(data stored in SCRATCH zone)

SWISSPROT: D6XX75_BACIE

ID   D6XX75_BACIE            Unreviewed;       132 AA.
AC   D6XX75;
DT   10-AUG-2010, integrated into UniProtKB/TrEMBL.
DT   10-AUG-2010, sequence version 1.
DT   08-MAY-2019, entry version 53.
DE   RecName: Full=Cytidine deaminase {ECO:0000256|RuleBase:RU364006};
DE            EC=3.5.4.5 {ECO:0000256|RuleBase:RU364006};
DE   AltName: Full=Cytidine aminohydrolase {ECO:0000256|RuleBase:RU364006};
GN   OrderedLocusNames=Bsel_0392 {ECO:0000313|EMBL:ADH97932.1};
OS   Bacillus selenitireducens (strain ATCC 700615 / DSM 15326 / MLS10).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Sporolactobacillaceae;
OC   unclassified Sporolactobacillaceae.
OX   NCBI_TaxID=439292 {ECO:0000313|EMBL:ADH97932.1, ECO:0000313|Proteomes:UP000000271};
RN   [1] {ECO:0000313|EMBL:ADH97932.1, ECO:0000313|Proteomes:UP000000271}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700615 / DSM 15326 / MLS10
RC   {ECO:0000313|Proteomes:UP000000271};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E.,
RA   Tice H., Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T.,
RA   Detter J.C., Han C., Larimer F., Land M., Hauser L., Kyrpides N.,
RA   Ovchinnikova G., Stolz J.;
RT   "Complete sequence of Bacillus selenitireducens MLS10.";
RL   Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: This enzyme scavenges exogenous and endogenous cytidine
CC       and 2'-deoxycytidine for UMP synthesis.
CC       {ECO:0000256|RuleBase:RU364006}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=2'-deoxycytidine + H(+) + H2O = 2'-deoxyuridine + NH4(+);
CC         Xref=Rhea:RHEA:13433, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15698, ChEBI:CHEBI:16450, ChEBI:CHEBI:28938;
CC         EC=3.5.4.5; Evidence={ECO:0000256|RuleBase:RU364006};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=cytidine + H(+) + H2O = NH4(+) + uridine;
CC         Xref=Rhea:RHEA:16069, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:16704, ChEBI:CHEBI:17562, ChEBI:CHEBI:28938;
CC         EC=3.5.4.5; Evidence={ECO:0000256|RuleBase:RU364006};
CC   -!- COFACTOR:
CC       Name=Zn(2+); Xref=ChEBI:CHEBI:29105;
CC         Evidence={ECO:0000256|RuleBase:RU364006};
CC   -!- SIMILARITY: Belongs to the cytidine and deoxycytidylate deaminase
CC       family. {ECO:0000256|RuleBase:RU364006}.
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DR   EMBL; CP001791; ADH97932.1; -; Genomic_DNA.
DR   RefSeq; WP_013171361.1; NC_014219.1.
DR   STRING; 439292.Bsel_0392; -.
DR   EnsemblBacteria; ADH97932; ADH97932; Bsel_0392.
DR   KEGG; bse:Bsel_0392; -.
DR   eggNOG; COG0295; LUCA.
DR   HOGENOM; HOG000014707; -.
DR   KO; K01489; -.
DR   OMA; CGACRQS; -.
DR   OrthoDB; 1895660at2; -.
DR   BioCyc; BSEL439292:G1GLR-422-MONOMER; -.
DR   Proteomes; UP000000271; Chromosome.
DR   GO; GO:0004126; F:cytidine deaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
DR   InterPro; IPR016192; APOBEC/CMP_deaminase_Zn-bd.
DR   InterPro; IPR002125; CMP_dCMP_dom.
DR   InterPro; IPR006262; Cyt_deam_tetra.
DR   InterPro; IPR016193; Cytidine_deaminase-like.
DR   Pfam; PF00383; dCMP_cyt_deam_1; 1.
DR   SUPFAM; SSF53927; SSF53927; 1.
DR   TIGRFAMs; TIGR01354; cyt_deam_tetra; 1.
DR   PROSITE; PS00903; CYT_DCMP_DEAMINASES_1; 1.
DR   PROSITE; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; D6XX75.
DR   SWISS-2DPAGE; D6XX75.
KW   Complete proteome {ECO:0000313|Proteomes:UP000000271};
KW   Hydrolase {ECO:0000256|RuleBase:RU364006};
KW   Metal-binding {ECO:0000256|RuleBase:RU364006};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000271};
KW   Zinc {ECO:0000256|RuleBase:RU364006}.
FT   DOMAIN        1    130       CMP/dCMP-type deaminase.
FT                                {ECO:0000259|PROSITE:PS51747}.
SQ   SEQUENCE   132 AA;  14544 MW;  93D4D78DAD42B7E0 CRC64;
     MDKEQLMQQA RSIKQHAYVP YSKFPVGAAF LMTDDRVITG VNVENVSFGA TNCAERTAMF
     TAMAEGYQKG DFKAVAVAGD TEDFLPPCAI CRQVMAELCP PDMPIYLTNA KGEISTHTLR
     EILPLAFTDL DM
//

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