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Database: UniProt
Entry: A0A0D3E1A4_BRAOL
LinkDB: A0A0D3E1A4_BRAOL
Original site: A0A0D3E1A4_BRAOL 
ID   A0A0D3E1A4_BRAOL        Unreviewed;       207 AA.
AC   A0A0D3E1A4;
DT   29-APR-2015, integrated into UniProtKB/TrEMBL.
DT   29-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 33.
DE   RecName: Full=Cytokinin riboside 5'-monophosphate phosphoribohydrolase {ECO:0000256|ARBA:ARBA00012205, ECO:0000256|RuleBase:RU363015};
DE            EC=3.2.2.n1 {ECO:0000256|ARBA:ARBA00012205, ECO:0000256|RuleBase:RU363015};
GN   Name=106318615 {ECO:0000313|EnsemblPlants:Bo9g011090.1};
OS   Brassica oleracea var. oleracea.
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; malvids; Brassicales; Brassicaceae; Brassiceae; Brassica.
OX   NCBI_TaxID=109376 {ECO:0000313|EnsemblPlants:Bo9g011090.1, ECO:0000313|Proteomes:UP000032141};
RN   [1] {ECO:0000313|EnsemblPlants:Bo9g011090.1, ECO:0000313|Proteomes:UP000032141}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=cv. TO1000 {ECO:0000313|Proteomes:UP000032141};
RX   PubMed=24916971; DOI=10.1186/gb-2014-15-6-r77;
RA   Parkin I.A., Koh C., Tang H., Robinson S.J., Kagale S., Clarke W.E.,
RA   Town C.D., Nixon J., Krishnakumar V., Bidwell S.L., Denoeud F., Belcram H.,
RA   Links M.G., Just J., Clarke C., Bender T., Huebert T., Mason A.S.,
RA   Pires J.C., Barker G., Moore J., Walley P.G., Manoli S., Batley J.,
RA   Edwards D., Nelson M.N., Wang X., Paterson A.H., King G., Bancroft I.,
RA   Chalhoub B., Sharpe A.G.;
RT   "Transcriptome and methylome profiling reveals relics of genome dominance
RT   in the mesopolyploid Brassica oleracea.";
RL   Genome Biol. 15:R77-R77(2014).
RN   [2] {ECO:0000313|EnsemblPlants:Bo9g011090.1}
RP   IDENTIFICATION.
RG   EnsemblPlants;
RL   Submitted (MAR-2015) to UniProtKB.
CC   -!- FUNCTION: Cytokinin-activating enzyme working in the direct activation
CC       pathway. Phosphoribohydrolase that converts inactive cytokinin
CC       nucleotides to the biologically active free-base forms.
CC       {ECO:0000256|ARBA:ARBA00024884, ECO:0000256|RuleBase:RU363015}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=9-ribosyl-trans-zeatin 5'-phosphate + H2O = D-ribose 5-
CC         phosphate + trans-zeatin; Xref=Rhea:RHEA:48564, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:16522, ChEBI:CHEBI:78346, ChEBI:CHEBI:87947; EC=3.2.2.n1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000881,
CC         ECO:0000256|RuleBase:RU363015};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=H2O + N(6)-(dimethylallyl)adenosine 5'-phosphate = D-ribose 5-
CC         phosphate + N(6)-dimethylallyladenine; Xref=Rhea:RHEA:48560,
CC         ChEBI:CHEBI:15377, ChEBI:CHEBI:17660, ChEBI:CHEBI:57526,
CC         ChEBI:CHEBI:78346; EC=3.2.2.n1;
CC         Evidence={ECO:0000256|ARBA:ARBA00000894,
CC         ECO:0000256|RuleBase:RU363015};
CC   -!- SIMILARITY: Belongs to the LOG family. {ECO:0000256|ARBA:ARBA00006763,
CC       ECO:0000256|RuleBase:RU363015}.
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DR   RefSeq; XP_013612122.1; XM_013756668.1.
DR   AlphaFoldDB; A0A0D3E1A4; -.
DR   STRING; 109376.A0A0D3E1A4; -.
DR   EnsemblPlants; Bo9g011090.1; Bo9g011090.1; Bo9g011090.
DR   GeneID; 106318615; -.
DR   Gramene; Bo9g011090.1; Bo9g011090.1; Bo9g011090.
DR   eggNOG; ENOG502QTZZ; Eukaryota.
DR   HOGENOM; CLU_058336_2_0_1; -.
DR   OMA; MEQGFPK; -.
DR   OrthoDB; 122997at2759; -.
DR   Proteomes; UP000032141; Chromosome C9.
DR   GO; GO:0005829; C:cytosol; IEA:UniProt.
DR   GO; GO:0005634; C:nucleus; IEA:UniProt.
DR   GO; GO:0102682; F:N6-(Delta2-isopentenyl)-adenosine 5'-monophosphate phosphoribohydrolase activity; IEA:RHEA.
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:SF64; CYTOKININ RIBOSIDE 5'-MONOPHOSPHATE PHOSPHORIBOHYDROLASE; 1.
DR   PANTHER; PTHR31223; 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|ARBA:ARBA00022712,
KW   ECO:0000256|RuleBase:RU363015}; Hydrolase {ECO:0000256|RuleBase:RU363015};
KW   Reference proteome {ECO:0000313|Proteomes:UP000032141}.
SQ   SEQUENCE   207 AA;  22506 MW;  203F9F187D1088A3 CRC64;
     MEENKRFKKV CVFCGSNSGH RDVFSLAAIE LGNELVKRKI DLVYGGGSVG LMGLISRRVS
     EGGCHVLGII PQALMPIEIS GETVGEVRIV ADMHERKAAM AQEAEAFIAL PGGYGTMEEL
     LEIITWAQLG IHKKTVGLLN VDGYYNNLLA LFDTGVEEGF IKPGARNIVV SAPSAKELLE
     KMELYTPSHK HIASHQSWKV EQLAGDS
//
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