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Reviewed, UniProtKB/Swiss-Prot P19079 (CDD_BACSU)

Last modified February 9, 2010. Version 89. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Cytidine deaminase
      Short name=CDA
    EC=3.5.4.5
Alternative name(s):
    Cytidine aminohydrolase
Gene names
Name: cdd
Ordered Locus Names: BSU25300
OrganismBacillus subtilis [Complete proteome] [HAMAP]
Taxonomic identifier1423 [NCBI]
Taxonomic lineageBacteriaFirmicutesBacillalesBacillaceaeBacillus

Protein attributes

Sequence length136 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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

Catalytic activity

Cytidine + H2O = uridine + NH3.

Cofactor

Binds 1 zinc ion per subunit.

Subunit structure

Homotetramer. Ref.5 Ref.6

Sequence similarities

Belongs to the cytidine and deoxycytidylate deaminase family.

Ontologies

Keywords
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processcytidine metabolic process

Inferred from electronic annotation. Source: InterPro

   Molecular functioncytidine deaminase activity

Inferred from electronic annotation. Source: EC

zinc ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 136136Cytidine deaminase
PRO_0000171678

Regions

Region42 – 443Substrate binding

Sites

Active site551Proton donor
Metal binding531Zinc; catalytic
Metal binding861Zinc; catalytic
Metal binding891Zinc; catalytic

Experimental info

Mutagenesis531C → H: Loss of activity. Reduces activity 500-fold, without effect on zinc binding; when associated with Q-56. Ref.6
Mutagenesis561R → A: No effect on zinc binding. Strongly reduces Vmax. Ref.6
Mutagenesis561R → D: Loss of activity. Reduces zinc binding by 80%. Ref.6
Mutagenesis561R → Q: No effect on zinc binding. Strongly reduces Vmax. Reduces activity 500-fold; when associated with H-53. Ref.6

Secondary structure

............................ 136
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P19079-1 [UniParc].

Last modified November 1, 1990. Version 1.
Checksum: 83755B1CDB2A534A

FASTA13614,854
        10         20         30         40         50         60 
MNRQELITEA LKARDMAYAP YSKFQVGAAL LTKDGKVYRG CNIENAAYSM CNCAERTALF 

        70         80         90        100        110        120 
KAVSEGDTEF QMLAVAADTP GPVSPCGACR QVISELCTKD VIVVLTNLQG QIKEMTVEEL 

