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Database: UniProt
Entry: A2QSF2_ASPNC
LinkDB: A2QSF2_ASPNC
Original site: A2QSF2_ASPNC 
ID   A2QSF2_ASPNC            Unreviewed;       517 AA.
AC   A2QSF2;
DT   06-MAR-2007, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2007, sequence version 1.
DT   13-SEP-2023, entry version 80.
DE   RecName: Full=Trehalose-6-phosphate synthase {ECO:0000256|RuleBase:RU362045};
DE            EC=2.4.1.15 {ECO:0000256|RuleBase:RU362045};
DE   AltName: Full=UDP-glucose-glucosephosphate glucosyltransferase {ECO:0000256|RuleBase:RU362045};
GN   Name=tpsA {ECO:0000313|EMBL:CAK45724.1};
GN   ORFNames=An08g10510 {ECO:0000313|EMBL:CAK45724.1};
OS   Aspergillus niger (strain ATCC MYA-4892 / CBS 513.88 / FGSC A1513).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=425011 {ECO:0000313|EMBL:CAK45724.1, ECO:0000313|Proteomes:UP000006706};
RN   [1] {ECO:0000313|EMBL:CAK45724.1, ECO:0000313|Proteomes:UP000006706}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892
RC   {ECO:0000313|Proteomes:UP000006706};
RX   PubMed=17259976; DOI=10.1038/nbt1282;
RA   Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA   Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA   Bendtsen J.D., Benen J.A., van den Berg M., Breestraat S., Caddick M.X.,
RA   Contreras R., Cornell M., Coutinho P.M., Danchin E.G., Debets A.J.,
RA   Dekker P., van Dijck P.W., van Dijk A., Dijkhuizen L., Driessen A.J.,
RA   d'Enfert C., Geysens S., Goosen C., Groot G.S., de Groot P.W.,
RA   Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.,
RA   van den Hondel C.A., van der Heijden R.T., van der Kaaij R.M., Klis F.M.,
RA   Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA   van der Maarel M.J., Meulenberg R., Menke H., Mortimer M.A., Nielsen J.,
RA   Oliver S.G., Olsthoorn M., Pal K., van Peij N.N., Ram A.F., Rinas U.,
RA   Roubos J.A., Sagt C.M., Schmoll M., Sun J., Ussery D., Varga J.,
RA   Vervecken W., van de Vondervoort P.J., Wedler H., Wosten H.A., Zeng A.P.,
RA   van Ooyen A.J., Visser J., Stam H.;
RT   "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT   niger CBS 513.88.";
RL   Nat. Biotechnol. 25:221-231(2007).
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|RuleBase:RU362045};
CC   -!- PATHWAY: Carbohydrate biosynthesis. {ECO:0000256|ARBA:ARBA00024331}.
CC   -!- SIMILARITY: Belongs to the glycosyltransferase 20 family.
CC       {ECO:0000256|RuleBase:RU362045}.
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DR   EMBL; AM270183; CAK45724.1; -; Genomic_DNA.
DR   RefSeq; XP_001393155.1; XM_001393118.2.
DR   AlphaFoldDB; A2QSF2; -.
DR   CAZy; GT20; Glycosyltransferase Family 20.
DR   EnsemblFungi; CAK45724; CAK45724; An08g10510.
DR   GeneID; 4983365; -.
DR   KEGG; ang:ANI_1_1406074; -.
DR   VEuPathDB; FungiDB:An08g10510; -.
DR   HOGENOM; CLU_002351_7_1_1; -.
DR   OrthoDB; 1023at2759; -.
DR   Proteomes; UP000006706; Chromosome 8R.
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   Gene3D; 3.40.50.2000; Glycogen Phosphorylase B; 2.
DR   InterPro; IPR001830; Glyco_trans_20.
DR   InterPro; IPR012766; Trehalose_OtsA.
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   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676,
KW   ECO:0000256|RuleBase:RU362045};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006706};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362045}.
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"
SQ   SEQUENCE   517 AA;  58304 MW;  80C484A9590FBFFB CRC64;
     MPSLENPTFQ NEARLLLVSN RLPITIKRSD DGRYDFSMSS GGLVSGLSGL SKSTTFQWYG
     WPGLEVPEGE 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
//
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