Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi407976.Sbal223_2663.

Structurei

3D structure databases

ProteinModelPortaliB8EF35.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini48 – 13891CMP/dCMP deaminase zinc-bindingAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni88 – 903Substrate 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.
PROSITEiPS00903. CYT_DCMP_DEAMINASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

B8EF35-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQDRFIRSIT QLPTPLADAL IPMLHQNFAG HLDAQQLATL TSASKMTEAE
60 70 80 90 100
VLLALLPIAA ALAKPPISEF YVGAIAKGKS GDIYMGANLE LPGEALFHSV
110 120 130 140 150
HAEQSAISHA WLSGESQIVD IIVNASPCGH CRQFMNELVE GSKISIHLPA
160 170 180 190 200
QESHPLAYYL PYAFGPKDLN VTSPLMAKQQ TEFALDSADP MIIEGLDHAG
210 220 230 240 250
LSYAPYTQSF AAVVLETRDG ATYCGRYAEN AAFNPSMLPM QMALSNLVRH
260 270 280 290
NREFSDISRA VLIESSQGKI SLVGATMDAL HTVAAIELEH IVIDPV
Length:296
Mass (Da):31,951
Last modified:March 3, 2009 - v1
Checksum:i38576F5FF2B0442E
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001252 Genomic DNA. Translation: ACK47153.1.
RefSeqiYP_002358576.1. NC_011663.1.

Genome annotation databases

EnsemblBacteriaiACK47153; ACK47153; Sbal223_2663.
GeneIDi7089948.
KEGGisbp:Sbal223_2663.
PATRICi23481623. VBISheBal125792_2743.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001252 Genomic DNA. Translation: ACK47153.1.
RefSeqiYP_002358576.1. NC_011663.1.

3D structure databases

ProteinModelPortaliB8EF35.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi407976.Sbal223_2663.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiACK47153; ACK47153; Sbal223_2663.
GeneIDi7089948.
KEGGisbp:Sbal223_2663.
PATRICi23481623. VBISheBal125792_2743.

Phylogenomic databases

eggNOGiCOG0295.
HOGENOMiHOG000218617.
KOiK01489.
OMAiSHAPYSK.
OrthoDBiEOG6XDH25.

Enzyme and pathway databases

BioCyciSBAL407976:GJ6Y-2762-MONOMER.

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.
PROSITEiPS00903. CYT_DCMP_DEAMINASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: OS223.

Entry informationi

Entry nameiCDD_SHEB2
AccessioniPrimary (citable) accession number: B8EF35
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 28, 2009
Last sequence update: March 3, 2009
Last modified: January 7, 2015
This is version 36 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.