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Protein

Cytidine deaminase

Gene

cdd

Organism
Shewanella sp. (strain MR-7)
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

BioCyciSSP60481:GHW6-2593-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:Shewmr7_2481
OrganismiShewanella sp. (strain MR-7)
Taxonomic identifieri60481 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
ProteomesiUP000001960: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 296296Cytidine deaminasePRO_1000068967Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi60481.Shewmr7_2481.

Structurei

3D structure databases

ProteinModelPortaliQ0HTT9.
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.

Q0HTT9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MQDRFIRSIT QLPTPLADAL IPLLHQNFAG HIDAQQLAEL VQSSQMTEAE
60 70 80 90 100
VLLALLPIAA ALAKPPISEF YVGAIAKGKS GDIYMGANLE LPGEALFHSV
110 120 130 140 150
HAEQSAISHA WLSGESQIVD MIVNASPCGH CRQFMNELVE GGQIKIHLPS
160 170 180 190 200
QDSHLLSYYL PYAFGPKDLN VQSPLLVKHE TEFALDSSDP MVIEALDHAG
210 220 230 240 250
LSYAPYTQSY AAVVLETADG ATYCGRYAEN AAFNPSMLPM QMALSNLTRH
260 270 280 290
NRDFGEIRRA VLVESSQGKI SLVGATMDAL HPVAAIELEH IVVDPV
Length:296
Mass (Da):32,082
Last modified:October 3, 2006 - v1
Checksum:i537E2442A26A4CF2
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000444 Genomic DNA. Translation: ABI43466.1.
RefSeqiWP_011626544.1. NC_008322.1.
YP_738523.1. NC_008322.1.

Genome annotation databases

EnsemblBacteriaiABI43466; ABI43466; Shewmr7_2481.
GeneIDi4256370.
KEGGishm:Shewmr7_2481.
PATRICi23590123. VBISheSp85603_2560.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000444 Genomic DNA. Translation: ABI43466.1.
RefSeqiWP_011626544.1. NC_008322.1.
YP_738523.1. NC_008322.1.

3D structure databases

ProteinModelPortaliQ0HTT9.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi60481.Shewmr7_2481.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABI43466; ABI43466; Shewmr7_2481.
GeneIDi4256370.
KEGGishm:Shewmr7_2481.
PATRICi23590123. VBISheSp85603_2560.

Phylogenomic databases

eggNOGiCOG0295.
HOGENOMiHOG000218617.
KOiK01489.
OMAiSHAPYSK.
OrthoDBiEOG6XDH25.

Enzyme and pathway databases

BioCyciSSP60481:GHW6-2593-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: MR-7.

Entry informationi

Entry nameiCDD_SHESR
AccessioniPrimary (citable) accession number: Q0HTT9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: October 3, 2006
Last modified: January 7, 2015
This is version 56 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.