TPS8_ARATH
ID TPS8_ARATH Reviewed; 856 AA.
AC Q0WUI9; O64608;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-SEP-2006, sequence version 1.
DT 03-AUG-2022, entry version 99.
DE RecName: Full=Probable alpha,alpha-trehalose-phosphate synthase [UDP-forming] 8;
DE EC=2.4.1.15;
DE AltName: Full=Trehalose-6-phosphate synthase 8;
DE Short=AtTPS8;
GN Name=TPS8; Synonyms=TPS2, TPSC; OrderedLocusNames=At1g70290;
GN ORFNames=F17O7.18;
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].
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 NUCLEOTIDE SEQUENCE [MRNA] OF 31-856.
RA Kim Y.S., Lee E.J., Kim J.S., Lim D.H., Kim C.K., Chung C.H.;
RT "Isolation and characterization of Arabidopsis trehalose-6-phosphate
RT synthase.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [6]
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).
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 -!- TISSUE SPECIFICITY: Expressed in leaves, roots, stems and flowers.
CC {ECO:0000269|PubMed:11520870}.
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC18810.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AC003671; AAC18810.1; ALT_INIT; Genomic_DNA.
DR EMBL; CP002684; AEE35042.1; -; Genomic_DNA.
DR EMBL; AK227167; BAE99209.1; -; mRNA.
DR EMBL; AF155150; AAO15311.1; -; mRNA.
DR PIR; T01494; T01494.
DR RefSeq; NP_177186.2; NM_105697.4.
DR AlphaFoldDB; Q0WUI9; -.
DR SMR; Q0WUI9; -.
DR BioGRID; 28585; 1.
DR STRING; 3702.AT1G70290.1; -.
DR CAZy; GT20; Glycosyltransferase Family 20.
DR iPTMnet; Q0WUI9; -.
DR PaxDb; Q0WUI9; -.
DR PRIDE; Q0WUI9; -.
DR ProteomicsDB; 228333; -.
DR EnsemblPlants; AT1G70290.1; AT1G70290.1; AT1G70290.
DR GeneID; 843365; -.
DR Gramene; AT1G70290.1; AT1G70290.1; AT1G70290.
DR KEGG; ath:AT1G70290; -.
DR Araport; AT1G70290; -.
DR TAIR; locus:2016179; AT1G70290.
DR eggNOG; KOG1050; Eukaryota.
DR HOGENOM; CLU_002351_3_1_1; -.
DR InParanoid; Q0WUI9; -.
DR OMA; DCEWKNI; -.
DR OrthoDB; 772297at2759; -.
DR PhylomeDB; Q0WUI9; -.
DR BioCyc; ARA:AT1G70290-MON; -.
DR PRO; PR:Q0WUI9; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q0WUI9; baseline and differential.
DR Genevisible; Q0WUI9; 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 2: Evidence at transcript level;
KW Glycosyltransferase; Phosphoprotein; Reference proteome; Transferase.
FT CHAIN 1..856
FT /note="Probable alpha,alpha-trehalose-phosphate synthase
FT [UDP-forming] 8"
FT /id="PRO_0000324829"
FT REGION 57..541
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 856 AA; 97561 MW; 7AA5627BF8307A7C CRC64;
MVSRSCANFL DLSSWDLLDF PQTPRTLPRV MTVPGIITDV DGDTTSEVTS TSGGSRERKI
IVANMLPLQS KRDAETGKWC FNWDEDSLQL QLRDGFSSET EFLYVGSLNV DIETNEQEEV
SQKLLEEFNC VATFLSQELQ EMFYLGFCKH QLWPLFHYML PMFPDHGDRF DRRLWQAYVS
ANKIFSDRVM EVINPEDDYV WIQDYHLMVL PTFLRKRFNR IKLGFFLHSP FPSSEIYRTL
PVRDEILRGL LNCDLIGFHT FDYARHFLSC CSRMLGLDYE SKRGHIGLDY FGRTVYIKIL
PVGVHMGRLE SVLSLDSTAA KTKEIQEQFK GKKLVLGIDD MDIFKGISLK LIAMEHLFET
YWHLKGKVVL VQIVNPARSS GKDVEEAKRE TYETARRINE RYGTSDYKPI VLIDRLVPRS
EKTAYYAAAD CCLVNAVRDG MNLVPYKYIV CRQGTRSNKA VVDSSPRTST LVVSEFIGCS
PSLSGAIRVN PWDVDAVAEA VNSALKMSET EKQLRHEKHY HYISTHDVGY WAKSFMQDLE
RACRDHYSKR CWGIGFGLGF RVLSLSPSFR KLSVEHIVPV YRKTQRRAIF LDYDGTLVPE
SSIVQDPSNE VVSVLKALCE DPNNTVFIVS GRGRESLSNW LSPCENLGIA AEHGYFIRWK
SKDEWETCYS PTDTEWRSMV EPVMRSYMEA TDGTSIEFKE SALVWHHQDA DPDFGSCQAK
EMLDHLESVL ANEPVVVKRG QHIVEVKPQG VSKGLAAEKV IREMVERGEP PEMVMCIGDD
RSDEDMFESI LSTVTNPELL VQPEVFACTV GRKPSKAKYF LDDEADVLKL LRGLGDSSSS
LKPSSSHTQV AFESIV
