TPS1_PICAN
ID TPS1_PICAN Reviewed; 475 AA.
AC O94213;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 60.
DE RecName: Full=Alpha,alpha-trehalose-phosphate synthase [UDP-forming];
DE EC=2.4.1.15 {ECO:0000305|PubMed:10419968};
DE AltName: Full=Trehalose-6-phosphate synthase;
DE AltName: Full=UDP-glucose-glucosephosphate glucosyltransferase;
GN Name=TPS1 {ECO:0000303|PubMed:10419968};
OS Pichia angusta (Yeast) (Hansenula polymorpha).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Pichiaceae; Ogataea.
OX NCBI_TaxID=870730;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, INDUCTION,
RP AND DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 34438 / CBS 4732 / DSM 70277 / JCM 3621 / NBRC 1476 / NRRL
RC Y-5445;
RX PubMed=10419968; DOI=10.1128/jb.181.15.4665-4668.1999;
RA Reinders A., Romano I., Wiemken A., De Virgilio C.;
RT "The thermophilic yeast hansenula polymorpha does not require trehalose
RT synthesis for growth at high temperatures but does for normal acquisition
RT of thermotolerance.";
RL J. Bacteriol. 181:4665-4668(1999).
CC -!- FUNCTION: Synthase catalytic subunit of the trehalose synthase complex
CC that catalyzes the production of trehalose from glucose-6-phosphate and
CC UDP-alpha-D-glucose in a two step process.
CC {ECO:0000269|PubMed:10419968}.
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:0000305|PubMed:10419968};
CC -!- PATHWAY: Carbohydrate biosynthesis. {ECO:0000305}.
CC -!- INDUCTION: Induced during thermal stress (at protein level).
CC {ECO:0000269|PubMed:10419968}.
CC -!- DISRUPTION PHENOTYPE: Abolishes trehalose biosynthesis.
CC {ECO:0000269|PubMed:10419968}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 20 family.
CC {ECO:0000305}.
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DR EMBL; AJ010725; CAB38058.1; -; Genomic_DNA.
DR AlphaFoldDB; O94213; -.
DR SMR; O94213; -.
DR CAZy; GT20; Glycosyltransferase Family 20.
DR PhylomeDB; O94213; -.
DR GO; GO:0003825; F:alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0102986; F:trehalose synthase activity; IGI:UniProtKB.
DR GO; GO:0005992; P:trehalose biosynthetic process; IGI:UniProtKB.
DR CDD; cd03788; GT20_TPS; 1.
DR InterPro; IPR001830; Glyco_trans_20.
DR InterPro; IPR012766; Trehalose_OtsA.
DR PANTHER; PTHR10788; PTHR10788; 1.
DR Pfam; PF00982; Glyco_transf_20; 1.
DR TIGRFAMs; TIGR02400; trehalose_OtsA; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Transferase.
FT CHAIN 1..475
FT /note="Alpha,alpha-trehalose-phosphate synthase [UDP-
FT forming]"
FT /id="PRO_0000122499"
FT BINDING 93
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 147
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 285
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 285
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 290
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 290
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 323
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 384..392
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 388..392
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
SQ SEQUENCE 475 AA; 54407 MW; 14F1A07AE88E12AB CRC64;
MVKGNVIVVS NRIPVTIKKT EDDENGKSRY DYTMSSGGLV TALQGLKNPF RWFGWPGMSV
DSEQGRQTVE RDLKEKFNCY PIWLSDEIAD LHYNGFSNSI LWPLFHYHPG EMNFDEIAWA
AYLEANKLFC QTILKEIKDG DVIWVHDYHL MLLPSLLRDQ LNSKGLPNVK IGFFLHTPFP
SSEIYRILPV RKEILEGVLS CDLIGFHTYD YVRHFLSSVE RILKLRTSPQ GVVYNDRQVT
VSAYPIGIDV DKFLNGLKTD EVKSRIKQLE TRFGKDCKLI IGVDRLDYIK GVPQKLHAFE
IFLERHPEWI GKVVLIQVAV PSRGDVEEYQ SLRAAVNELV GRINGRFGTV EFVPIHFLHK
SVNFQELISV YAASDVCVVS STRDGMNLVS YEYIACQQDR KGSLVLSEFA GAAQSLNGAL
VVNPWNTEEL SEAIYEGLIM SEEKRRGNFQ KMFKYIEKYT ASYWGENFVK ELTRV
