LOG1_ARATH
ID LOG1_ARATH Reviewed; 213 AA.
AC Q8RUN2; Q9ASW6;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=Cytokinin riboside 5'-monophosphate phosphoribohydrolase LOG1;
DE EC=3.2.2.n1;
DE AltName: Full=Protein LONELY GUY 1;
GN Name=LOG1; OrderedLocusNames=At2g28305; ORFNames=T1B3.18, T3B23.2;
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=10617197; DOI=10.1038/45471;
RA Lin X., Kaul S., Rounsley S.D., Shea T.P., Benito M.-I., Town C.D.,
RA Fujii C.Y., Mason T.M., Bowman C.L., Barnstead M.E., Feldblyum T.V.,
RA Buell C.R., Ketchum K.A., Lee J.J., Ronning C.M., Koo H.L., Moffat K.S.,
RA Cronin L.A., Shen M., Pai G., Van Aken S., Umayam L., Tallon L.J.,
RA Gill J.E., Adams M.D., Carrera A.J., Creasy T.H., Goodman H.M.,
RA Somerville C.R., Copenhaver G.P., Preuss D., Nierman W.C., White O.,
RA Eisen J.A., Salzberg S.L., Fraser C.M., Venter J.C.;
RT "Sequence and analysis of chromosome 2 of the plant Arabidopsis thaliana.";
RL Nature 402:761-768(1999).
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].
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Brover V.V., Troukhan M.E., Alexandrov N.A., Lu Y.-P., Flavell R.B.,
RA Feldmann K.A.;
RT "Full-length cDNA from Arabidopsis thaliana.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
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, TISSUE
RP SPECIFICITY, SUBCELLULAR LOCATION, 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.
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=16 uM for N(6)-(Delta(2)-isopentenyl)-adenosine 5'-phosphate
CC {ECO:0000269|PubMed:19837870};
CC Vmax=2.1 umol/min/mg enzyme with N(6)-(Delta(2)-isopentenyl)-
CC adenosine 5'-phosphate as substrate {ECO:0000269|PubMed:19837870};
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 vascular tissues of roots, cotyledons, leaves and pistils, in the shoot
CC apical meristem and in immature flowers. {ECO:0000269|PubMed:19837870}.
CC -!- SIMILARITY: Belongs to the LOG family. {ECO:0000305}.
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DR EMBL; AC006202; AAM15149.1; -; Genomic_DNA.
DR EMBL; AC006283; AAM15229.1; -; Genomic_DNA.
DR EMBL; CP002685; AEC08102.1; -; Genomic_DNA.
DR EMBL; AF361629; AAK32797.1; -; mRNA.
DR EMBL; AY081836; AAL87406.1; -; mRNA.
DR EMBL; AY086265; AAM64338.1; -; mRNA.
DR RefSeq; NP_565668.1; NM_128389.3.
DR AlphaFoldDB; Q8RUN2; -.
DR SMR; Q8RUN2; -.
DR BioGRID; 2726; 1.
DR STRING; 3702.AT2G28305.1; -.
DR PaxDb; Q8RUN2; -.
DR PRIDE; Q8RUN2; -.
DR ProteomicsDB; 238415; -.
DR EnsemblPlants; AT2G28305.1; AT2G28305.1; AT2G28305.
DR GeneID; 817376; -.
DR Gramene; AT2G28305.1; AT2G28305.1; AT2G28305.
DR KEGG; ath:AT2G28305; -.
DR Araport; AT2G28305; -.
DR TAIR; locus:2828223; AT2G28305.
DR eggNOG; ENOG502QSR9; Eukaryota.
DR HOGENOM; CLU_058336_2_0_1; -.
DR OMA; ICPNARQ; -.
DR OrthoDB; 979502at2759; -.
DR PhylomeDB; Q8RUN2; -.
DR PRO; PR:Q8RUN2; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8RUN2; baseline and differential.
DR Genevisible; Q8RUN2; 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..213
FT /note="Cytokinin riboside 5'-monophosphate
FT phosphoribohydrolase LOG1"
FT /id="PRO_0000395044"
FT BINDING 78
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B2HS63"
FT BINDING 96..97
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B2HS63"
FT BINDING 113..119
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B2HS63"
FT BINDING 125
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B2HS63"
FT CONFLICT 133
FT /note="D -> N (in Ref. 3; AAL87406/AAK32797)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 213 AA; 23203 MW; A12DE0EB02148636 CRC64;
MEIESKFKRI CVFCGSSAGN KVSYKDAAIE LGTELVSRNI DLVYGGGSIG LMGLISQAVF
NGGRHVIGVI PKTLMPREIT GETVGEVKAV ADMHQRKAEM AKHSDAFIAL PGGYGTLEEL
LEVITWAQLG IHDKPVGLLN VEGYYNSLLS FIDKAVEEGF ISPTARHIIV SAPSAKELVK
KLEDYVPRHE KVASKKSWEM EQIGLSPTCE ISR
