ID   LOGL2_ORYSJ             Reviewed;         244 AA.
AC   B9F166; A0A0P0VLX1;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   24-MAR-2009, sequence version 1.
DT   03-AUG-2022, entry version 59.
DE   RecName: Full=Probable cytokinin riboside 5'-monophosphate phosphoribohydrolase LOGL2;
DE            EC=3.2.2.n1;
DE   AltName: Full=Protein LONELY GUY-like 2;
GN   Name=LOGL2; OrderedLocusNames=Os02g0628000, LOC_Os02g41770;
GN   ORFNames=OsJ_07599;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [5]
RP   GENE FAMILY, AND NOMENCLATURE.
RX   PubMed=19837870; DOI=10.1105/tpc.109.068676;
RA   Kuroha T., Tokunaga H., Kojima M., Ueda N., Ishida T., Nagawa S.,
RA   Fukuda H., Sugimoto K., Sakakibara H.;
RT   "Functional analyses of LONELY GUY cytokinin-activating enzymes reveal the
RT   importance of the direct activation pathway in Arabidopsis.";
RL   Plant Cell 21:3152-3169(2009).
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 (By similarity).
CC       {ECO:0000250}.
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   -!- 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   -!- SIMILARITY: Belongs to the LOG family. {ECO:0000305}.
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DR   EMBL; AP008208; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AP014958; BAS79874.1; -; Genomic_DNA.
DR   EMBL; CM000139; EEE57408.1; -; Genomic_DNA.
DR   RefSeq; XP_015622862.1; XM_015767376.1.
DR   AlphaFoldDB; B9F166; -.
DR   SMR; B9F166; -.
DR   STRING; 4530.OS02T0628000-00; -.
DR   PaxDb; B9F166; -.
DR   PRIDE; B9F166; -.
DR   EnsemblPlants; Os02t0628000-00; Os02t0628000-00; Os02g0628000.
DR   GeneID; 107275650; -.
DR   Gramene; Os02t0628000-00; Os02t0628000-00; Os02g0628000.
DR   KEGG; osa:107275650; -.
DR   eggNOG; ENOG502QSR9; Eukaryota.
DR   HOGENOM; CLU_058336_2_0_1; -.
DR   InParanoid; B9F166; -.
DR   OMA; TLVWGGS; -.
DR   OrthoDB; 979502at2759; -.
DR   Proteomes; UP000000763; Chromosome 2.
DR   Proteomes; UP000007752; Chromosome 2.
DR   Proteomes; UP000059680; Chromosome 2.
DR   Genevisible; B9F166; OS.
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   InterPro; IPR005269; LOG.
DR   InterPro; IPR031100; LOG_fam.
DR   Pfam; PF03641; Lysine_decarbox; 1.
DR   TIGRFAMs; TIGR00730; TIGR00730; 1.
PE   3: Inferred from homology;
KW   Cytokinin biosynthesis; Hydrolase; Reference proteome.
FT   CHAIN           1..244
FT                   /note="Probable cytokinin riboside 5'-monophosphate
FT                   phosphoribohydrolase LOGL2"
FT                   /id="PRO_0000395054"
FT   BINDING         91
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B2HS63"
FT   BINDING         109..110
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B2HS63"
FT   BINDING         126..132
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B2HS63"
SQ   SEQUENCE   244 AA;  27246 MW;  A8E833E5728F8142 CRC64;
     MEIKDEETTA EVAMVVQSRF RRVCVFCGSS HGKKKIYQDA AIELGKELVA RNIDLVYGGG
     SVGLMGLVSQ AVHNGGRHVI GVIPKTLMPR EISGETVGEV KAVSDMHQRK AEMARQSDAF
     IALPGGYGTL EELLEVIAWA QLGIHDKPVG LLNVDGYYNP LLSFIDKAVE EGFIRPSARH
     IIVLAPTPKE LIEKLEEYSP QHEKVVSKMK WEMEQMSYPQ NYDIPRPKEG KMIIEAQRGS
     RLWM