TPS7_ARATH
ID TPS7_ARATH Reviewed; 851 AA.
AC Q9LMI0; Q0WPW3;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Probable alpha,alpha-trehalose-phosphate synthase [UDP-forming] 7;
DE EC=2.4.1.15;
DE AltName: Full=Trehalose-6-phosphate synthase 7;
DE Short=AtTPS7;
GN Name=TPS7; Synonyms=TPSA; OrderedLocusNames=At1g06410; ORFNames=T2D23.11;
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 [MRNA], AND TISSUE SPECIFICITY.
RC STRAIN=cv. Landsberg erecta;
RX PubMed=11520870; DOI=10.1093/jexbot/52.362.1817;
RA Vogel G., Fiehn O., Jean-Richard-dit-Bressel L., Boller T., Wiemken A.,
RA Aeschbacher R.A., Wingler A.;
RT "Trehalose metabolism in Arabidopsis: occurrence of trehalose and molecular
RT cloning and characterization of trehalose-6-phosphate synthase
RT homologues.";
RL J. Exp. Bot. 52:1817-1826(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. Columbia;
RX PubMed=11130712; DOI=10.1038/35048500;
RA Theologis A., Ecker J.R., Palm C.J., Federspiel N.A., Kaul S., White O.,
RA Alonso J., Altafi H., Araujo R., Bowman C.L., Brooks S.Y., Buehler E.,
RA Chan A., Chao Q., Chen H., Cheuk R.F., Chin C.W., Chung M.K., Conn L.,
RA Conway A.B., Conway A.R., Creasy T.H., Dewar K., Dunn P., Etgu P.,
RA Feldblyum T.V., Feng J.-D., Fong B., Fujii C.Y., Gill J.E., Goldsmith A.D.,
RA Haas B., Hansen N.F., Hughes B., Huizar L., Hunter J.L., Jenkins J.,
RA Johnson-Hopson C., Khan S., Khaykin E., Kim C.J., Koo H.L.,
RA Kremenetskaia I., Kurtz D.B., Kwan A., Lam B., Langin-Hooper S., Lee A.,
RA Lee J.M., Lenz C.A., Li J.H., Li Y.-P., Lin X., Liu S.X., Liu Z.A.,
RA Luros J.S., Maiti R., Marziali A., Militscher J., Miranda M., Nguyen M.,
RA Nierman W.C., Osborne B.I., Pai G., Peterson J., Pham P.K., Rizzo M.,
RA Rooney T., Rowley D., Sakano H., Salzberg S.L., Schwartz J.R., Shinn P.,
RA Southwick A.M., Sun H., Tallon L.J., Tambunga G., Toriumi M.J., Town C.D.,
RA Utterback T., Van Aken S., Vaysberg M., Vysotskaia V.S., Walker M., Wu D.,
RA Yu G., Fraser C.M., Venter J.C., Davis R.W.;
RT "Sequence and analysis of chromosome 1 of the plant Arabidopsis thaliana.";
RL Nature 408:816-820(2000).
RN [3]
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 559-851.
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 (JUL-2006) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP GENE FAMILY, AND NOMENCLATURE.
RX PubMed=11701378; DOI=10.1016/s1360-1385(01)02125-2;
RA Leyman B., Van Dijck P., Thevelein J.M.;
RT "An unexpected plethora of trehalose biosynthesis genes in Arabidopsis
RT thaliana.";
RL Trends Plant Sci. 6:510-513(2001).
RN [6]
RP PHOSPHORYLATION, INTERACTION WITH GRF/14-3-3, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RX PubMed=16771775; DOI=10.1111/j.1365-313x.2006.02780.x;
RA Harthill J.E., Meek S.E.M., Morrice N., Peggie M.W., Borch J., Wong B.H.C.,
RA Mackintosh C.;
RT "Phosphorylation and 14-3-3 binding of Arabidopsis trehalose-phosphate
RT synthase 5 in response to 2-deoxyglucose.";
RL Plant J. 47:211-223(2006).
RN [7]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=cv. Columbia;
RX PubMed=19245862; DOI=10.1016/j.jprot.2009.02.004;
RA Jones A.M.E., MacLean D., Studholme D.J., Serna-Sanz A., Andreasson E.,
RA Rathjen J.P., Peck S.C.;
RT "Phosphoproteomic analysis of nuclei-enriched fractions from Arabidopsis
RT thaliana.";
RL J. Proteomics 72:439-451(2009).
RN [8]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19376835; DOI=10.1104/pp.109.138677;
RA Reiland S., Messerli G., Baerenfaller K., Gerrits B., Endler A.,
RA Grossmann J., Gruissem W., Baginsky S.;
RT "Large-scale Arabidopsis phosphoproteome profiling reveals novel
RT chloroplast kinase substrates and phosphorylation networks.";
RL Plant Physiol. 150:889-903(2009).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=D-glucose 6-phosphate + UDP-alpha-D-glucose = alpha,alpha-
CC trehalose 6-phosphate + H(+) + UDP; Xref=Rhea:RHEA:18889,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:58223, ChEBI:CHEBI:58429,
CC ChEBI:CHEBI:58885, ChEBI:CHEBI:61548; EC=2.4.1.15;
CC -!- SUBUNIT: Binds to the phosphopeptide-binding site of GRF/14-3-3.
CC -!- TISSUE SPECIFICITY: Expressed in seedlings, leaves, roots, stems,
CC flowers and siliques. {ECO:0000269|PubMed:11520870}.
