ID H0EUI8_GLAL7 Unreviewed; 541 AA.
AC H0EUI8;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 40.
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 ORFNames=M7I_6423 {ECO:0000313|EMBL:EHK97764.1};
OS Glarea lozoyensis (strain ATCC 74030 / MF5533).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Helotiaceae; Glarea.
OX NCBI_TaxID=1104152 {ECO:0000313|EMBL:EHK97764.1, ECO:0000313|Proteomes:UP000005446};
RN [1] {ECO:0000313|EMBL:EHK97764.1, ECO:0000313|Proteomes:UP000005446}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 74030 / MF5533 {ECO:0000313|Proteomes:UP000005446};
RX PubMed=22302591; DOI=10.1128/EC.05302-11;
RA Youssar L., Gruening B.A., Erxleben A., Guenther S., Huettel W.;
RT "Genome sequence of the fungus Glarea lozoyensis: the first genome sequence
RT of a species from the Helotiaceae family.";
RL Eukaryot. Cell 11:250-250(2012).
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 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}.
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:EHK97764.1}.
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DR EMBL; AGUE01000177; EHK97764.1; -; Genomic_DNA.
DR AlphaFoldDB; H0EUI8; -.
DR HOGENOM; CLU_002351_7_1_1; -.
DR InParanoid; H0EUI8; -.
DR Proteomes; UP000005446; Unassembled WGS sequence.
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:UP000005446};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362045}.
FT REGION 497..541
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 499..541
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 541 AA; 60488 MW; 89D9D0E4A21105A6 CRC64;
MPALVQEDAK PQGRLLLVSN RLPITIKRSD DGTYAFSMSS GGLVTGLSGL SKTTTFQWYG
WPGLEVPDAE AAPLVKRLKD EYGAVPVFVE DDLADRHYNG FSNSILWPLF HYHPGEITFD
ESAWAAYKDV NRLFAKTMAK DVQDGDLIWV HDYHLMLLPE MLREEIGTSK KNVKIGFFLH
TPFPSIRESL LLGVLHCDLI GFHTYDYARH FLSSCSRILG TSTTPNGVDF NGKFVTVAAF
PIGIDPEKFV EGLQKKSVQD RIAVLERKFE GVKLIVGVDR LDYIKGVPQK LHALEVFLSE
HPEWVGKVVL VQVAVPSRQD VEEYQNLRAV VNELVGRING RFGTVEFMPI HFLHQSVSFE
ELTALYAVSD ACLVSSTRDG MNLVSYEYIA TQRARHGVMI LSEFTGAAQS LNGALIVNPW
NTEELAGAIH DAVTMSPESR EINFKKLEKY VFKYTSAWWG ESFVSELVRI SEHAEKKQKR
NAGSVAGKVQ GLVEGVKGMV VGKDEKENQD AGAKEERKHK SRHGDHQESP SSDGFDRPES
K
//
