TPS9_ARATH
ID TPS9_ARATH Reviewed; 867 AA.
AC Q9LRA7;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 123.
DE RecName: Full=Probable alpha,alpha-trehalose-phosphate synthase [UDP-forming] 9;
DE EC=2.4.1.15;
DE AltName: Full=Trehalose-6-phosphate synthase 9;
DE Short=AtTPS9;
GN Name=TPS9; OrderedLocusNames=At1g23870; ORFNames=T23E23.3;
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=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 [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 NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=cv. Columbia;
RX PubMed=14593172; DOI=10.1126/science.1088305;
RA Yamada K., Lim J., Dale J.M., Chen H., Shinn P., Palm C.J., Southwick A.M.,
RA Wu H.C., Kim C.J., Nguyen M., Pham P.K., Cheuk R.F., Karlin-Newmann G.,
RA Liu S.X., Lam B., Sakano H., Wu T., Yu G., Miranda M., Quach H.L.,
RA Tripp M., Chang C.H., Lee J.M., Toriumi M.J., Chan M.M., Tang C.C.,
RA Onodera C.S., Deng J.M., Akiyama K., Ansari Y., Arakawa T., Banh J.,
RA Banno F., Bowser L., Brooks S.Y., Carninci P., Chao Q., Choy N., Enju A.,
RA Goldsmith A.D., Gurjal M., Hansen N.F., Hayashizaki Y., Johnson-Hopson C.,
RA Hsuan V.W., Iida K., Karnes M., Khan S., Koesema E., Ishida J., Jiang P.X.,
RA Jones T., Kawai J., Kamiya A., Meyers C., Nakajima M., Narusaka M.,
RA Seki M., Sakurai T., Satou M., Tamse R., Vaysberg M., Wallender E.K.,
RA Wong C., Yamamura Y., Yuan S., Shinozaki K., Davis R.W., Theologis A.,
RA Ecker J.R.;
RT "Empirical analysis of transcriptional activity in the Arabidopsis
RT genome.";
RL Science 302:842-846(2003).
RN [4]
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 -!- 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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AC002423; AAF87136.1; -; Genomic_DNA.
DR EMBL; CP002684; AEE30444.1; -; Genomic_DNA.
DR EMBL; AY072210; AAL60031.1; -; mRNA.
DR EMBL; AY096366; AAM20007.1; -; mRNA.
DR RefSeq; NP_173799.1; NM_102235.2.
DR AlphaFoldDB; Q9LRA7; -.
DR SMR; Q9LRA7; -.
DR IntAct; Q9LRA7; 1.
DR STRING; 3702.AT1G23870.1; -.
DR CAZy; GT20; Glycosyltransferase Family 20.
DR iPTMnet; Q9LRA7; -.
DR PaxDb; Q9LRA7; -.
DR PRIDE; Q9LRA7; -.
DR ProteomicsDB; 228385; -.
DR EnsemblPlants; AT1G23870.1; AT1G23870.1; AT1G23870.
DR GeneID; 838998; -.
DR Gramene; AT1G23870.1; AT1G23870.1; AT1G23870.
DR KEGG; ath:AT1G23870; -.
DR Araport; AT1G23870; -.
DR TAIR; locus:2199847; AT1G23870.
DR eggNOG; KOG1050; Eukaryota.
DR HOGENOM; CLU_002351_3_1_1; -.
DR InParanoid; Q9LRA7; -.
DR OMA; NWKRDDV; -.
DR OrthoDB; 772297at2759; -.
DR PhylomeDB; Q9LRA7; -.
DR PRO; PR:Q9LRA7; -.
DR Proteomes; UP000006548; Chromosome 1.
DR ExpressionAtlas; Q9LRA7; baseline and differential.
DR Genevisible; Q9LRA7; 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..867
FT /note="Probable alpha,alpha-trehalose-phosphate synthase
FT [UDP-forming] 9"
FT /id="PRO_0000324830"
FT REGION 59..546
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 867 AA; 98496 MW; 606736BC2B78FE81 CRC64;
MVSRSCANFL DLASWDLLDF PQTQRALPRV MTVPGIISEL DGGYSDGSSD VNSSNSSRER
KIIVANMLPL QAKRDTETGQ WCFSWDEDSL LLQLRDGFSS DTEFVYIGSL NADIGISEQE
EVSHKLLLDF NCVPTFLPKE MQEKFYLGFC KHHLWPLFHY MLPMFPDHGD RFDRRLWQAY
VSANKIFSDR VMEVINPEED YVWIHDYHLM VLPTFLRKRF NRIKLGFFLH SPFPSSEIYR
TLPVRDDLLR GLLNCDLIGF HTFDYARHFL SCCSRMLGLD YESKRGHIGL DYFGRTVFIK
ILPVGIHMGR LESVLNLPST AAKMKEIQEQ FKGKKLILGV DDMDIFKGIS LKLIAMERLF
ETYWHMRGKL VLIQIVNPAR ATGKDVEEAK KETYSTAKRI NERYGSAGYQ PVILIDRLVP
RYEKTAYYAM ADCCLVNAVR DGMNLVPYKY IICRQGTPGM DKAMGISHDS ARTSMLVVSE
FIGCSPSLSG AIRVNPWDVD AVAEAVNLAL TMGETEKRLR HEKHYHYVST HDVGYWAKSF
MQDLERACRE HYNKRCWGIG FGLSFRVLSL SPSFRKLSID HIVSTYRNTQ RRAIFLDYDG
TLVPESSIIK TPNAEVLSVL KSLCGDPKNT VFVVSGRGWE SLSDWLSPCE NLGIAAEHGY
FIRWSSKKEW ETCYSSAEAE WKTMVEPVMR SYMDATDGST IEYKESALVW HHQDADPDFG
ACQAKELLDH LESVLANEPV VVKRGQHIVE VKPQGVSKGL AVEKVIHQMV EDGNPPDMVM
CIGDDRSDED MFESILSTVT NPDLPMPPEI FACTVGRKPS KAKYFLDDVS DVLKLLGGLA
AATSSSKPEY QQQSSSLHTQ VAFESII
