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Protein

Cytidine deaminase

Gene

cdd

Organism
Shewanella sp. (strain W3-18-1)
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:Sputw3181_2531
OrganismiShewanella sp. (strain W3-18-1)
Taxonomic identifieri351745 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaAlteromonadalesShewanellaceaeShewanella

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_10000689681 – 296Cytidine deaminaseAdd BLAST296

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Structurei

3D structure databases

ProteinModelPortaliA1RL10.
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

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.

A1RL10-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQDRFIRSIT QLPLPLADAL IPLLHQNFAG HIDAMQLAKL TLASKMTEAE
60 70 80 90 100
VLLALLPIAA ALAKPPISEF YVGAIAKGKS GDIYMGANLE LPGEALFHSV
110 120 130 140 150
HAEQSAISHA WLSGESQIVD IIVNASPCGH CRQFMNELVD GANITIHLPA
160 170 180 190 200
QESHSLAYYL PYAFGPKDLN VVSPLLAKQQ TEFVLDSSDP MIIEGLDHAG
210 220 230 240 250
LSYAPYTQSF AAVVLETHDG ATYCGRYAEN AAFNPSMLPM QMALSNLTRH
260 270 280 290
NREFSDIRRA VLIESSQGKI SLVGATMDAL HTIAAVELEH IVVDPV
Length:296
Mass (Da):32,023
Last modified:February 6, 2007 - v1
Checksum:i74D9F7F0192A0AE6
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000503 Genomic DNA. Translation: ABM25355.1.
RefSeqiWP_011789815.1. NC_008750.1.

Genome annotation databases

EnsemblBacteriaiABM25355; ABM25355; Sputw3181_2531.
KEGGishw:Sputw3181_2531.
PATRICi23598841. VBISheSp103602_2648.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP000503 Genomic DNA. Translation: ABM25355.1.
RefSeqiWP_011789815.1. NC_008750.1.

3D structure databases

ProteinModelPortaliA1RL10.
ModBaseiSearch...
MobiDBiSearch...

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiABM25355; ABM25355; Sputw3181_2531.
KEGGishw:Sputw3181_2531.
PATRICi23598841. VBISheSp103602_2648.

Phylogenomic databases

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_SHESW
AccessioniPrimary (citable) accession number: A1RL10
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: February 6, 2007
Last modified: November 2, 2016
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

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.