ID   A0A100IQ14_ASPNG        Unreviewed;       855 AA.
AC   A0A100IQ14;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 27.
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   ORFNames=ABL_07929 {ECO:0000313|EMBL:GAQ45268.1};
OS   Aspergillus niger.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=5061 {ECO:0000313|EMBL:GAQ45268.1, ECO:0000313|Proteomes:UP000068243};
RN   [1] {ECO:0000313|Proteomes:UP000068243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=An76 {ECO:0000313|Proteomes:UP000068243};
RX   PubMed=26893421; DOI=10.1128/genomeA.01700-15;
RA   Gong W., Cheng Z., Zhang H., Liu L., Gao P., Wang L.;
RT   "Draft genome sequence of Aspergillus niger strain An76.";
RL   Genome Announc. 4:E0170015-E0170015(2016).
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   -!- PATHWAY: Carbohydrate biosynthesis. {ECO:0000256|ARBA:ARBA00024331}.
CC   -!- SIMILARITY: Belongs to the universal ribosomal protein uS17 family.
CC       {ECO:0000256|ARBA:ARBA00010254}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:GAQ45268.1}.
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DR   EMBL; BCMY01000015; GAQ45268.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A100IQ14; -.
DR   VEuPathDB; FungiDB:An08g10500; -.
DR   VEuPathDB; FungiDB:An08g10510; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1043184; -.
DR   VEuPathDB; FungiDB:ASPNIDRAFT2_1180293; -.
DR   VEuPathDB; FungiDB:ATCC64974_98360; -.
DR   VEuPathDB; FungiDB:ATCC64974_98370; -.
DR   VEuPathDB; FungiDB:M747DRAFT_296606; -.
DR   VEuPathDB; FungiDB:M747DRAFT_315913; -.
DR   Proteomes; UP000068243; Unassembled WGS sequence.
DR   GO; GO:0005840; C:ribosome; IEA:InterPro.
DR   GO; GO:0003825; F:alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity; IEA:UniProtKB-EC.
DR   GO; GO:0003735; F:structural constituent of ribosome; IEA:InterPro.
DR   GO; GO:0006412; P:translation; IEA:InterPro.
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   Gene3D; 2.40.50.140; Nucleic acid-binding proteins; 1.
DR   InterPro; IPR001830; Glyco_trans_20.
DR   InterPro; IPR012340; NA-bd_OB-fold.
DR   InterPro; IPR000266; Ribosomal_uS17.
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   Pfam; PF00366; Ribosomal_S17; 1.
DR   SUPFAM; SSF50249; Nucleic acid-binding proteins; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
KW   Glycosyltransferase {ECO:0000256|ARBA:ARBA00022676};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   REGION          486..516
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          643..662
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          675..710
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          815..837
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        493..512
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   855 AA;  96632 MW;  5E40343A1CB1CB7B CRC64;
     MPSLENPTFQ SEARLLLVSN RLPITIKRSD DGRYDFSMSS GGLVSGLSGL SKSTTFQWYG
     WPGLEVPEEE IPVVKQRLKQ EYNAVPVFID DELADRHYNG FSNSILWPLF HYHPGEITFD
     ESAWEAYKEA NRLFAKAVAK EVQDGDLIWV HDYHLMLLPE MLREEIGHSK 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 GERSNGVDTP DQEQVAQGLH FADTLRRMRG EEWDAKYANM
     PEISEILGEL IRGRDAPPAW TASLAASPIT LNFSRRIPKA DNSCRTRCPA PPQRLQKLPS
     KRIDLAVLPP QHHLYNQRSI RSFKYTTTMR PANFLRALQP LRSSMMRSTT TTSSTTAPSL
     YQTTLRSLTT TVPRLNEQQQ QQPQQQEADL SSSTTTTTTA VPPSLRSYPY KTKTGTVVSV
     GRMDRTVRVS HRHTIWDAHI QKPYPKITNY LVSDPRNSLR EGDVIEFSSG YPKSRNVRHV
     VERIIAPFGS AIEDRPAVLT REERDAERAA KRAAKWERRE ARRAEAGVSE SEGKGGEHVG
     RIRRLVLERT GGVEV
//