LOG2_ARATH
ID LOG2_ARATH Reviewed; 213 AA.
AC Q5BPS0; Q6DSS0; Q6DSS1; Q9SJ51;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 12-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Cytokinin riboside 5'-monophosphate phosphoribohydrolase LOG2;
DE EC=3.2.2.n1;
DE AltName: Full=Protein LONELY GUY 2;
GN Name=LOG2; OrderedLocusNames=At2g35990; ORFNames=F11F19.10;
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] (ISOFORMS 1 AND 2).
RC STRAIN=cv. Columbia;
RA Underwood B.A., Xiao Y.-L., Moskal W.A. Jr., Monaghan E.L., Wang W.,
RA Redman J.C., Wu H.C., Utterback T., Town C.D.;
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
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 [5]
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=58 uM for N(6)-(Delta(2)-isopentenyl)-adenosine 5'-phosphate
CC {ECO:0000269|PubMed:19837870};
CC Vmax=14 umol/min/mg enzyme with N(6)-(Delta(2)-isopentenyl)-adenosine
CC 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5BPS0-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5BPS0-2; Sequence=VSP_039355;
CC -!- TISSUE SPECIFICITY: Expressed in roots and shoots. Detected in root
CC hairs. {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=AAD21458.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC007017; AAD21458.1; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC09186.1; -; Genomic_DNA.
DR EMBL; AY924758; AAX23833.1; -; mRNA.
DR EMBL; AY648327; AAT68738.1; -; mRNA.
DR EMBL; AY648328; AAT68739.1; -; mRNA.
DR PIR; E84775; E84775.
DR RefSeq; NP_181143.3; NM_129158.4. [Q5BPS0-1]
DR AlphaFoldDB; Q5BPS0; -.
DR SMR; Q5BPS0; -.
DR STRING; 3702.AT2G35990.1; -.
DR PaxDb; Q5BPS0; -.
DR PRIDE; Q5BPS0; -.
DR EnsemblPlants; AT2G35990.1; AT2G35990.1; AT2G35990. [Q5BPS0-1]
DR GeneID; 818172; -.
DR Gramene; AT2G35990.1; AT2G35990.1; AT2G35990. [Q5BPS0-1]
DR KEGG; ath:AT2G35990; -.
DR Araport; AT2G35990; -.
DR TAIR; locus:2039175; AT2G35990.
DR eggNOG; ENOG502QSR9; Eukaryota.
DR HOGENOM; CLU_058336_2_2_1; -.
DR OMA; MVWDDIS; -.
DR OrthoDB; 979502at2759; -.
DR PhylomeDB; Q5BPS0; -.
DR PRO; PR:Q5BPS0; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q5BPS0; baseline and differential.
DR Genevisible; Q5BPS0; 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 Alternative splicing; Cytokinin biosynthesis; Cytoplasm; Hydrolase;
KW Nucleus; Reference proteome.
FT CHAIN 1..213
FT /note="Cytokinin riboside 5'-monophosphate
FT phosphoribohydrolase LOG2"
FT /id="PRO_0000395045"
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"
FT VAR_SEQ 1..93
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.3"
FT /id="VSP_039355"
SQ SEQUENCE 213 AA; 23314 MW; 8F574BF7DD9CDF1C CRC64;
MEETKSRFRR ICVFCGSSSG NKTTYHDAAL QLAHQLVERN IDLVYGGGSV GLMGLISQAV
HDGGRHVLGI IPKSLAPREI TGESIGEVIT VSTMHQRKAE MGRQADAFIA LPGGYGTFEE
LLEVITWSQL GIHTKPVGLL NVDGFYDSLL TFIDKAVDEG FVSSTARRII VSAPNAPQLL
QLLEEYVPKH DDFVSKMVWD NTTDAFTLEG DSF
