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Protein

Cytidine deaminase

Gene

cdd

Organism
Escherichia coli (strain K12)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

This enzyme scavenges exogenous and endogenous cytidine and 2'-deoxycytidine for UMP synthesis.

Catalytic activityi

Cytidine + H2O = uridine + NH3.UniRule annotation
2'deoxycytidine + H2O = 2'-deoxyuridine + NH3.UniRule annotation

Cofactori

Zn2+3 PublicationsNote: Binds 1 zinc ion.3 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi102Zinc; catalytic3 Publications1
Active sitei104Proton donor3 Publications1
Metal bindingi129Zinc; catalytic3 Publications1
Metal bindingi132Zinc; catalytic3 Publications1

GO - Molecular functioni

  • cytidine deaminase activity Source: EcoCyc
  • deoxycytidine deaminase activity Source: EcoCyc
  • pyrimidine nucleoside binding Source: EcoliWiki
  • zinc ion binding Source: EcoCyc

GO - Biological processi

  • cytidine deamination Source: EcoCyc
  • deoxycytidine catabolic process Source: EcoCyc
  • nucleobase-containing small molecule interconversion Source: EcoliWiki
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

BioCyciEcoCyc:CYTIDEAM-MONOMER.
ECOL316407:JW2131-MONOMER.
MetaCyc:CYTIDEAM-MONOMER.
BRENDAi3.5.4.5. 2026.

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:b2143, JW2131
OrganismiEscherichia coli (strain K12)
Taxonomic identifieri83333 [NCBI]
Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacteralesEnterobacteriaceaeEscherichia
Proteomesi
  • UP000000318 Componenti: Chromosome
  • UP000000625 Componenti: Chromosome

Organism-specific databases

EcoGeneiEG10137. cdd.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: UniProtKB
Complete GO annotation...

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001716491 – 294Cytidine deaminaseAdd BLAST294

Proteomic databases

EPDiP0ABF6.
PaxDbiP0ABF6.
PRIDEiP0ABF6.

2D gel databases

SWISS-2DPAGEP0ABF6.

Interactioni

Subunit structurei

Homodimer.UniRule annotation3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-550703,EBI-550703

Protein-protein interaction databases

BioGridi4263038. 9 interactors.
DIPiDIP-36169N.
IntActiP0ABF6. 2 interactors.
MINTiMINT-1283574.
STRINGi511145.b2143.

Structurei

Secondary structure

1294
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 5Combined sources3
Helixi6 – 10Combined sources5
Helixi14 – 20Combined sources7
Turni21 – 25Combined sources5
Beta strandi31 – 33Combined sources3
Helixi35 – 44Combined sources10
Helixi49 – 62Combined sources14
Turni67 – 69Combined sources3
Beta strandi74 – 79Combined sources6
Beta strandi84 – 88Combined sources5
Helixi97 – 99Combined sources3
Helixi103 – 113Combined sources11
Beta strandi119 – 126Combined sources8
Helixi130 – 136Combined sources7
Helixi142 – 144Combined sources3
Beta strandi146 – 148Combined sources3
Helixi157 – 160Combined sources4
Helixi167 – 170Combined sources4
Helixi190 – 200Combined sources11
Turni205 – 207Combined sources3
Beta strandi211 – 217Combined sources7
Beta strandi222 – 226Combined sources5
Helixi239 – 249Combined sources11
Helixi254 – 256Combined sources3
Beta strandi257 – 264Combined sources8
Helixi273 – 283Combined sources11
Beta strandi288 – 292Combined sources5

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AF2X-ray2.30A1-294[»]
1ALNX-ray2.30A1-294[»]
1CTTX-ray2.20A1-294[»]
1CTUX-ray2.30A1-294[»]
ProteinModelPortaliP0ABF6.
SMRiP0ABF6.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP0ABF6.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini48 – 168CMP/dCMP-type deaminase 1PROSITE-ProRule annotationAdd BLAST121
Domaini186 – 294CMP/dCMP-type deaminase 2PROSITE-ProRule annotationAdd BLAST109

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni89 – 91Substrate binding3 Publications3

Domaini

Each monomer is composed of a small N-terminal alpha-helical domain and two larger core domains that have nearly identical tertiary structures and are related by approximate two-fold symmetry, but lack homology.

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.
InParanoidiP0ABF6.
KOiK01489.
OMAiNQSHAPY.
PhylomeDBiP0ABF6.

