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Protein

Cytidine deaminase

Gene

cdd

Organism
Shewanella amazonensis (strain ATCC BAA-1098 / SB2B)
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)DescriptionActionsGraphical viewLength
Metal bindingi101Zinc; catalyticUniRule annotation1
Active sitei103Proton donorUniRule annotation1
Metal bindingi128Zinc; catalyticUniRule annotation1
Metal bindingi131Zinc; catalyticUniRule annotation1

GO - Molecular functioni

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:Sama_1974
OrganismiShewanella amazonensis (strain ATCC BAA-1098 / SB2B)
Taxonomic identifieri326297 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella
Proteomesi
  • UP000009175 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000689591 – 296Cytidine deaminaseAdd BLAST296

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi326297.Sama_1974.

Structurei

3D structure databases

ProteinModelPortaliA1S723.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini47 – 167CMP/dCMP-type deaminase 1PROSITE-ProRule annotationAdd BLAST121
Domaini186 – 296CMP/dCMP-type deaminase 2PROSITE-ProRule annotationAdd BLAST111

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni88 – 90Substrate bindingUniRule annotation3

Sequence similaritiesi

Belongs to the cytidine and deoxycytidylate deaminase family.UniRule annotation
Contains 2 CMP/dCMP-type deaminase domains.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiENOG4107T42. Bacteria.
COG0295. LUCA.
HOGENOMiHOG000218617.
KOiK01489.
OMAiNQSHAPY.
OrthoDBiPOG091H026Y.

Family and domain databases

HAMAPiMF_01558. Cyt_deam. 1 hit.
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. 1 hit.
PS51747. CYT_DCMP_DEAMINASES_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

A1S723-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQDRFVRRIN ELPKALADEL LPMLGEQFCG HLDAQQVKQL CAVSAMDSHE
60 70 80 90 100
LGLALLPIAA ALAKPPVSNF YVGAIAVGSG GDFYMGANLE LQGEALFHSV
110 120 130 140 150
HAEQSAISHA WLSGETQISD IIVNASPCGH CRQFMNELVQ GQAIRIHLPG
160 170 180 190 200
QDTAPLSHYL PYAFGPADLN VTAPLLSKQQ TELVLESDDP LLIEALDHAG
210 220 230 240 250
LSYAPYSQCH AAVVLETEDG ASFCGRYAEN AAFNPSMLPM QMALSALVRH
260 270 280 290
NRSFSDIKRA VLLESSQGKI SLVGATMDAL HAVAVVELEH LVVDPV
Length:296
Mass (Da):31,802
Last modified:February 6, 2007 - v1
Checksum:iBF1B6BF257D052F8
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000507 Genomic DNA. Translation: ABM00180.1.
RefSeqiWP_011760087.1. NC_008700.1.

Genome annotation databases

EnsemblBacteriaiABM00180; ABM00180; Sama_1974.
KEGGisaz:Sama_1974.
PATRICi23452695. VBISheAma74963_2036.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000507 Genomic DNA. Translation: ABM00180.1.
RefSeqiWP_011760087.1. NC_008700.1.

3D structure databases

ProteinModelPortaliA1S723.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi326297.Sama_1974.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABM00180; ABM00180; Sama_1974.
KEGGisaz:Sama_1974.
PATRICi23452695. VBISheAma74963_2036.

Phylogenomic databases

eggNOGiENOG4107T42. Bacteria.
COG0295. LUCA.
HOGENOMiHOG000218617.
KOiK01489.
OMAiNQSHAPY.
OrthoDBiPOG091H026Y.

Family and domain databases

HAMAPiMF_01558. Cyt_deam. 1 hit.
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. 1 hit.
PS51747. CYT_DCMP_DEAMINASES_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCDD_SHEAM
AccessioniPrimary (citable) accession number: A1S723
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 6, 2007
Last modified: November 2, 2016
This is version 60 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, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families

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 one 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.