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LOG_ORYSJ
ID   LOG_ORYSJ               Reviewed;         242 AA.
AC   Q5ZC82; A0A0N7KD87;
DT   15-JUN-2010, integrated into UniProtKB/Swiss-Prot.
DT   23-NOV-2004, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Cytokinin riboside 5'-monophosphate phosphoribohydrolase LOG;
DE            EC=3.2.2.n1;
DE   AltName: Full=Protein LONELY GUY;
GN   Name=LOG; OrderedLocusNames=Os01g0588900, LOC_Os01g40630;
GN   ORFNames=OsJ_02411, P0415C01.3;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12447438; DOI=10.1038/nature01184;
RA   Sasaki T., Matsumoto T., Yamamoto K., Sakata K., Baba T., Katayose Y.,
RA   Wu J., Niimura Y., Cheng Z., Nagamura Y., Antonio B.A., Kanamori H.,
RA   Hosokawa S., Masukawa M., Arikawa K., Chiden Y., Hayashi M., Okamoto M.,
RA   Ando T., Aoki H., Arita K., Hamada M., Harada C., Hijishita S., Honda M.,
RA   Ichikawa Y., Idonuma A., Iijima M., Ikeda M., Ikeno M., Ito S., Ito T.,
RA   Ito Y., Ito Y., Iwabuchi A., Kamiya K., Karasawa W., Katagiri S.,
RA   Kikuta A., Kobayashi N., Kono I., Machita K., Maehara T., Mizuno H.,
RA   Mizubayashi T., Mukai Y., Nagasaki H., Nakashima M., Nakama Y.,
RA   Nakamichi Y., Nakamura M., Namiki N., Negishi M., Ohta I., Ono N., Saji S.,
RA   Sakai K., Shibata M., Shimokawa T., Shomura A., Song J., Takazaki Y.,
RA   Terasawa K., Tsuji K., Waki K., Yamagata H., Yamane H., Yoshiki S.,
RA   Yoshihara R., Yukawa K., Zhong H., Iwama H., Endo T., Ito H., Hahn J.H.,
RA   Kim H.-I., Eun M.-Y., Yano M., Jiang J., Gojobori T.;
RT   "The genome sequence and structure of rice chromosome 1.";
RL   Nature 420:312-316(2002).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [4]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [6]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [7]
RP   FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION,
RP   BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF GLY-73, AND DISRUPTION
RP   PHENOTYPE.
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   [8]
RP   FUNCTION, 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. Controls the shoot meristem activity. Phosphoribohydrolase
CC       that converts inactive cytokinin nucleotides to the biologically active
CC       free-base forms. Reacts specifically with cytokinin nucleoside 5'-
CC       monophosphates, but not with di- or triphosphate.
CC       {ECO:0000269|PubMed:17287810, 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:17287810};
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:17287810};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=11.7 uM for N(6)-(Delta(2)-isopentenyl)-adenosine 5'-phosphate
CC         {ECO:0000269|PubMed:17287810};
CC         KM=22.0 uM for trans-zeatine riboside monophosphate
CC         {ECO:0000269|PubMed:17287810};
CC         Vmax=5.6 umol/min/mg enzyme with N(6)-(Delta(2)-isopentenyl)-
CC         adenosine 5'-phosphate as substrate {ECO:0000269|PubMed:17287810};
CC         Vmax=4.2 umol/min/mg enzyme with trans-zeatine riboside monophosphate
CC         as substrate {ECO:0000269|PubMed:17287810};
CC         Note=can also use benzyladenosine 5'-phosphate as substrate, but no
CC         activity with cytokinin ribosides.;
CC       pH dependence:
CC         Optimum pH is 6.5. {ECO:0000269|PubMed:17287810};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:17287810}.
CC   -!- TISSUE SPECIFICITY: Expressed in roots, leaves, stems, tiller buds,
CC       immature inflorescences and flowers. Expressed in the upper part of
CC       shoot meristems, including axillary meristems, meristems of developing
CC       panicle and floral meristems. {ECO:0000269|PubMed:17287810}.
CC   -!- DISRUPTION PHENOTYPE: Premature termination of the floral meristem.
CC       {ECO:0000269|PubMed:17287810}.
CC   -!- MISCELLANEOUS: The name lonely guy came from the fact that flowers of
CC       the mutants often contained only one stamen but no pistil.
CC   -!- SIMILARITY: Belongs to the LOG family. {ECO:0000305}.
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DR   EMBL; AP003243; BAD52880.1; -; Genomic_DNA.
DR   EMBL; AP008207; BAF05353.1; -; Genomic_DNA.
DR   EMBL; AP014957; BAS72929.1; -; Genomic_DNA.
DR   EMBL; CM000138; EAZ12515.1; -; Genomic_DNA.
DR   EMBL; AK071695; BAG92633.1; -; mRNA.
DR   RefSeq; XP_015621391.1; XM_015765905.1.
DR   AlphaFoldDB; Q5ZC82; -.
DR   SMR; Q5ZC82; -.
DR   STRING; 4530.OS01T0588900-01; -.
DR   PaxDb; Q5ZC82; -.
DR   PRIDE; Q5ZC82; -.
DR   EnsemblPlants; Os01t0588900-01; Os01t0588900-01; Os01g0588900.
DR   GeneID; 4324445; -.
DR   Gramene; Os01t0588900-01; Os01t0588900-01; Os01g0588900.
DR   KEGG; osa:4324445; -.
DR   eggNOG; ENOG502QSR9; Eukaryota.
DR   HOGENOM; CLU_058336_2_2_1; -.
DR   InParanoid; Q5ZC82; -.
DR   OMA; EVDRFSY; -.
DR   OrthoDB; 979502at2759; -.
DR   BioCyc; MetaCyc:MON-15646; -.
DR   PlantReactome; R-OSA-9608575; Reproductive meristem phase change.
DR   Proteomes; UP000000763; Chromosome 1.
DR   Proteomes; UP000007752; Chromosome 1.
DR   Proteomes; UP000059680; Chromosome 1.
DR   ExpressionAtlas; Q5ZC82; baseline and differential.
DR   Genevisible; Q5ZC82; OS.
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; IDA:UniProtKB.
DR   GO; GO:0048509; P:regulation of meristem development; IMP:UniProtKB.
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; Reference proteome.
FT   CHAIN           1..242
FT                   /note="Cytokinin riboside 5'-monophosphate
FT                   phosphoribohydrolase LOG"
FT                   /id="PRO_0000395052"
FT   REGION          9..30
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         106
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B2HS63"
FT   BINDING         124..125
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B2HS63"
FT   BINDING         141..147
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B2HS63"
FT   BINDING         153
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250|UniProtKB:B2HS63"
FT   MUTAGEN         73
FT                   /note="G->D: In LOG-4; decreased activity."
FT                   /evidence="ECO:0000269|PubMed:17287810"
SQ   SEQUENCE   242 AA;  25846 MW;  CC80A2BE86FCAC97 CRC64;
     MAMEAAAERS AGAGAAATAA PESGGGGAGE RRSRFRRICV YCGSAKGRKA SYQDAAVELG
     KELVERGIDL VYGGGSIGLM GLVSHAVHDG GRHVIGVIPK SLMPREVTGE PVGEVRAVSG
     MHERKAEMAR FADAFIALPG GYGTLEELLE VITWAQLGIH KKPVGLLNVD GFYDPFLSFI
     DMAVSEGFIA EDARRIIISA PTARELVLKL EEYVPEYEVG LVWDDQMPHS FAPDLETRIT
     SS
 
 
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