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Database: UniProt
Entry: A0A0K9NNL0_ZOSMR
LinkDB: A0A0K9NNL0_ZOSMR
Original site: A0A0K9NNL0_ZOSMR 
ID   A0A0K9NNL0_ZOSMR        Unreviewed;       250 AA.
AC   A0A0K9NNL0;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   13-SEP-2023, entry version 25.
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   ORFNames=ZOSMA_77G00080 {ECO:0000313|EMBL:KMZ58351.1};
OS   Zostera marina (Eelgrass).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Zosteraceae; Zostera.
OX   NCBI_TaxID=29655 {ECO:0000313|EMBL:KMZ58351.1, ECO:0000313|Proteomes:UP000036987};
RN   [1] {ECO:0000313|Proteomes:UP000036987}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Finnish {ECO:0000313|Proteomes:UP000036987};
RX   PubMed=26814964; DOI=10.1038/nature16548;
RA   Olsen J.L., Rouze P., Verhelst B., Lin Y.-C., Bayer T., Collen J.,
RA   Dattolo E., De Paoli E., Dittami S., Maumus F., Michel G., Kersting A.,
RA   Lauritano C., Lohaus R., Toepel M., Tonon T., Vanneste K., Amirebrahimi M.,
RA   Brakel J., Bostroem C., Chovatia M., Grimwood J., Jenkins J.W.,
RA   Jueterbock A., Mraz A., Stam W.T., Tice H., Bornberg-Bauer E., Green P.J.,
RA   Pearson G.A., Procaccini G., Duarte C.M., Schmutz J., Reusch T.B.H.,
RA   Van de Peer Y.;
RT   "The genome of the seagrass Zostera marina reveals angiosperm adaptation to
RT   the sea.";
RL   Nature 530:331-335(2016).
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|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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KMZ58351.1}.
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DR   EMBL; LFYR01001945; KMZ58351.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0K9NNL0; -.
DR   STRING; 29655.A0A0K9NNL0; -.
DR   OMA; GKRECYR; -.
DR   OrthoDB; 462759at2759; -.
DR   Proteomes; UP000036987; Unassembled WGS sequence.
DR   GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR   GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR   GO; GO:0016799; F:hydrolase activity, hydrolyzing N-glycosyl compounds; IBA:GO_Central.
DR   GO; GO:0102682; F:N6-(Delta2-isopentenyl)-adenosine 5'-monophosphate phosphoribohydrolase activity; IEA:RHEA.
DR   GO; GO:0009691; P:cytokinin biosynthetic process; IBA:GO_Central.
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:SF14; CYTOKININ RIBOSIDE 5'-MONOPHOSPHATE PHOSPHORIBOHYDROLASE LOG5; 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:UP000036987}.
SQ   SEQUENCE   250 AA;  27142 MW;  5FB5D18CF74325A7 CRC64;
     MSLEMGEVHN PDKVVVDQDI LNTNNINNDT AEMGSERGCS RFKRICVFGG SSSGKKDCYQ
     DAAVDLGKEL VSRKVDLVYG GGSIGLMGLV SQAVHQGGGY VIGIIPTSLI GKEITGETVG
     ELKVVTGMHQ RKAEMSHQSD AFIALPGGYG TMEELLEVIS WAQLGIHNKP VGLLNVDGYY
     NSLLDFIDKA VDDGFIKPYQ RQIIISSPDP KDLLQKLEEH VPVQDGAVAK LRWEIQHAGY
     NSSLLVEIGR
//
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