TPS1A_ASPNG
ID TPS1A_ASPNG Reviewed; 517 AA.
AC Q00075;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 77.
DE RecName: Full=Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 1;
DE EC=2.4.1.15 {ECO:0000305|PubMed:9006911};
DE AltName: Full=Trehalose-6-phosphate synthase;
DE AltName: Full=UDP-glucose-glucosephosphate glucosyltransferase;
GN Name=tpsA {ECO:0000303|PubMed:9006911}; Synonyms=tps1;
OS Aspergillus niger.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=5061;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP DISRUPTION PHENOTYPE.
RC STRAIN=ATCC 11414 / NRRL 2270 / VTT D-77050 / A-1-233;
RX PubMed=9006911; DOI=10.1074/jbc.272.5.2729;
RA Wolschek M.F., Kubicek C.P.;
RT "The filamentous fungus Aspergillus niger contains two 'differentially
RT regulated' trehalose-6-phosphate synthase-encoding genes, tpsA and tpsB.";
RL J. Biol. Chem. 272:2729-2735(1997).
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:9006911}.
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:9006911};
CC -!- PATHWAY: Carbohydrate biosynthesis. {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Decreases cellular trehalose level during hyphal
CC growth (PubMed:9006911). Sensitive to therml stress (PubMed:9006911).
CC {ECO:0000269|PubMed:9006911}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 20 family.
CC {ECO:0000305}.
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DR EMBL; U07184; AAA21861.1; -; Unassigned_DNA.
DR AlphaFoldDB; Q00075; -.
DR SMR; Q00075; -.
DR STRING; 5061.CADANGAP00007233; -.
DR CAZy; GT20; Glycosyltransferase Family 20.
DR PRIDE; Q00075; -.
DR VEuPathDB; FungiDB:An08g10510; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1180293; -.
DR VEuPathDB; FungiDB:ATCC64974_98360; -.
DR VEuPathDB; FungiDB:M747DRAFT_315913; -.
DR eggNOG; KOG1050; Eukaryota.
DR GO; GO:0003825; F:alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0102986; F:trehalose synthase activity; IMP:UniProtKB.
DR GO; GO:0005992; P:trehalose biosynthetic process; IMP: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..517
FT /note="Alpha,alpha-trehalose-phosphate synthase [UDP-
FT forming] 1"
FT /id="PRO_0000122494"
FT REGION 486..517
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 493..517
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 98
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 152
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 288
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 288
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 293
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 293
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 326
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 387..395
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 391..395
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
SQ SEQUENCE 517 AA; 58376 MW; 8EF38ED40D66A1CC CRC64;
MPSLENPTFQ NEARLLLVSN RLPITIKRSD DGRYDFSMSS GGLVSGLSGL SKSTTFQWYG
WPGLEVPEEE IPVVKERLKQ EYNAVPVFID DELADRHYNG FSNSILWPLF HYHPGEITFD
ESAWEAYKEA NRLFAKAVAK EVQDGDLIWV HDYHLMLLPE MLREEIGDSK ENVKIGFFLH
TPFPSSEIYR ILPVRNELLL GVLHCDLIGF HTYDYTRHFL SACSRLLGLT TTPNGIEFQG
KIIACGAFPI GIDPEKFEEG LKKEKVQKRI AMLEQKFQGV KLMVGVDRLD YIKGVPQKLH
ALEVFLSDHP EWVGKVVLVQ VAVPSRQDVE EYQNLRAVVN ELVGRINGKF GTVEFMPIHF
LHKSVNFDEL IALYAVSDAC IVSSTRDGMN LVAYEYIATQ KKRHGVLVLS EFAGAAQSLN
GSIIINPWNT EELAGAYQEA VTMSDEQRAL NFSKLDKYVN KYTSAFWGQS FVTELTRISE
HSAEKFHAKK ASFSDNNSEN GEPSNGVETP AQEQVAQ
