(data stored in ACNUC7421 zone)

SWISSPROT: B2TFC6_PARPJ

ID   B2TFC6_PARPJ            Unreviewed;       129 AA.
AC   B2TFC6;
DT   01-JUL-2008, integrated into UniProtKB/TrEMBL.
DT   01-JUL-2008, sequence version 1.
DT   08-MAY-2019, entry version 65.
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=Bphyt_4421 {ECO:0000313|EMBL:ACD18797.1};
OS   Paraburkholderia phytofirmans (strain DSM 17436 / LMG 22146 / PsJN)
OS   (Burkholderia phytofirmans).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Paraburkholderia.
OX   NCBI_TaxID=398527 {ECO:0000313|EMBL:ACD18797.1, ECO:0000313|Proteomes:UP000001739};
RN   [1] {ECO:0000313|EMBL:ACD18797.1, ECO:0000313|Proteomes:UP000001739}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17436 / LMG 22146 / PsJN
RC   {ECO:0000313|Proteomes:UP000001739};
RX   PubMed=21551308; DOI=10.1128/JB.05055-11;
RA   Weilharter A., Mitter B., Shin M.V., Chain P.S., Nowak J.,
RA   Sessitsch A.;
RT   "Complete genome sequence of the plant growth-promoting endophyte
RT   Burkholderia phytofirmans strain PsJN.";
RL   J. Bacteriol. 193:3383-3384(2011).
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; CP001053; ACD18797.1; -; Genomic_DNA.
DR   RefSeq; WP_012426313.1; NC_010676.1.
DR   STRING; 398527.Bphyt_4421; -.
DR   EnsemblBacteria; ACD18797; ACD18797; Bphyt_4421.
DR   KEGG; bpy:Bphyt_4421; -.
DR   eggNOG; ENOG4105KG3; Bacteria.
DR   eggNOG; COG0295; LUCA.
DR   HOGENOM; HOG000014707; -.
DR   KO; K01489; -.
DR   OMA; AVYMTKP; -.
DR   OrthoDB; 1895660at2; -.
DR   BioCyc; BPHY398527:GJEX-4411-MONOMER; -.
DR   Proteomes; UP000001739; Chromosome 2.
DR   GO; GO:0004126; F:cytidine deaminase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008270; F:zinc ion binding; IEA:UniProtKB-UniRule.
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; PS51747; CYT_DCMP_DEAMINASES_2; 1.
PE   3: Inferred from homology;
DR   PRODOM; B2TFC6.
DR   SWISS-2DPAGE; B2TFC6.
KW   Complete proteome {ECO:0000313|Proteomes:UP000001739};
KW   Hydrolase {ECO:0000256|RuleBase:RU364006};
KW   Metal-binding {ECO:0000256|RuleBase:RU364006};
KW   Zinc {ECO:0000256|RuleBase:RU364006}.
FT   DOMAIN        1    129       CMP/dCMP-type deaminase.
FT                                {ECO:0000259|PROSITE:PS51747}.
SQ   SEQUENCE   129 AA;  13818 MW;  3E151C6F31F6C7CD CRC64;
     MNMEQLLERA GVAREKAYAP YSKFKVGAAL LTKDGQVFDG CNVENASYGL CNCAERTAFF
     SAIAAGYQRD QFAALAVIGD TDGPIAPCGA CRQVIIELGG PELPIRLGNL HGATRDTTAR
     EQLPDAFYL
//

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