ID B9WLZ4_CANDC Unreviewed; 478 AA.
AC B9WLZ4;
DT 24-MAR-2009, integrated into UniProtKB/TrEMBL.
DT 24-MAR-2009, sequence version 1.
DT 27-MAR-2024, entry version 74.
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=TPS1 {ECO:0000313|EMBL:CAX40107.1};
GN OrderedLocusNames=Cd36_31110 {ECO:0000313|CGD:CAL0000165763};
GN ORFNames=CD36_31110 {ECO:0000313|EMBL:CAX40107.1};
OS Candida dubliniensis (strain CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 /
OS NRRL Y-17841) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=573826 {ECO:0000313|EMBL:CAX40107.1, ECO:0000313|Proteomes:UP000002605};
RN [1] {ECO:0000313|EMBL:CAX40107.1, ECO:0000313|Proteomes:UP000002605}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CD36 / ATCC MYA-646 / CBS 7987 / NCPF 3949 / NRRL Y-17841
RC {ECO:0000313|Proteomes:UP000002605};
RX PubMed=19745113; DOI=10.1101/gr.097501.109;
RA Jackson A.P., Gamble J.A., Yeomans T., Moran G.P., Saunders D., Harris D.,
RA Aslett M., Barrell J.F., Butler G., Citiulo F., Coleman D.C.,
RA de Groot P.W.J., Goodwin T.J., Quail M.A., McQuillan J., Munro C.A.,
RA Pain A., Poulter R.T., Rajandream M.A., Renauld H., Spiering M.J.,
RA Tivey A., Gow N.A.R., Barrell B., Sullivan D.J., Berriman M.;
RT "Comparative genomics of the fungal pathogens Candida dubliniensis and
RT Candida albicans.";
RL Genome Res. 19:2231-2244(2009).
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}.
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DR EMBL; FM992695; CAX40107.1; -; Genomic_DNA.
DR RefSeq; XP_002422105.1; XM_002422060.1.
DR AlphaFoldDB; B9WLZ4; -.
DR CAZy; GT20; Glycosyltransferase Family 20.
DR GeneID; 8049735; -.
DR KEGG; cdu:CD36_31110; -.
DR CGD; CAL0000165763; Cd36_31110.
DR VEuPathDB; FungiDB:CD36_31110; -.
DR eggNOG; KOG1050; Eukaryota.
DR HOGENOM; CLU_002351_7_2_1; -.
DR OrthoDB; 1023at2759; -.
DR Proteomes; UP000002605; Chromosome R.
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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|RuleBase:RU362045}.
SQ SEQUENCE 478 AA; 54413 MW; 0D904900F466BBB9 CRC64;
MVQGKVLVVS NRIPVTIKRL DNGSYDYSMS SGGLVTALQG LKKTTEFQWY GWPGLEIPDD
EQAKVNEELK SKFNCTAIFL SDTIADLHYN GFSNSILWPL FHYHPGEMNF DENAWAAYIE
ANKKFALEIV KQVNDDDMIW VHDYHLMLLP EMLRQEIGNK KKNIKIGFFL HTPFPSSEIY
RILPVRKEIL EGVLSCDLIG FHTYDYARHF ISSVSRIVPN VSTLPNGIKY QGRSISIGAF
PIGIDVDNFI DGLKKDSVVE RIKQLKSKFK DVKVIVGVDR LDYIKGVPQK LHAFEVFLNE
NPEWIGKVVL VQVAVPSRGD VEEYQSLRST VSELVGRING EFGTVEFVPI HYLHKSIPFD
ELISLYNVSD VCLVSSTRDG MNLVSYEYIA CQQDRKGVLI LSEFAGAAQS LNGALIVNPW
NTEDLSEAIK ESLTLPEEKR EFNFKKLFTY ISKYTSGFWG ESFVKELYKC NPQKSLRD
//
