TPS1B_ASPNG
ID TPS1B_ASPNG Reviewed; 480 AA.
AC Q00217;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 1.
DT 03-AUG-2022, entry version 82.
DE RecName: Full=Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 2;
DE EC=2.4.1.15 {ECO:0000250|UniProtKB:Q00764};
DE AltName: Full=Trehalose-6-phosphate synthase;
DE AltName: Full=UDP-glucose-glucosephosphate glucosyltransferase;
GN Name=tpsB {ECO:0000303|PubMed:9006911};
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], AND INDUCTION.
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:0000250|UniProtKB:Q00764}.
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:0000250|UniProtKB:Q00764};
CC -!- PATHWAY: Carbohydrate biosynthesis. {ECO:0000305}.
CC -!- INDUCTION: Induced by thermal stress. {ECO:0000269|PubMed:9006911}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 20 family.
CC {ECO:0000305}.
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DR EMBL; U63416; AAB05869.1; -; Genomic_DNA.
DR AlphaFoldDB; Q00217; -.
DR SMR; Q00217; -.
DR STRING; 5061.CADANGAP00006023; -.
DR CAZy; GT20; Glycosyltransferase Family 20.
DR VEuPathDB; FungiDB:An07g08710; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1105321; -.
DR VEuPathDB; FungiDB:ATCC64974_49340; -.
DR VEuPathDB; FungiDB:M747DRAFT_141122; -.
DR eggNOG; KOG1050; Eukaryota.
DR GO; GO:0003825; F:alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0005992; P:trehalose biosynthetic process; IEA:InterPro.
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 2: Evidence at transcript level;
KW Glycosyltransferase; Transferase.
FT CHAIN 1..480
FT /note="Alpha,alpha-trehalose-phosphate synthase [UDP-
FT forming] 2"
FT /id="PRO_0000122495"
FT BINDING 97
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 151
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 480 AA; 53886 MW; DD0E89A1FF7F4C22 CRC64;
MAANGSSSEG DHRLLIVSNR LPITIRRSGG GKYEFSMSSG GLVTGLSGLS KTTTFQWYGW
PGLEVPEDEI DSVKQRLQEE FNATPVFMDD KLADRHYNGF SNSILWPLLH YHPGEIVFDE
AAWDAYREAN RLFAKTIAHE AREGDLVWVH DYHLMLLPEV LREELAALGK NNIRIGFFLH
TPFPSSEIYR ILPVRSQLLR GVLQCDLIGF HTYDYARHFL SCCSHILGLV TTPSSVKFKD
RSVAVGAFPI GIDPDKFTEG LKSPKVQNRI ASLENKFQGT KLMVSVDRLD YIKGIPQKLH
ALEVFLSQHP EWVGKVVLVQ VAVPSRQDVE EYQNLRAVVN ELVGRINGKF GTVDYMPIHF
MHKSVSFDEL IALYAASDAC VVSSTRDGMN LVSFEYVATQ QKRKGVLILS EFAGAAQSLN
GSIVVNPWNT EELASAYHEA VSMSDDLRAQ KFEKLYKYIS KYTSAFWGKS FVAELSKCST