       130 
LPGAFSSEDL HDERKL 

« Hide

References

« Hide 'large scale' references
[1]"Chromosomal location, cloning and nucleotide sequence of the Bacillus subtilis cdd gene encoding cytidine/deoxycytidine deaminase."
Song B.-H., Neuhard J.
Mol. Gen. Genet. 216:462-468(1989) [PubMed: 2526291] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168.
[2]"Systematic sequencing of the 283 kb 210 degrees-232 degrees region of the Bacillus subtilis genome containing the skin element and many sporulation genes."
Mizuno M., Masuda S., Takemaru K., Hosono S., Sato T., Takeuchi M., Kobayashi Y.
Microbiology 142:3103-3111(1996) [PubMed: 8969508] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: 168 / JH642.
[3]"The complete genome sequence of the Gram-positive bacterium Bacillus subtilis."
Kunst F., Ogasawara N., Moszer I., Albertini A.M., Alloni G., Azevedo V., Bertero M.G., Bessieres P., Bolotin A., Borchert S., Borriss R., Boursier L., Brans A., Braun M., Brignell S.C., Bron S., Brouillet S., Bruschi C.V. expand/collapse author list , Caldwell B., Capuano V., Carter N.M., Choi S.-K., Codani J.-J., Connerton I.F., Cummings N.J., Daniel R.A., Denizot F., Devine K.M., Duesterhoeft A., Ehrlich S.D., Emmerson P.T., Entian K.-D., Errington J., Fabret C., Ferrari E., Foulger D., Fritz C., Fujita M., Fujita Y., Fuma S., Galizzi A., Galleron N., Ghim S.-Y., Glaser P., Goffeau A., Golightly E.J., Grandi G., Guiseppi G., Guy B.J., Haga K., Haiech J., Harwood C.R., Henaut A., Hilbert H., Holsappel S., Hosono S., Hullo M.-F., Itaya M., Jones L.-M., Joris B., Karamata D., Kasahara Y., Klaerr-Blanchard M., Klein C., Kobayashi Y., Koetter P., Koningstein G., Krogh S., Kumano M., Kurita K., Lapidus A., Lardinois S., Lauber J., Lazarevic V., Lee S.-M., Levine A., Liu H., Masuda S., Mauel C., Medigue C., Medina N., Mellado R.P., Mizuno M., Moestl D., Nakai S., Noback M., Noone D., O'Reilly M., Ogawa K., Ogiwara A., Oudega B., Park S.-H., Parro V., Pohl T.M., Portetelle D., Porwollik S., Prescott A.M., Presecan E., Pujic P., Purnelle B., Rapoport G., Rey M., Reynolds S., Rieger M., Rivolta C., Rocha E., Roche B., Rose M., Sadaie Y., Sato T., Scanlan E., Schleich S., Schroeter R., Scoffone F., Sekiguchi J., Sekowska A., Seror S.J., Serror P., Shin B.-S., Soldo B., Sorokin A., Tacconi E., Takagi T., Takahashi H., Takemaru K., Takeuchi M., Tamakoshi A., Tanaka T., Terpstra P., Tognoni A., Tosato V., Uchiyama S., Vandenbol M., Vannier F., Vassarotti A., Viari A., Wambutt R., Wedler E., Wedler H., Weitzenegger T., Winters P., Wipat A., Yamamoto H., Yamane K., Yasumoto K., Yata K., Yoshida K., Yoshikawa H.-F., Zumstein E., Yoshikawa H., Danchin A.
Nature 390:249-256(1997) [PubMed: 9384377] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 168.
[4]"Nucleotide sequence upstream of the cdd locus in Bacillus subtilis."
Kim K., Hwang S., Suh J., Song B.-H., Hong S., Kim J.
Submitted (JUL-1995) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-10.
Strain: ED40.
[5]"Crystal structure of the tetrameric cytidine deaminase from Bacillus subtilis at 2.0 A resolution."
Johansson E., Mejlhede N., Neuhard J., Larsen S.
Biochemistry 41:2563-2570(2002) [PubMed: 11851403] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH SUBSTRATE ANALOG AND ZINC IONS, SUBUNIT.
[6]"Structural, kinetic, and mutational studies of the zinc ion environment in tetrameric cytidine deaminase."
Johansson E., Neuhard J., Willemoes M., Larsen S.
Biochemistry 43:6020-6029(2004) [PubMed: 15147186] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) OF MUTANTS IN COMPLEX WITH SUBSTRATE ANALOG AND ZINC IONS, SUBUNIT, MUTAGENESIS OF CYS-53 AND ARG-56.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRJE0022.
RefSeqNP_390408.1.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ModBaseSearch...

Genome annotation databases

GeneID937885.
GenomeReviewsGene locus BSU25300 in contig AL009126_GR.
KEGGbsu:BSU25300.
NMPDRfig|224308.1.peg.2533.

Organism-specific databases

SubtiListBG10477. cdd. [Micado]
CMRSearch...

Phylogenomic databases

HOGENOMHBG352939.
OMANTSPEAI.
PhylomeDBP19079.

Enzyme and pathway databases

BRENDA3.5.4.5. 150.

Family and domain databases

InterProIPR016192. APOBEC/CMP_deaminase_Zn-bd.
IPR002125. CMP_dCMP_Zn_bd.
IPR006262. Cyt_deam_tetra.
IPR016193. Cytidine_deaminase-like.
[Graphical view]
PANTHERPTHR11644:SF2. Cyt_deam_tetra. 1 hit.
PfamPF00383. dCMP_cyt_deam_1. 1 hit.
[Graphical view]
TIGRFAMsTIGR01354. cyt_deam_tetra. 1 hit.
PROSITEPS00903. CYT_DCMP_DEAMINASES. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameCDD_BACSU
AccessionPrimary (citable) accession number: P19079
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: November 1, 1990
Last modified: February 9, 2010
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

Bacillus subtilis

Bacillus subtilis (strain 168): entries, gene names and cross-references to SubtiList

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents