ID   Q2UDZ5_ASPOR            Unreviewed;       928 AA.
AC   Q2UDZ5;
DT   24-JAN-2006, integrated into UniProtKB/TrEMBL.
DT   24-JAN-2006, sequence version 1.
DT   13-SEP-2023, entry version 79.
DE   RecName: Full=Trehalose-6-phosphate synthase component TPS1 {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AO090026000820 {ECO:0000313|EMBL:BAE60220.1};
OS   Aspergillus oryzae (strain ATCC 42149 / RIB 40) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=510516 {ECO:0000313|EMBL:BAE60220.1, ECO:0000313|Proteomes:UP000006564};
RN   [1] {ECO:0000313|EMBL:BAE60220.1, ECO:0000313|Proteomes:UP000006564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 42149 / RIB 40 {ECO:0000313|Proteomes:UP000006564};
RX   PubMed=16372010; DOI=10.1038/nature04300;
RA   Machida M., Asai K., Sano M., Tanaka T., Kumagai T., Terai G., Kusumoto K.,
RA   Arima T., Akita O., Kashiwagi Y., Abe K., Gomi K., Horiuchi H.,
RA   Kitamoto K., Kobayashi T., Takeuchi M., Denning D.W., Galagan J.E.,
RA   Nierman W.C., Yu J., Archer D.B., Bennett J.W., Bhatnagar D.,
RA   Cleveland T.E., Fedorova N.D., Gotoh O., Horikawa H., Hosoyama A.,
RA   Ichinomiya M., Igarashi R., Iwashita K., Juvvadi P.R., Kato M., Kato Y.,
RA   Kin T., Kokubun A., Maeda H., Maeyama N., Maruyama J., Nagasaki H.,
RA   Nakajima T., Oda K., Okada K., Paulsen I., Sakamoto K., Sawano T.,
RA   Takahashi M., Takase K., Terabayashi Y., Wortman J., Yamada O.,
RA   Yamagata Y., Anazawa H., Hata Y., Koide Y., Komori T., Koyama Y.,
RA   Minetoki T., Suharnan S., Tanaka A., Isono K., Kuhara S., Ogasawara N.,
RA   Kikuchi H.;
RT   "Genome sequencing and analysis of Aspergillus oryzae.";
RL   Nature 438:1157-1161(2005).
CC   -!- SIMILARITY: In the C-terminal section; belongs to the trehalose
CC       phosphatase family. {ECO:0000256|ARBA:ARBA00006330}.
CC   -!- SIMILARITY: In the N-terminal section; belongs to the
CC       glycosyltransferase 20 family. {ECO:0000256|ARBA:ARBA00005409}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP007159; BAE60220.1; -; Genomic_DNA.
DR   RefSeq; XP_001822222.1; XM_001822170.2.
DR   AlphaFoldDB; Q2UDZ5; -.
DR   STRING; 510516.Q2UDZ5; -.
DR   CAZy; GT20; Glycosyltransferase Family 20.
DR   EnsemblFungi; BAE60220; BAE60220; AO090026000820.
DR   GeneID; 5994250; -.
DR   KEGG; aor:AO090026000820; -.
DR   VEuPathDB; FungiDB:AO090026000820; -.
DR   HOGENOM; CLU_002351_2_2_1; -.
DR   OMA; TSWDKRR; -.
DR   OrthoDB; 1023at2759; -.
DR   Proteomes; UP000006564; Chromosome 3.
DR   GO; GO:0003824; F:catalytic activity; 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; 3.40.50.1000; HAD superfamily/HAD-like; 1.
DR   InterPro; IPR001830; Glyco_trans_20.
DR   InterPro; IPR036412; HAD-like_sf.
DR   InterPro; IPR006379; HAD-SF_hydro_IIB.
DR   InterPro; IPR023214; HAD_sf.
DR   InterPro; IPR003337; Trehalose_PPase.
DR   NCBIfam; TIGR01484; HAD-SF-IIB; 1.
DR   NCBIfam; TIGR00685; T6PP; 1.
DR   PANTHER; PTHR10788:SF15; TREHALOSE SYNTHASE COMPLEX REGULATORY SUBUNIT TPS3-RELATED; 1.
DR   PANTHER; PTHR10788; TREHALOSE-6-PHOSPHATE SYNTHASE; 1.
DR   Pfam; PF00982; Glyco_transf_20; 1.
DR   Pfam; PF02358; Trehalose_PPase; 1.
DR   SUPFAM; SSF56784; HAD-like; 1.
DR   SUPFAM; SSF53756; UDP-Glycosyltransferase/glycogen phosphorylase; 1.
PE   3: Inferred from homology;
KW   Reference proteome {ECO:0000313|Proteomes:UP000006564}.
FT   REGION          23..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          76..178
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        88..121
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   928 AA;  104253 MW;  33DEF0EB44710095 CRC64;
     MTIYIASLFL PYTVNFHLNE SKDRPLHTGS EPSETGAEAS ASTASAAVSL FERQNRDQKV
     GLTPGATTEH ERIFSSDLAK AEQEHSGYPF PDTTQDGSLL TESEAHSPAW GSTLSLNQPR
     PRATIPPSPS ILKHQEPFAP MTEPSPKKSD KEQKPLYTQR PSGVHHSREP SRKGSFSSAE
     WTIETAEQGN GGLRNAVRSA TDAGQLEDKV WVGTLGMPTD ALSKYTKSAI AEKLEDEYDS
     LTVYVSDGDF DGHYTHFCKT ILWPVFHYQI PDNPKSKAYE DHSWVYYVKT NQAFAERIAR
     NWKRGDSIWI QDYHLLLVPA MLRKLLPDAQ IGFFLHIAFP SSEVFRCLAP RKELLEGILG
     ANLVGFQTEE YCRHFLQTCS RILCVEATNE GVQLEDRFVN VNKFPIGIDP TSWDKRRKAT
     DVEQWVKTIS ERYEGKRLIV SRDKIDGVRG IRQKLLSYEL FLNTYPEWRD QVVLIQVATS
     TTEQPELEAT ISDIAMRINS TFSTLAHQPL VFLKQDLAFP QYLALISVAD ALMITSLREG
     MNLTSHEFVY CQDGKYGNKK YGSLILSEFT GSASVFGNHA LLVNPWNYRQ CAEAIHTALS
     RSEEERKQVW TQLHSAVLQN STANWVKSFS ETLNRVWNEQ SSREIMAVPR LSVGKLEEAY
     RRSSRRLIIV DYEGTLASWG SPKSIIVTTP QRAITTLTEL TEDPRNIVFV MSSRMPEEME
     RLFRMVAGLG LIAENGCFVR EPKTDEWFKL TNKAQTDAWK EAVRQILGYY QERAEGSWIE
     QRHCSLMLHY GSAEDQAAAS RLASECADHI NDSCANQGVH AVMMNGALVV EPADTNKASA
     AAMVWRHCLE RSKSDHSGRP DFLMAIGDGR DDEPVFRWAN KLENAKGVDY AMTVTLGSRS
     TEAKATLTQG VTGVLSCLER LAASSLEQ
//