ID D8T2E5_SELML Unreviewed; 991 AA.
AC D8T2E5;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=alpha,alpha-trehalose-phosphate synthase (UDP-forming) {ECO:0000256|ARBA:ARBA00012538};
DE EC=2.4.1.15 {ECO:0000256|ARBA:ARBA00012538};
GN Name=TPS2 {ECO:0000313|EMBL:EFJ09193.1};
GN ORFNames=SELMODRAFT_184811 {ECO:0000313|EMBL:EFJ09193.1};
OS Selaginella moellendorffii (Spikemoss).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Lycopodiopsida; Selaginellales; Selaginellaceae; Selaginella.
OX NCBI_TaxID=88036 {ECO:0000313|Proteomes:UP000001514};
RN [1] {ECO:0000313|EMBL:EFJ09193.1, ECO:0000313|Proteomes:UP000001514}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=21551031; DOI=10.1126/science.1203810;
RA Banks J.A., Nishiyama T., Hasebe M., Bowman J.L., Gribskov M.,
RA dePamphilis C., Albert V.A., Aono N., Aoyama T., Ambrose B.A., Ashton N.W.,
RA Axtell M.J., Barker E., Barker M.S., Bennetzen J.L., Bonawitz N.D.,
RA Chapple C., Cheng C., Correa L.G., Dacre M., DeBarry J., Dreyer I.,
RA Elias M., Engstrom E.M., Estelle M., Feng L., Finet C., Floyd S.K.,
RA Frommer W.B., Fujita T., Gramzow L., Gutensohn M., Harholt J., Hattori M.,
RA Heyl A., Hirai T., Hiwatashi Y., Ishikawa M., Iwata M., Karol K.G.,
RA Koehler B., Kolukisaoglu U., Kubo M., Kurata T., Lalonde S., Li K., Li Y.,
RA Litt A., Lyons E., Manning G., Maruyama T., Michael T.P., Mikami K.,
RA Miyazaki S., Morinaga S., Murata T., Mueller-Roeber B., Nelson D.R.,
RA Obara M., Oguri Y., Olmstead R.G., Onodera N., Petersen B.L., Pils B.,
RA Prigge M., Rensing S.A., Riano-Pachon D.M., Roberts A.W., Sato Y.,
RA Scheller H.V., Schulz B., Schulz C., Shakirov E.V., Shibagaki N.,
RA Shinohara N., Shippen D.E., Soerensen I., Sotooka R., Sugimoto N.,
RA Sugita M., Sumikawa N., Tanurdzic M., Theissen G., Ulvskov P., Wakazuki S.,
RA Weng J.K., Willats W.W., Wipf D., Wolf P.G., Yang L., Zimmer A.D., Zhu Q.,
RA Mitros T., Hellsten U., Loque D., Otillar R., Salamov A., Schmutz J.,
RA Shapiro H., Lindquist E., Lucas S., Rokhsar D., Grigoriev I.V.;
RT "The Selaginella genome identifies genetic changes associated with the
RT evolution of vascular plants.";
RL Science 332:960-963(2011).
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 Evidence={ECO:0000256|ARBA:ARBA00001516};
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 20 family. {ECO:0000256|ARBA:ARBA00005409}.
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DR EMBL; GL377665; EFJ09193.1; -; Genomic_DNA.
DR RefSeq; XP_002989716.1; XM_002989670.1.
DR AlphaFoldDB; D8T2E5; -.
DR STRING; 88036.D8T2E5; -.
DR EnsemblPlants; EFJ09193; EFJ09193; SELMODRAFT_184811.
DR GeneID; 9628963; -.
DR Gramene; EFJ09193; EFJ09193; SELMODRAFT_184811.
DR KEGG; smo:SELMODRAFT_184811; -.
DR eggNOG; KOG1050; Eukaryota.
DR HOGENOM; CLU_002351_0_1_1; -.
DR InParanoid; D8T2E5; -.
DR OMA; HTASHWG; -.
DR OrthoDB; 1023at2759; -.
DR Proteomes; UP000001514; Unassembled WGS sequence.
DR GO; GO:0003825; F:alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity; IBA:GO_Central.
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 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; 1.
DR InterPro; IPR001830; Glyco_trans_20.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR012766; Trehalose_OtsA.
DR InterPro; IPR003337; Trehalose_PPase.
DR NCBIfam; TIGR00685; T6PP; 1.
DR NCBIfam; TIGR02400; trehalose_OtsA; 1.
DR PANTHER; PTHR10788:SF106; BCDNA.GH08860; 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.
PE 3: Inferred from homology;
KW Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW Reference proteome {ECO:0000313|Proteomes:UP000001514};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT REGION 1..117
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 877..908
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 969..991
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 49..67
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 97..111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 893..908
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 991 AA; 111318 MW; 9CC76F367A871BA6 CRC64;
MPQYPPLNSQ DDDPVGKPQP RRKEAAVAAA APFVPPNLNL PPSLASSRVE RLVRERQLRR
SERASASEDA IDEDDAADQP QEQPPADNIS LEHQARDDNP PPSQQQQEDL PADQGGGEKQ
RLLVVANRLP VSATRKGDTQ WSLEVSAGGL VSALLGVKQF QVIWIGWPGV YVQDDVGRQS
LAQALEEKGF VGVLLDEATV DQYYNGYCNN VLWPLFHYIG LRQEDRLAAT RSLQSQFNAY
KRANQLFADA VIKNYQEGDF VWCHDYHLMV LPSYLKEYNS HMKVGWFLHT PFPSSEIYRT
LPLRAELLQG VLAADLVGFH TYDYARHFVS ACTRILGLEG TPEGVEDQGK ITRVAAFPVG
IDSERFTHAV ETEAVKQHIQ ELSARFAGRK VMLGVDRLDM IKGIPQKLLA FEKFLEENPE
WRDKVILVQI AVPTRTDVLE YQKLASQVHE IVGRINGRYG SLTTVPIHHL DRSMKFPELC
ALYAITDVLL VTSLRDGMNL VSYEFVACQN VKKGALVLSE FAGAAQSLGA GSILINPWNI
IESANAIAEA LNMPEEEREE RHRHNFMHVT THSAQVWAET FTRQVLLFSF LFLNSRTYST
SEMNDSILEA ELRTLHIPPQ LPTEKAIANY SASKNRLMIL GFNSTLTAQV EAPRGRAPDQ
IREMKIRLHP NLKEVFNVLC TDPKTTIVIL SGSERAVLDE AFGEFDMWLA AENGMFLRHT
QGEWMTTMPE HLNMDWVESV QLVFEYFCER TPRSFVETRE TSLVWNYKYA DVEFGRVQAR
DMLQHLWTGP ISNAAVDVVQ GGKSVEVRPV GVSKGSAIDR ILGEIVHSKH MLSPIDHVMC
IGHFLSKDED IYTFFEPELP FLDAAVFSSK LQDKRVSKSS SKHGSSRHAK SHPATMSPDR
KRSEEEQLIE EAGRWEGSSV LDLKGENYFS CAVGASKRSL ARYCLNSSDE VVTFLSSLAA
ATETFPKKES FKKSGWHSPT PRSPRVVTVS N
//
