LOG4_ARATH
ID LOG4_ARATH Reviewed; 215 AA.
AC Q9LFH3;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Cytokinin riboside 5'-monophosphate phosphoribohydrolase LOG4;
DE EC=3.2.2.n1;
DE AltName: Full=Protein LONELY GUY 4;
GN Name=LOG4; OrderedLocusNames=At3g53450; ORFNames=F4P12.150;
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=11130713; DOI=10.1038/35048706;
RA Salanoubat M., Lemcke K., Rieger M., Ansorge W., Unseld M., Fartmann B.,
RA Valle G., Bloecker H., Perez-Alonso M., Obermaier B., Delseny M.,
RA Boutry M., Grivell L.A., Mache R., Puigdomenech P., De Simone V.,
RA Choisne N., Artiguenave F., Robert C., Brottier P., Wincker P.,
RA Cattolico L., Weissenbach J., Saurin W., Quetier F., Schaefer M.,
RA Mueller-Auer S., Gabel C., Fuchs M., Benes V., Wurmbach E., Drzonek H.,
RA Erfle H., Jordan N., Bangert S., Wiedelmann R., Kranz H., Voss H.,
RA Holland R., Brandt P., Nyakatura G., Vezzi A., D'Angelo M., Pallavicini A.,
RA Toppo S., Simionati B., Conrad A., Hornischer K., Kauer G., Loehnert T.-H.,
RA Nordsiek G., Reichelt J., Scharfe M., Schoen O., Bargues M., Terol J.,
RA Climent J., Navarro P., Collado C., Perez-Perez A., Ottenwaelder B.,
RA Duchemin D., Cooke R., Laudie M., Berger-Llauro C., Purnelle B., Masuy D.,
RA de Haan M., Maarse A.C., Alcaraz J.-P., Cottet A., Casacuberta E.,
RA Monfort A., Argiriou A., Flores M., Liguori R., Vitale D., Mannhaupt G.,
RA Haase D., Schoof H., Rudd S., Zaccaria P., Mewes H.-W., Mayer K.F.X.,
RA Kaul S., Town C.D., Koo H.L., Tallon L.J., Jenkins J., Rooney T., Rizzo M.,
RA Walts A., Utterback T., Fujii C.Y., Shea T.P., Creasy T.H., Haas B.,
RA Maiti R., Wu D., Peterson J., Van Aken S., Pai G., Militscher J.,
RA Sellers P., Gill J.E., Feldblyum T.V., Preuss D., Lin X., Nierman W.C.,
RA Salzberg S.L., White O., Venter J.C., Fraser C.M., Kaneko T., Nakamura Y.,
RA Sato S., Kato T., Asamizu E., Sasamoto S., Kimura T., Idesawa K.,
RA Kawashima K., Kishida Y., Kiyokawa C., Kohara M., Matsumoto M., Matsuno A.,
RA Muraki A., Nakayama S., Nakazaki N., Shinpo S., Takeuchi C., Wada T.,
RA Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence and analysis of chromosome 3 of the plant Arabidopsis thaliana.";
RL Nature 408:820-822(2000).
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 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 [4]
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=8.6 uM for N(6)-(Delta(2)-isopentenyl)-adenosine 5'-phosphate
CC {ECO:0000269|PubMed:19837870};
CC Vmax=4.4 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 root
CC procambium, lateral root primordia, vascular tissues of cotyledons,
CC leaves and stems, shoot apical meristem, axillary buds, young
CC inflorescences, fruit abscission zones and basal part of ovules.
CC {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}.
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DR EMBL; AL132966; CAB67652.1; -; Genomic_DNA.
DR EMBL; CP002686; AEE79088.1; -; Genomic_DNA.
DR PIR; T45885; T45885.
DR RefSeq; NP_190913.1; NM_115205.2.
DR AlphaFoldDB; Q9LFH3; -.
DR SMR; Q9LFH3; -.
DR STRING; 3702.AT3G53450.1; -.
DR PaxDb; Q9LFH3; -.
DR PRIDE; Q9LFH3; -.
DR ProteomicsDB; 238792; -.
DR DNASU; 824513; -.
DR EnsemblPlants; AT3G53450.1; AT3G53450.1; AT3G53450.
DR GeneID; 824513; -.
DR Gramene; AT3G53450.1; AT3G53450.1; AT3G53450.
DR KEGG; ath:AT3G53450; -.
DR Araport; AT3G53450; -.
DR TAIR; locus:2084051; AT3G53450.
DR eggNOG; ENOG502QSR9; Eukaryota.
DR HOGENOM; CLU_058336_2_0_1; -.
DR OMA; WEIERID; -.
DR OrthoDB; 979502at2759; -.
DR PhylomeDB; Q9LFH3; -.
DR PRO; PR:Q9LFH3; -.
DR Proteomes; UP000006548; Chromosome 3.
DR ExpressionAtlas; Q9LFH3; baseline and differential.
DR Genevisible; Q9LFH3; 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..215
FT /note="Cytokinin riboside 5'-monophosphate
FT phosphoribohydrolase LOG4"
FT /id="PRO_0000395047"
FT BINDING 84
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B2HS63"
FT BINDING 102..103
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B2HS63"
FT BINDING 119..125
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B2HS63"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B2HS63"
SQ SEQUENCE 215 AA; 23545 MW; DBF8DAFD39A429C6 CRC64;
MEVNNETMQK SKFGRICVFC GSSQGKKSSY QDAAVDLGNE LVLRNIDLVY GGGSIGLMGL
VSQAVHDGGR HVIGVIPKTL MPRELTGETV GEVRAVADMH QRKAEMARHS DAFIALPGGY
GTLEELLEVI TWAQLGIHDK PVGLLNVDGY YNSLLSFIDK AVEEGFISTN ARQIIISAPT
AKELVKKLEE YSPCHESVAT KLCWEIERID YSSED
