(data stored in SCRATCH zone)

SWISSPROT: B8ICG3_METNO

ID   B8ICG3_METNO            Unreviewed;       142 AA.
AC   B8ICG3;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   07-JUN-2017, entry version 48.
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=Mnod_0510 {ECO:0000313|EMBL:ACL55551.1};
OS   Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales;
OC   Methylobacteriaceae; Methylobacterium.
OX   NCBI_TaxID=460265 {ECO:0000313|EMBL:ACL55551.1, ECO:0000313|Proteomes:UP000008207};
RN   [1] {ECO:0000313|EMBL:ACL55551.1, ECO:0000313|Proteomes:UP000008207}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060
RC   {ECO:0000313|Proteomes:UP000008207};
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   Ivanova N., Marx C.J., Richardson P.;
RT   "Complete sequence of chromosome of Methylobacterium nodulans ORS
RT   2060.";
RL   Submitted (JAN-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: 2'deoxycytidine + H(2)O = 2'-deoxyuridine +
CC       NH(3). {ECO:0000256|RuleBase:RU364006}.
CC   -!- CATALYTIC ACTIVITY: Cytidine + H(2)O = uridine + NH(3).
CC       {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; CP001349; ACL55551.1; -; Genomic_DNA.
DR   ProteinModelPortal; B8ICG3; -.
DR   STRING; 460265.Mnod_0510; -.
DR   EnsemblBacteria; ACL55551; ACL55551; Mnod_0510.
DR   KEGG; mno:Mnod_0510; -.
DR   eggNOG; ENOG4105KG3; Bacteria.
DR   eggNOG; COG0295; LUCA.
DR   HOGENOM; HOG000014707; -.
DR   KO; K01489; -.
DR   OMA; AVYMTKP; -.
DR   OrthoDB; POG091H026Y; -.
DR   Proteomes; UP000008207; 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; B8ICG3.
DR   SWISS-2DPAGE; B8ICG3.
KW   Complete proteome {ECO:0000313|Proteomes:UP000008207};
KW   Hydrolase {ECO:0000256|RuleBase:RU364006};
KW   Metal-binding {ECO:0000256|RuleBase:RU364006};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008207};
KW   Zinc {ECO:0000256|RuleBase:RU364006}.
FT   DOMAIN        9    136       CMP/dCMP-type deaminase.
FT                                {ECO:0000259|PROSITE:PS51747}.
SQ   SEQUENCE   142 AA;  14277 MW;  B688C7C621656D62 CRC64;
     MPTVPDRMSP IDALFSAALA VQARAHAPYS GFRVGAAVLD ETGAVHAGCN VENAAYPVGT
     CAEAGAIAAM VAGGGRRIAA ILVLGDGEAL VTPCGACRQR IREFAAPDAP VHVAGPEGLR
     RSFTLDALLP VSFGPDNLGV GA
//

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