LOG3_ARATH
ID LOG3_ARATH Reviewed; 215 AA.
AC Q8L8B8; Q9ZQD5;
DT 15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 112.
DE RecName: Full=Cytokinin riboside 5'-monophosphate phosphoribohydrolase LOG3;
DE EC=3.2.2.n1;
DE AltName: Full=Protein LONELY GUY 3;
GN Name=LOG3; OrderedLocusNames=At2g37210; ORFNames=T2N18.3;
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 [MRNA].
RX PubMed=12481096; DOI=10.1104/pp.010207;
RA Xiao Y.-L., Malik M., Whitelaw C.A., Town C.D.;
RT "Cloning and sequencing of cDNAs for hypothetical genes from chromosome 2
RT of Arabidopsis.";
RL Plant Physiol. 130:2118-2128(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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 (MAR-2005) 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, 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).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.95 ANGSTROMS).
RX PubMed=17048257; DOI=10.1002/prot.21166;
RA Jeon W.B., Allard S.T., Bingman C.A., Bitto E., Han B.W., Wesenberg G.E.,
RA Phillips G.N. Jr.;
RT "X-ray crystal structures of the conserved hypothetical proteins from
RT Arabidopsis thaliana gene loci At5g11950 and At2g37210.";
RL Proteins 65:1051-1054(2006).
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=14 uM for N(6)-(Delta(2)-isopentenyl)-adenosine 5'-phosphate
CC {ECO:0000269|PubMed:19837870};
CC Vmax=1.5 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 -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=1;
CC Comment=A number of isoforms are produced. According to EST
CC sequences.;
CC Name=1;
CC IsoId=Q8L8B8-1; Sequence=Displayed;
CC -!- TISSUE SPECIFICITY: Expressed in roots and shoots. Detected in root
CC procambium, lateral root primordia, vascular tissues of immature
CC leaves, axillary buds, style and ovular funiculus.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAD18138.2; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AC006260; AAD18138.2; ALT_SEQ; Genomic_DNA.
DR EMBL; CP002685; AEC09367.1; -; Genomic_DNA.
DR EMBL; AY102554; AAM76759.1; -; mRNA.
DR EMBL; AY954818; AAX55144.1; -; mRNA.
DR PIR; H84789; H84789.
DR RefSeq; NP_181258.2; NM_129277.3. [Q8L8B8-1]
DR PDB; 2A33; X-ray; 1.95 A; A/B=1-215.
DR PDB; 2Q4O; X-ray; 1.95 A; A/B=1-215.
DR PDBsum; 2A33; -.
DR PDBsum; 2Q4O; -.
DR AlphaFoldDB; Q8L8B8; -.
DR SMR; Q8L8B8; -.
DR BioGRID; 3642; 2.
DR PRIDE; Q8L8B8; -.
DR ProteomicsDB; 238585; -. [Q8L8B8-1]
DR DNASU; 818298; -.
DR EnsemblPlants; AT2G37210.1; AT2G37210.1; AT2G37210. [Q8L8B8-1]
DR GeneID; 818298; -.
DR Gramene; AT2G37210.1; AT2G37210.1; AT2G37210. [Q8L8B8-1]
DR KEGG; ath:AT2G37210; -.
DR Araport; AT2G37210; -.
DR HOGENOM; CLU_058336_2_0_1; -.
DR OMA; TLVWGGS; -.
DR PhylomeDB; Q8L8B8; -.
DR EvolutionaryTrace; Q8L8B8; -.
DR PRO; PR:Q8L8B8; -.
DR Proteomes; UP000006548; Chromosome 2.
DR ExpressionAtlas; Q8L8B8; baseline and differential.
DR Genevisible; Q8L8B8; AT.
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 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytokinin biosynthesis; Cytoplasm;
KW Hydrolase; Nucleus; Reference proteome.
FT CHAIN 1..215
FT /note="Cytokinin riboside 5'-monophosphate
FT phosphoribohydrolase LOG3"
FT /id="PRO_0000395046"
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"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:2A33"
FT HELIX 28..43
FT /evidence="ECO:0007829|PDB:2A33"
FT STRAND 47..50
FT /evidence="ECO:0007829|PDB:2A33"
FT HELIX 56..67
FT /evidence="ECO:0007829|PDB:2A33"
FT STRAND 72..79
FT /evidence="ECO:0007829|PDB:2A33"
FT STRAND 92..98
FT /evidence="ECO:0007829|PDB:2A33"
FT HELIX 99..108
FT /evidence="ECO:0007829|PDB:2A33"
FT STRAND 111..115
FT /evidence="ECO:0007829|PDB:2A33"
FT HELIX 120..134
FT /evidence="ECO:0007829|PDB:2A33"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:2A33"
FT HELIX 147..149
FT /evidence="ECO:0007829|PDB:2A33"
FT HELIX 152..163
FT /evidence="ECO:0007829|PDB:2A33"
FT HELIX 169..172
FT /evidence="ECO:0007829|PDB:2A33"
FT STRAND 175..180
FT /evidence="ECO:0007829|PDB:2A33"
FT HELIX 181..189
FT /evidence="ECO:0007829|PDB:2A33"
SQ SEQUENCE 215 AA; 23558 MW; 4782E3570DE4B1FF CRC64;
MEIKGESMQK SKFRRICVFC GSSQGKKSSY QDAAVDLGNE LVSRNIDLVY GGGSIGLMGL
VSQAVHDGGR HVIGIIPKTL MPRELTGETV GEVRAVADMH QRKAEMAKHS DAFIALPGGY
GTLEELLEVI TWAQLGIHDK PVGLLNVDGY YNSLLSFIDK AVEEGFISPT AREIIVSAPT
AKELVKKLEE YAPCHERVAT KLCWEMERIG YSSEE
