LOG8_ARATH
ID LOG8_ARATH Reviewed; 216 AA.
AC Q84MC2; Q0WTA9; Q570P8; Q9LYH8;
DT 24-JAN-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Cytokinin riboside 5'-monophosphate phosphoribohydrolase LOG8;
DE EC=3.2.2.n1;
DE AltName: Full=LOG family protein At5g11950;
DE AltName: Full=Protein LONELY GUY 8;
GN Name=LOG8; OrderedLocusNames=At5g11950; ORFNames=F14F18.120;
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=11130714; DOI=10.1038/35048507;
RA Tabata S., Kaneko T., Nakamura Y., Kotani H., Kato T., Asamizu E.,
RA Miyajima N., Sasamoto S., Kimura T., Hosouchi T., Kawashima K., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakayama S., Nakazaki N., Naruo K.,
RA Okumura S., Shinpo S., Takeuchi C., Wada T., Watanabe A., Yamada M.,
RA Yasuda M., Sato S., de la Bastide M., Huang E., Spiegel L., Gnoj L.,
RA O'Shaughnessy A., Preston R., Habermann K., Murray J., Johnson D.,
RA Rohlfing T., Nelson J., Stoneking T., Pepin K., Spieth J., Sekhon M.,
RA Armstrong J., Becker M., Belter E., Cordum H., Cordes M., Courtney L.,
RA Courtney W., Dante M., Du H., Edwards J., Fryman J., Haakensen B.,
RA Lamar E., Latreille P., Leonard S., Meyer R., Mulvaney E., Ozersky P.,
RA Riley A., Strowmatt C., Wagner-McPherson C., Wollam A., Yoakum M., Bell M.,
RA Dedhia N., Parnell L., Shah R., Rodriguez M., Hoon See L., Vil D.,
RA Baker J., Kirchoff K., Toth K., King L., Bahret A., Miller B., Marra M.A.,
RA Martienssen R., McCombie W.R., Wilson R.K., Murphy G., Bancroft I.,
RA Volckaert G., Wambutt R., Duesterhoeft A., Stiekema W., Pohl T.,
RA Entian K.-D., Terryn N., Hartley N., Bent E., Johnson S., Langham S.-A.,
RA McCullagh B., Robben J., Grymonprez B., Zimmermann W., Ramsperger U.,
RA Wedler H., Balke K., Wedler E., Peters S., van Staveren M., Dirkse W.,
RA Mooijman P., Klein Lankhorst R., Weitzenegger T., Bothe G., Rose M.,
RA Hauf J., Berneiser S., Hempel S., Feldpausch M., Lamberth S.,
RA Villarroel R., Gielen J., Ardiles W., Bents O., Lemcke K., Kolesov G.,
RA Mayer K.F.X., Rudd S., Schoof H., Schueller C., Zaccaria P., Mewes H.-W.,
RA Bevan M., Fransz P.F.;
RT "Sequence and analysis of chromosome 5 of the plant Arabidopsis thaliana.";
RL Nature 408:823-826(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 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].
RC STRAIN=cv. Columbia;
RA Totoki Y., Seki M., Ishida J., Nakajima M., Enju A., Kamiya A.,
RA Narusaka M., Shin-i T., Nakagawa M., Sakamoto N., Oishi K., Kohara Y.,
RA Kobayashi M., Toyoda A., Sakaki Y., Sakurai T., Iida K., Akiyama K.,
RA Satou M., Toyoda T., Konagaya A., Carninci P., Kawai J., Hayashizaki Y.,
RA Shinozaki K.;
RT "Large-scale analysis of RIKEN Arabidopsis full-length (RAFL) cDNAs.";
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 (2.15 ANGSTROMS) OF 2-216.
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=17 uM for N(6)-(Delta(2)-isopentenyl)-adenosine 5'-phosphate
CC {ECO:0000269|PubMed:19837870};
CC Vmax=0.053 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 7.0. {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 root
CC quiescent center and vasculature, in cotyledons, hypocotyls, stems,
CC leaves, stomata, axillary buds, flowers and fruit abscission zones.
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; AL163812; CAB87668.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91743.1; -; Genomic_DNA.
DR EMBL; CP002688; AED91744.1; -; Genomic_DNA.
DR EMBL; CP002688; ANM70822.1; -; Genomic_DNA.
DR EMBL; BT006409; AAP21217.1; -; mRNA.
DR EMBL; AK220660; BAD95184.1; -; mRNA.
DR EMBL; AK227652; BAE99639.1; -; mRNA.
DR PIR; T48554; T48554.
DR RefSeq; NP_001332403.1; NM_001343223.1.
DR RefSeq; NP_196756.2; NM_121233.4.
DR RefSeq; NP_974768.1; NM_203039.3.
