LOG7_ARATH
ID LOG7_ARATH Reviewed; 217 AA.
AC Q8GW29; Q9FNH8;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 15-JUN-2010, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Cytokinin riboside 5'-monophosphate phosphoribohydrolase LOG7;
DE EC=3.2.2.n1;
DE AltName: Full=Protein LONELY GUY 7;
GN Name=LOG7; OrderedLocusNames=At5g06300; ORFNames=MHF15.18;
OS Arabidopsis thaliana (Mouse-ear cress).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Brassicales; Brassicaceae; Camelineae; Arabidopsis.
OX NCBI_TaxID=3702;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=9405937; DOI=10.1093/dnares/4.4.291;
RA Kotani H., Nakamura Y., Sato S., Kaneko T., Asamizu E., Miyajima N.,
RA Tabata S.;
RT "Structural analysis of Arabidopsis thaliana chromosome 5. II. Sequence
RT features of the regions of 1,044,062 bp covered by thirteen physically
RT assigned P1 clones.";
RL DNA Res. 4:291-300(1997).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=cv. Columbia;
RX PubMed=27862469; DOI=10.1111/tpj.13415;
RA Cheng C.Y., Krishnakumar V., Chan A.P., Thibaud-Nissen F., Schobel S.,
RA Town C.D.;
RT "Araport11: a complete reannotation of the Arabidopsis thaliana reference
RT genome.";
RL Plant J. 89:789-804(2017).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4-217.
RC STRAIN=cv. Columbia;
RX PubMed=11910074; DOI=10.1126/science.1071006;
RA Seki M., Narusaka M., Kamiya A., Ishida J., Satou M., Sakurai T.,
RA Nakajima M., Enju A., Akiyama K., Oono Y., Muramatsu M., Hayashizaki Y.,
RA Kawai J., Carninci P., Itoh M., Ishii Y., Arakawa T., Shibata K.,
RA Shinagawa A., Shinozaki K.;
RT "Functional annotation of a full-length Arabidopsis cDNA collection.";
RL Science 296:141-145(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 53-217.
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [5]
RP IDENTIFICATION.
RX PubMed=17287810; DOI=10.1038/nature05504;
RA Kurakawa T., Ueda N., Maekawa M., Kobayashi K., Kojima M., Nagato Y.,
RA Sakakibara H., Kyozuka J.;
RT "Direct control of shoot meristem activity by a cytokinin-activating
RT enzyme.";
RL Nature 445:652-655(2007).
RN [6]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, DISRUPTION
RP PHENOTYPE, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, GENE FAMILY, AND
RP 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.
CC {ECO:0000269|PubMed:19837870}.
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:0000269|PubMed:19837870};
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:0000269|PubMed:19837870};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.7 uM for N(6)-(Delta(2)-isopentenyl)-adenosine 5'-phosphate
CC {ECO:0000269|PubMed:19837870};
CC Vmax=3.8 umol/min/mg enzyme with N(6)-(Delta(2)-isopentenyl)-
CC adenosine 5'-phosphate as substrate {ECO:0000269|PubMed:19837870};
CC Note=can also use benzyladenosine 5'-phosphate as substrate.;
CC pH dependence:
CC Optimum pH is 6.5. {ECO:0000269|PubMed:19837870};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19837870}. Nucleus
CC {ECO:0000269|PubMed:19837870}.
CC -!- TISSUE SPECIFICITY: Expressed in roots and shoots. Detected in the
CC epidermis of the root elongation zone, cotyledon and leaves, in
CC trichomes and pollen. {ECO:0000269|PubMed:19837870}.
CC -!- DISRUPTION PHENOTYPE: No visible phenotype under normal growth
CC conditions; due to the redundancy with other LOG proteins.
CC {ECO:0000269|PubMed:19837870}.
CC -!- SIMILARITY: Belongs to the LOG family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC43688.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AB006700; BAB08952.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91000.1; -; Genomic_DNA.
DR EMBL; AK119117; BAC43688.1; ALT_INIT; mRNA.
DR EMBL; BT003704; AAO39932.1; -; mRNA.
DR RefSeq; NP_196248.3; NM_120713.5.
DR AlphaFoldDB; Q8GW29; -.
DR SMR; Q8GW29; -.
DR BioGRID; 15797; 1.
DR STRING; 3702.AT5G06300.1; -.
DR PaxDb; Q8GW29; -.
DR PRIDE; Q8GW29; -.
DR ProteomicsDB; 238472; -.
DR EnsemblPlants; AT5G06300.1; AT5G06300.1; AT5G06300.
DR GeneID; 830518; -.
DR Gramene; AT5G06300.1; AT5G06300.1; AT5G06300.
DR KEGG; ath:AT5G06300; -.
DR Araport; AT5G06300; -.
DR TAIR; locus:2164280; AT5G06300.
DR eggNOG; ENOG502QSX6; Eukaryota.
DR HOGENOM; CLU_058336_2_0_1; -.
DR OMA; IWDEGIQ; -.
DR OrthoDB; 979502at2759; -.
DR PhylomeDB; Q8GW29; -.
DR BioCyc; ARA:AT5G06300-MON; -.
DR PRO; PR:Q8GW29; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q8GW29; baseline and differential.
DR Genevisible; Q8GW29; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
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 1: Evidence at protein level;
KW Cytokinin biosynthesis; Cytoplasm; Hydrolase; Nucleus; Reference proteome.
FT CHAIN 1..217
FT /note="Cytokinin riboside 5'-monophosphate
FT phosphoribohydrolase LOG7"
FT /id="PRO_0000395050"
FT BINDING 79
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B2HS63"
FT BINDING 97..98
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B2HS63"
FT BINDING 114..120
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B2HS63"
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B2HS63"
SQ SEQUENCE 217 AA; 23889 MW; 8DC0DCA2D1622939 CRC64;
MEETKSRFKR ICVFCGSSSG KKPSYQEAAI QLGNELVERR IDLVYGGGSV GLMGLVSQAV
HHGGRHVLGV IPKTLMPREI TGETIGEVKA VADMHQRKAE MARQADAFIA LPGGYGTLEE
LLEVITWAQL GIHRKPVGLL NVDGYYNSLL TFIDKAVDEG FISPMARRII VSAPNAKELV
RQLEEYEPEF DEITSKLVWD EVDRISYVPG SEVATAT
