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Protein

Cytidine deaminase

Gene

cdd

Organism
Pasteurella multocida (strain Pm70)
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 bindingi103 – 1031Zinc; catalyticUniRule annotation
Active sitei105 – 1051Proton donorUniRule annotation
Metal bindingi130 – 1301Zinc; catalyticUniRule annotation
Metal bindingi133 – 1331Zinc; 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

BioCyciPMUL272843:GC8W-263-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:PM0259
OrganismiPasteurella multocida (strain Pm70)
Taxonomic identifieri272843 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaePasteurella
ProteomesiUP000000809: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 294294Cytidine deaminasePRO_0000171656Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi272843.PM0259.

Structurei

3D structure databases

ProteinModelPortaliQ9CP11.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini61 – 14282CMP/dCMP deaminase zinc-bindingAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni90 – 923Substrate 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.
TIGRFAMsiTIGR01355. cyt_deam_dimer. 1 hit.
PROSITEiPS00903. CYT_DCMP_DEAMINASES. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9CP11-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MSEKIRKTLS LIESQQLAQD VWHILQEQHF KGMLPYFTVE HLCTKHQLTP
60 70 80 90 100
QQLALKLLPI AAAYSLAPIS QFHVGAIAIG QRGAYYFGAN LEFASTHIQQ
110 120 130 140 150
TVHAEQSAIS HAWMNHESAI TDVVVNYTPC GHCRQFMNEL KTAPQLKIHL
160 170 180 190 200
PHSQNNLLHS YLPDAFGPAD LDIQHFLLDA QNNQLTYETQ DPVMLTALEC
210 220 230 240 250
ANAAHAPYSK SYHGIAIETK DKQIYRGSYA ENAAFNPSLP ALQVALNHLL
260 270 280 290
LSGDTLQNIQ RIVMIEKANH LCYRHMAEDL VANLVDIPLD YIAL
Length:294
Mass (Da):32,994
Last modified:June 1, 2001 - v1
Checksum:iB490DEDF9BF351CA
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004439 Genomic DNA. Translation: AAK02343.1.
RefSeqiNP_245196.1. NC_002663.1.

Genome annotation databases

EnsemblBacteriaiAAK02343; AAK02343; PM0259.
GeneIDi1243606.
KEGGipmu:PM0259.
PATRICi22869670. VBIPasMul88067_0267.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE004439 Genomic DNA. Translation: AAK02343.1.
RefSeqiNP_245196.1. NC_002663.1.

3D structure databases

ProteinModelPortaliQ9CP11.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi272843.PM0259.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAK02343; AAK02343; PM0259.
GeneIDi1243606.
KEGGipmu:PM0259.
PATRICi22869670. VBIPasMul88067_0267.

Phylogenomic databases

eggNOGiCOG0295.
HOGENOMiHOG000218617.
KOiK01489.
OMAiSHAPYSK.
OrthoDBiEOG6XDH25.

Enzyme and pathway databases

BioCyciPMUL272843:GC8W-263-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.
TIGRFAMsiTIGR01355. cyt_deam_dimer. 1 hit.
PROSITEiPS00903. CYT_DCMP_DEAMINASES. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: Pm70.

Entry informationi

Entry nameiCDD_PASMU
AccessioniPrimary (citable) accession number: Q9CP11
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 10, 2006
Last sequence update: June 1, 2001
Last modified: February 4, 2015
This is version 81 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

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.