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LOG9_ARATH
ID   LOG9_ARATH              Reviewed;         143 AA.
AC   Q9XH06;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1999, sequence version 1.
DT   03-AUG-2022, entry version 95.
DE   RecName: Full=Putative cytokinin riboside 5'-monophosphate phosphoribohydrolase LOG9;
DE            EC=3.2.2.n1;
DE   AltName: Full=Protein LONELY GUY 9;
GN   Name=LOG9; OrderedLocusNames=At5g26140; ORFNames=T1N24.16;
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   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   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 (By similarity).
CC       {ECO:0000250}.
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   -!- 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   -!- SIMILARITY: Belongs to the LOG family. {ECO:0000305}.
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DR   EMBL; AF149413; AAD40141.1; -; Genomic_DNA.
DR   EMBL; CP002688; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   AlphaFoldDB; Q9XH06; -.
DR   SMR; Q9XH06; -.
DR   STRING; 3702.AT5G26140.1; -.
DR   PaxDb; Q9XH06; -.
DR   Araport; AT5G26140; -.
DR   TAIR; locus:2180672; AT5G26140.
DR   eggNOG; ENOG502QTZZ; Eukaryota.
DR   HOGENOM; CLU_058336_2_2_1; -.
DR   PhylomeDB; Q9XH06; -.
DR   PRO; PR:Q9XH06; -.
DR   Proteomes; UP000006548; Chromosome 5.
DR   ExpressionAtlas; Q9XH06; baseline and differential.
DR   Genevisible; Q9XH06; 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; IPR031100; LOG_fam.
DR   Pfam; PF03641; Lysine_decarbox; 1.
PE   3: Inferred from homology;
KW   Cytokinin biosynthesis; Hydrolase; Reference proteome.
FT   CHAIN           1..143
FT                   /note="Putative cytokinin riboside 5'-monophosphate
FT                   phosphoribohydrolase LOG9"
FT                   /id="PRO_0000395051"
FT   BINDING         23..24
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B2HS63"
FT   BINDING         41..47
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B2HS63"
FT   BINDING         53
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B2HS63"
SQ   SEQUENCE   143 AA;  16140 MW;  B6105F84FD5616C5 CRC64;
     MHIEHISGET VGEVRIVSDM HERKATMAQE AGAFIALLGE RYETMEELLE MITWAQLGIH
     KKTVGLLNVD GYYNNLLAFF DTGVEEGFIK QGACNIVVSA PSARELMEKM ELYTPSHKYI
     ASHQSWKVEP LGDYPLLNEN KPQ
 
 
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