CC -!- PTM: Phosphorylated. {ECO:0000269|PubMed:16771775}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 20 family. {ECO:0000305}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the trehalose
CC phosphatase family. {ECO:0000305}.
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DR EMBL; AC068143; AAF82169.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE27983.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59083.1; -; Genomic_DNA.
DR EMBL; CP002684; ANM59084.1; -; Genomic_DNA.
DR EMBL; AK228947; BAF00836.1; -; mRNA.
DR PIR; A86200; A86200.
DR RefSeq; NP_001321475.1; NM_001331627.1.
DR RefSeq; NP_001321476.1; NM_001331626.1.
DR RefSeq; NP_172129.1; NM_100521.3.
DR AlphaFoldDB; Q9LMI0; -.
DR SMR; Q9LMI0; -.
DR BioGRID; 22393; 1.
DR IntAct; Q9LMI0; 1.
DR STRING; 3702.AT1G06410.1; -.
DR CAZy; GT20; Glycosyltransferase Family 20.
DR iPTMnet; Q9LMI0; -.
DR PaxDb; Q9LMI0; -.
DR PRIDE; Q9LMI0; -.
DR ProteomicsDB; 232503; -.
DR EnsemblPlants; AT1G06410.1; AT1G06410.1; AT1G06410.
DR EnsemblPlants; AT1G06410.2; AT1G06410.2; AT1G06410.
DR EnsemblPlants; AT1G06410.3; AT1G06410.3; AT1G06410.
DR GeneID; 837152; -.
DR Gramene; AT1G06410.1; AT1G06410.1; AT1G06410.
DR Gramene; AT1G06410.2; AT1G06410.2; AT1G06410.
DR Gramene; AT1G06410.3; AT1G06410.3; AT1G06410.
DR KEGG; ath:AT1G06410; -.
DR Araport; AT1G06410; -.
DR TAIR; locus:2202290; AT1G06410.
DR eggNOG; KOG1050; Eukaryota.
DR HOGENOM; CLU_002351_3_1_1; -.
DR InParanoid; Q9LMI0; -.
DR OMA; RMAYYSI; -.
DR OrthoDB; 772297at2759; -.
DR PhylomeDB; Q9LMI0; -.
DR BioCyc; ARA:AT1G06410-MON; -.
DR PRO; PR:Q9LMI0; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LMI0; baseline and differential.
DR Genevisible; Q9LMI0; AT.
DR GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR GO; GO:0005992; P:trehalose biosynthetic process; IBA:GO_Central.
DR GO; GO:0070413; P:trehalose metabolism in response to stress; IBA:GO_Central.
DR CDD; cd03788; GT20_TPS; 1.
DR Gene3D; 3.40.50.1000; -; 2.
DR InterPro; IPR001830; Glyco_trans_20.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006379; HAD-SF_hydro_IIB.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR003337; Trehalose_PPase.
DR PANTHER; PTHR10788; PTHR10788; 1.
DR Pfam; PF00982; Glyco_transf_20; 1.
DR Pfam; PF02358; Trehalose_PPase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01484; HAD-SF-IIB; 1.
DR TIGRFAMs; TIGR00685; T6PP; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..851
FT /note="Probable alpha,alpha-trehalose-phosphate synthase
FT [UDP-forming] 7"
FT /id="PRO_0000324828"
FT REGION 59..540
FT /note="Glycosyltransferase"
FT MOD_RES 5
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O23617"
FT MOD_RES 32
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O23617"
SQ SEQUENCE 851 AA; 96688 MW; 1799F009CF8E4A1B CRC64;
MISRSYTNLL DLASGNFPVM GRERRRLPRV MTVPGNVSEF DEDQAYSVSS DNPSSVSSDR
MIIVANRLPL KAEKRNGSWS FSWDQDSLYL QLKDGLPEDM EILYVGSLSV DVDSNEQDDV
AQILLDKFKC VPTFFPPDLQ SKFYDGFCKR QIWPLFHYML PFSADHGGRF DRSLWEAYVA
TNKLFFQKVI EVINPDDDFV WIHDYHLMVL PTFLRRRFNR IRMGFFLHSP FPSSEIYRSL
PVREEILKAL LNSDLIGFHT FDYARHFLTC CSRMLGLEYQ SKRGYIGLEY YGRTVGIKIM
PVGINMGRIQ SVMRYSEEEG KVMELRNRFE GKTVLLGIDD MDIFKGINLK LLAMEQMLRQ
HPNWRGRAVL VQIVNPARGK GIDVEEIRGE IEESCRRING EFGKPGYQPI IYIDTPVSIN
EINAYYHIAE CVVVTAVRDG MNLTPYEYIV CRQGLLGSES DFSGPKKSML VASEFIGCSP
SLSGAIRVNP WNVEATGEAL NEALSMSDAE KQLRHEKHFR YVSTHDVAYW SRSFLQDLER
ICVDHFKKRC WGMGISFGFR VVALDPNFRK LSIPCIVSDY KRAKSRAILL DYDGTLMPQN
SINKAPSQEV LNFLDALCED KKNSIFIVSG RGRESLSKWF TPCKKIGIAA EHGYFLKWSG
SEEWETCGQS SDFGWMQIVE PVMKQYTEST DGSSIEIKES ALVWQYRDAD PGFGSLQAKE
MLEHLESVLA NEPVAVKSGH YIVEVKPQGV SKGSVSEKIF SSMAGKGKPV DFVLCIGDDR
SDEDMFEAIG NAMSKRLLCD NALVFACTVG QKPSKAKYYL DDTTEVTCML ESLAEASEAS
NFSMRELDEA L