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Protein

Cytidine deaminase

Gene

cdd

Organism
Bacillus subtilis (strain 168)
Status
Reviewed-Annotation score: -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.
2'-deoxycytidine + H2O = 2'-deoxyuridine + NH3.

Cofactori

Zn2+Note: Binds 1 zinc ion per subunit.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi53Zinc; catalytic1
Active sitei55Proton donor1
Metal bindingi86Zinc; catalytic1
Metal bindingi89Zinc; catalytic1

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase
LigandMetal-binding, Zinc

Enzyme and pathway databases

BioCyciBSUB:BSU25300-MONOMER
MetaCyc:BSU25300-MONOMER
BRENDAi3.5.4.5 658

Names & Taxonomyi

Protein namesi
Recommended name:
Cytidine deaminase (EC:3.5.4.5)
Short name:
CDA
Alternative name(s):
Cytidine aminohydrolase
Gene namesi
Name:cdd
Ordered Locus Names:BSU25300
OrganismiBacillus subtilis (strain 168)
Taxonomic identifieri224308 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeBacillus
Proteomesi
  • UP000001570 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi53C → H: Loss of activity. Reduces activity 500-fold, without effect on zinc binding; when associated with Q-56. 1 Publication1
Mutagenesisi56R → A: No effect on zinc binding. Strongly reduces Vmax. 1 Publication1
Mutagenesisi56R → D: Loss of activity. Reduces zinc binding by 80%. 1 Publication1
Mutagenesisi56R → Q: No effect on zinc binding. Strongly reduces Vmax. Reduces activity 500-fold; when associated with H-53. 1 Publication1

Chemistry databases

DrugBankiDB03562 Tetrahydrodeoxyuridine

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001716781 – 136Cytidine deaminaseAdd BLAST136

Proteomic databases

PaxDbiP19079
PRIDEiP19079

Interactioni

Subunit structurei

Homotetramer.2 Publications

Protein-protein interaction databases

STRINGi224308.Bsubs1_010100013836

Structurei

Secondary structure

1136
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi3 – 14Combined sources12
Turni20 – 22Combined sources3
Beta strandi26 – 32Combined sources7
Beta strandi37 – 41Combined sources5
Helixi48 – 50Combined sources3
Helixi54 – 64Combined sources11
Beta strandi70 – 78Combined sources9
Beta strandi80 – 82Combined sources3
Helixi87 – 96Combined sources10
Beta strandi102 – 106Combined sources5
Beta strandi108 – 110Combined sources3
Beta strandi112 – 116Combined sources5
Helixi117 – 120Combined sources4
Helixi127 – 129Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1JTKX-ray2.04A/B1-136[»]
1UWZX-ray1.99A/B1-136[»]
1UX0X-ray1.99A/B1-136[»]
1UX1X-ray2.36A/B/C/D1-136[»]
ProteinModelPortaliP19079
SMRiP19079
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP19079

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1 – 128CMP/dCMP-type deaminasePROSITE-ProRule annotationAdd BLAST128

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni42 – 44Substrate binding3

Sequence similaritiesi

Phylogenomic databases

eggNOGiENOG4105KG3 Bacteria
COG0295 LUCA
HOGENOMiHOG000014707
InParanoidiP19079
KOiK01489
OMAiNQENASY
PhylomeDBiP19079

Family and domain databases

InterProiView protein in InterPro
IPR016192 APOBEC/CMP_deaminase_Zn-bd
IPR002125 CMP_dCMP_dom
IPR006262 Cyt_deam_tetra
IPR016193 Cytidine_deaminase-like
PfamiView protein in Pfam
PF00383 dCMP_cyt_deam_1, 1 hit
SUPFAMiSSF53927 SSF53927, 1 hit
TIGRFAMsiTIGR01354 cyt_deam_tetra, 1 hit
PROSITEiView protein in PROSITE
PS00903 CYT_DCMP_DEAMINASES_1, 1 hit
PS51747 CYT_DCMP_DEAMINASES_2, 1 hit

Sequencei

Sequence statusi: Complete.

P19079-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNRQELITEA LKARDMAYAP YSKFQVGAAL LTKDGKVYRG CNIENAAYSM
60 70 80 90 100
CNCAERTALF KAVSEGDTEF QMLAVAADTP GPVSPCGACR QVISELCTKD
110 120 130
VIVVLTNLQG QIKEMTVEEL LPGAFSSEDL HDERKL
Length:136
Mass (Da):14,854
Last modified:November 1, 1990 - v1
Checksum:i83755B1CDB2A534A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U18532 Genomic DNA Translation: AAB59993.1
X17430 Genomic DNA Translation: CAB57856.1
D84432 Genomic DNA Translation: BAA12481.1
K02174 Genomic DNA Translation: AAB05347.1
AL009126 Genomic DNA Translation: CAB14459.1
U29177 Genomic DNA Translation: AAA70045.1
PIRiJE0022
RefSeqiNP_390408.1, NC_000964.3
WP_003230049.1, NZ_JNCM01000036.1

Genome annotation databases

EnsemblBacteriaiCAB14459; CAB14459; BSU25300
GeneIDi937885
KEGGibsu:BSU25300
PATRICifig|224308.179.peg.2750

Similar proteinsi

Entry informationi

Entry nameiCDD_BACSU
AccessioniPrimary (citable) accession number: P19079
Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: May 23, 2018
This is version 140 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Bacillus subtilis
    Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

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