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.
TIGRFAMsiTIGR01355. cyt_deam_dimer. 1 hit.
PROSITEiPS00903. CYT_DCMP_DEAMINASES_1. 1 hit.
PS51747. CYT_DCMP_DEAMINASES_2. 2 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P0ABF6-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MHPRFQTAFA QLADNLQSAL EPILADKYFP ALLTGEQVSS LKSATGLDED
60 70 80 90 100
ALAFALLPLA AACARTPLSN FNVGAIARGV SGTWYFGANM EFIGATMQQT
110 120 130 140 150
VHAEQSAISH AWLSGEKALA AITVNYTPCG HCRQFMNELN SGLDLRIHLP
160 170 180 190 200
GREAHALRDY LPDAFGPKDL EIKTLLMDEQ DHGYALTGDA LSQAAIAAAN
210 220 230 240 250
RSHMPYSKSP SGVALECKDG RIFSGSYAEN AAFNPTLPPL QGALILLNLK
260 270 280 290
GYDYPDIQRA VLAEKADAPL IQWDATSATL KALGCHSIDR VLLA
Length:294
Mass (Da):31,540
Last modified:October 25, 2005 - v1
Checksum:iF0B5CD68AB145D7D
GO

Sequence cautioni

The sequence CAA44849 differs from that shown. Reason: Frameshift at position 255.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti4R → I AA sequence (PubMed:8899705).Curated1
Sequence conflicti58 – 77PLAAA…VGAIA → RWRRPVRVRHCRILMLAQLR (PubMed:2575702).CuratedAdd BLAST20

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60916 Genomic DNA. Translation: AAA23542.1.
X63144 Genomic DNA. Translation: CAA44849.1. Frameshift.
U00007 Genomic DNA. Translation: AAA60533.1.
U00096 Genomic DNA. Translation: AAC75204.1.
AP009048 Genomic DNA. Translation: BAE76620.1.
X16419 Genomic DNA. Translation: CAA34441.1.
Z47804 Genomic DNA. Translation: CAA87765.1.
PIRiF64982.
RefSeqiNP_416648.1. NC_000913.3.
WP_000553555.1. NZ_LN832404.1.

Genome annotation databases

EnsemblBacteriaiAAC75204; AAC75204; b2143.
BAE76620; BAE76620; BAE76620.
GeneIDi946663.
KEGGiecj:JW2131.
eco:b2143.
PATRICi32119629. VBIEscCol129921_2225.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M60916 Genomic DNA. Translation: AAA23542.1.
X63144 Genomic DNA. Translation: CAA44849.1. Frameshift.
U00007 Genomic DNA. Translation: AAA60533.1.
U00096 Genomic DNA. Translation: AAC75204.1.
AP009048 Genomic DNA. Translation: BAE76620.1.
X16419 Genomic DNA. Translation: CAA34441.1.
Z47804 Genomic DNA. Translation: CAA87765.1.
PIRiF64982.
RefSeqiNP_416648.1. NC_000913.3.
WP_000553555.1. NZ_LN832404.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1AF2X-ray2.30A1-294[»]
1ALNX-ray2.30A1-294[»]
1CTTX-ray2.20A1-294[»]
1CTUX-ray2.30A1-294[»]
ProteinModelPortaliP0ABF6.
SMRiP0ABF6.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi4263038. 9 interactors.
DIPiDIP-36169N.
IntActiP0ABF6. 2 interactors.
MINTiMINT-1283574.
STRINGi511145.b2143.

2D gel databases

SWISS-2DPAGEP0ABF6.

Proteomic databases

EPDiP0ABF6.
PaxDbiP0ABF6.
PRIDEiP0ABF6.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAC75204; AAC75204; b2143.
BAE76620; BAE76620; BAE76620.
GeneIDi946663.
KEGGiecj:JW2131.
eco:b2143.
PATRICi32119629. VBIEscCol129921_2225.

Organism-specific databases

EchoBASEiEB0135.
EcoGeneiEG10137. cdd.

Phylogenomic databases

eggNOGiENOG4107T42. Bacteria.
COG0295. LUCA.
HOGENOMiHOG000218617.
InParanoidiP0ABF6.
KOiK01489.
OMAiNQSHAPY.
PhylomeDBiP0ABF6.

Enzyme and pathway databases

BioCyciEcoCyc:CYTIDEAM-MONOMER.
ECOL316407:JW2131-MONOMER.
MetaCyc:CYTIDEAM-MONOMER.
BRENDAi3.5.4.5. 2026.

Miscellaneous databases

EvolutionaryTraceiP0ABF6.
PROiP0ABF6.

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.
TIGRFAMsiTIGR01355. cyt_deam_dimer. 1 hit.
PROSITEiPS00903. CYT_DCMP_DEAMINASES_1. 1 hit.
PS51747. CYT_DCMP_DEAMINASES_2. 2 hits.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiCDD_ECOLI
AccessioniPrimary (citable) accession number: P0ABF6
Secondary accession number(s): P13652, Q2MAT6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 25, 2005
Last sequence update: October 25, 2005
Last modified: November 2, 2016
This is version 96 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Escherichia coli
    Escherichia coli (strain K12): entries and cross-references to EcoGene
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.