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   24-JAN-2024, entry version 128.
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;
GN   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; 27.
DR   STRING; 3702.Q9LMI0; -.
DR   CAZy; GT20; Glycosyltransferase Family 20.
DR   iPTMnet; Q9LMI0; -.
DR   PaxDb; 3702-AT1G06410-1; -.
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; AT1G06410; TPS7.
DR   eggNOG; KOG1050; Eukaryota.
DR   HOGENOM; CLU_002351_3_1_1; -.
DR   InParanoid; Q9LMI0; -.
DR   OMA; KFRCVPA; -.
DR   OrthoDB; 1023at2759; -.
DR   PhylomeDB; Q9LMI0; -.
DR   BioCyc; ARA:AT1G06410-MONOMER; -.
DR   PRO; PR:Q9LMI0; -.
DR   Proteomes; UP000006548; Chromosome 1.
DR   ExpressionAtlas; Q9LMI0; baseline and differential.
DR   GO; GO:0016757; F:glycosyltransferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005992; P:trehalose biosynthetic process; IEA:InterPro.
DR   CDD; cd03788; GT20_TPS; 1.
DR   CDD; cd01627; HAD_TPP; 1.
DR   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 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   NCBIfam; TIGR01484; HAD-SF-IIB; 1.
DR   NCBIfam; TIGR00685; T6PP; 1.
DR   PANTHER; PTHR10788:SF116; ALPHA,ALPHA-TREHALOSE-PHOSPHATE SYNTHASE [UDP-FORMING] 7-RELATED; 1.
DR   PANTHER; PTHR10788; TREHALOSE-6-PHOSPHATE SYNTHASE; 1.
DR   Pfam; PF00982; Glyco_transf_20; 1.
DR   Pfam; PF02358; Trehalose_PPase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
DR   Genevisible; Q9LMI0; AT.
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
//