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Database: UniProt
Entry: Q7VS93_BORPE
LinkDB: Q7VS93_BORPE
Original site: Q7VS93_BORPE 
ID   Q7VS93_BORPE            Unreviewed;       195 AA.
AC   Q7VS93;
DT   01-OCT-2003, integrated into UniProtKB/TrEMBL.
DT   01-OCT-2003, sequence version 1.
DT   27-MAR-2024, entry version 86.
DE   RecName: Full=Cytokinin riboside 5'-monophosphate phosphoribohydrolase {ECO:0000256|RuleBase:RU363015};
DE            EC=3.2.2.n1 {ECO:0000256|RuleBase:RU363015};
GN   OrderedLocusNames=BP0547 {ECO:0000313|EMBL:CAE44875.1};
OS   Bordetella pertussis (strain Tohama I / ATCC BAA-589 / NCTC 13251).
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Alcaligenaceae; Bordetella.
OX   NCBI_TaxID=257313 {ECO:0000313|EMBL:CAE44875.1, ECO:0000313|Proteomes:UP000002676};
RN   [1] {ECO:0000313|EMBL:CAE44875.1, ECO:0000313|Proteomes:UP000002676}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Tohama I / ATCC BAA-589 / NCTC 13251
RC   {ECO:0000313|Proteomes:UP000002676};
RX   PubMed=12910271; DOI=10.1038/ng1227;
RA   Parkhill J., Sebaihia M., Preston A., Murphy L.D., Thomson N.R.,
RA   Harris D.E., Holden M.T.G., Churcher C.M., Bentley S.D., Mungall K.L.,
RA   Cerdeno-Tarraga A.-M., Temple L., James K.D., Harris B., Quail M.A.,
RA   Achtman M., Atkin R., Baker S., Basham D., Bason N., Cherevach I.,
RA   Chillingworth T., Collins M., Cronin A., Davis P., Doggett J., Feltwell T.,
RA   Goble A., Hamlin N., Hauser H., Holroyd S., Jagels K., Leather S.,
RA   Moule S., Norberczak H., O'Neil S., Ormond D., Price C., Rabbinowitsch E.,
RA   Rutter S., Sanders M., Saunders D., Seeger K., Sharp S., Simmonds M.,
RA   Skelton J., Squares R., Squares S., Stevens K., Unwin L., Whitehead S.,
RA   Barrell B.G., Maskell D.J.;
RT   "Comparative analysis of the genome sequences of Bordetella pertussis,
RT   Bordetella parapertussis and Bordetella bronchiseptica.";
RL   Nat. Genet. 35:32-40(2003).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=AMP + H2O = adenine + D-ribose 5-phosphate;
CC         Xref=Rhea:RHEA:20129, ChEBI:CHEBI:15377, ChEBI:CHEBI:16708,
CC         ChEBI:CHEBI:78346, ChEBI:CHEBI:456215; EC=3.2.2.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00000274};
CC   -!- SIMILARITY: Belongs to the LOG family. {ECO:0000256|RuleBase:RU363015}.
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DR   EMBL; BX640412; CAE44875.1; -; Genomic_DNA.
DR   RefSeq; NP_879395.1; NC_002929.2.
DR   RefSeq; WP_010929870.1; NZ_CP039022.1.
DR   AlphaFoldDB; Q7VS93; -.
DR   STRING; 257313.BP0547; -.
DR   PaxDb; 257313-BP0547; -.
DR   GeneID; 69600273; -.
DR   KEGG; bpe:BP0547; -.
DR   PATRIC; fig|257313.5.peg.588; -.
DR   eggNOG; COG1611; Bacteria.
DR   HOGENOM; CLU_058336_4_2_4; -.
DR   Proteomes; UP000002676; Chromosome.
DR   GO; GO:0008714; F:AMP nucleosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009691; P:cytokinin biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.40.50.450; -; 1.
DR   InterPro; IPR005269; LOG.
DR   InterPro; IPR031100; LOG_fam.
DR   NCBIfam; TIGR00730; Rossman fold protein, TIGR00730 family; 1.
DR   PANTHER; PTHR31223; LOG FAMILY PROTEIN YJL055W; 1.
DR   PANTHER; PTHR31223:SF11; LOG FAMILY PROTEIN YJL055W; 1.
DR   Pfam; PF03641; Lysine_decarbox; 1.
DR   SUPFAM; SSF102405; MCP/YpsA-like; 1.
PE   3: Inferred from homology;
KW   Cytokinin biosynthesis {ECO:0000256|RuleBase:RU363015};
KW   Hydrolase {ECO:0000256|RuleBase:RU363015};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002676}.
SQ   SEQUENCE   195 AA;  21292 MW;  7A3074B15294AD52 CRC64;
     MKIQNICVYC GSNSGRQPEY IEHAQGFARE LVKRGLGLVY GGASVGIMGA VADTVMAEGG
     RVIGIIPEAL MKKELAHRGL TELHVVQSMH ERKTLMAQKA DGFVALPGGA GTLEEIFEIW
     TWAQLGMHQK PCGLLNIAGY YDLLGQFLNH TVDEAFMRPQ HRAMLAIDHD PAALLDHFAS
     YVAPTVSKWI APGEH
//
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