DR PDB; 1YDH; X-ray; 2.15 A; A/B=2-216.
DR PDB; 2Q4D; X-ray; 2.15 A; A/B=2-216.
DR PDBsum; 1YDH; -.
DR PDBsum; 2Q4D; -.
DR AlphaFoldDB; Q84MC2; -.
DR SMR; Q84MC2; -.
DR STRING; 3702.AT5G11950.1; -.
DR PaxDb; Q84MC2; -.
DR PRIDE; Q84MC2; -.
DR ProteomicsDB; 238586; -.
DR DNASU; 831068; -.
DR EnsemblPlants; AT5G11950.1; AT5G11950.1; AT5G11950.
DR EnsemblPlants; AT5G11950.2; AT5G11950.2; AT5G11950.
DR EnsemblPlants; AT5G11950.3; AT5G11950.3; AT5G11950.
DR GeneID; 831068; -.
DR Gramene; AT5G11950.1; AT5G11950.1; AT5G11950.
DR Gramene; AT5G11950.2; AT5G11950.2; AT5G11950.
DR Gramene; AT5G11950.3; AT5G11950.3; AT5G11950.
DR KEGG; ath:AT5G11950; -.
DR Araport; AT5G11950; -.
DR TAIR; locus:2143029; AT5G11950.
DR eggNOG; ENOG502QTZZ; Eukaryota.
DR HOGENOM; CLU_058336_2_0_1; -.
DR OMA; HQKPIGL; -.
DR OrthoDB; 979502at2759; -.
DR PhylomeDB; Q84MC2; -.
DR EvolutionaryTrace; Q84MC2; -.
DR PRO; PR:Q84MC2; -.
DR Proteomes; UP000006548; Chromosome 5.
DR ExpressionAtlas; Q84MC2; baseline and differential.
DR Genevisible; Q84MC2; AT.
DR GO; GO:0005829; C:cytosol; IDA:TAIR.
DR GO; GO:0005634; C:nucleus; IDA:TAIR.
DR GO; GO:0005886; C:plasma membrane; HDA: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:0042803; F:protein homodimerization activity; IDA:TAIR.
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; Cytokinin biosynthesis; Cytoplasm; Hydrolase; Nucleus;
KW Reference proteome.
FT CHAIN 1..216
FT /note="Cytokinin riboside 5'-monophosphate
FT phosphoribohydrolase LOG8"
FT /id="PRO_0000220614"
FT BINDING 80
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B2HS63"
FT BINDING 98..99
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B2HS63"
FT BINDING 115..121
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B2HS63"
FT BINDING 127
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:B2HS63"
FT CONFLICT 114
FT /note="Missing (in Ref. 1; CAB87668)"
FT /evidence="ECO:0000305"
FT STRAND 10..15
FT /evidence="ECO:0007829|PDB:1YDH"
FT HELIX 24..39
FT /evidence="ECO:0007829|PDB:1YDH"
FT STRAND 43..46
FT /evidence="ECO:0007829|PDB:1YDH"
FT HELIX 52..63
FT /evidence="ECO:0007829|PDB:1YDH"
FT STRAND 68..73
FT /evidence="ECO:0007829|PDB:1YDH"
FT HELIX 74..76
FT /evidence="ECO:0007829|PDB:1YDH"
FT HELIX 77..80
FT /evidence="ECO:0007829|PDB:1YDH"
FT STRAND 87..94
FT /evidence="ECO:0007829|PDB:1YDH"
FT HELIX 95..105
FT /evidence="ECO:0007829|PDB:1YDH"
FT STRAND 107..111
FT /evidence="ECO:0007829|PDB:1YDH"
FT HELIX 116..130
FT /evidence="ECO:0007829|PDB:1YDH"
FT STRAND 137..141
FT /evidence="ECO:0007829|PDB:1YDH"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:1YDH"
FT HELIX 148..159
FT /evidence="ECO:0007829|PDB:1YDH"
FT HELIX 165..168
FT /evidence="ECO:0007829|PDB:1YDH"
FT STRAND 171..176
FT /evidence="ECO:0007829|PDB:1YDH"
FT HELIX 177..186
FT /evidence="ECO:0007829|PDB:1YDH"
SQ SEQUENCE 216 AA; 23831 MW; 04A48D451B259F16 CRC64;
MEDNQRSRFR KICVFCGSHS GHREVFSDAA IELGNELVKR KIDLVYGGGS VGLMGLISRR
VYEGGLHVLG IIPKALMPIE ISGETVGDVR VVADMHERKA AMAQEAEAFI ALPGGYGTME
ELLEMITWSQ LGIHKKTVGL LNVDGYYNNL LALFDTGVEE GFIKPGARNI VVSAPTAKEL
MEKMEEYTPS HMHVASHESW KVEELGDYPG QENKPQ
