TPS1_BOTFB
ID TPS1_BOTFB Reviewed; 523 AA.
AC A0A384JAD8; Q156F5;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 07-NOV-2018, sequence version 1.
DT 03-AUG-2022, entry version 15.
DE RecName: Full=Alpha,alpha-trehalose-phosphate synthase [UDP-forming] {ECO:0000305};
DE EC=2.4.1.15 {ECO:0000305|PubMed:16946258};
DE AltName: Full=Trehalose-6-phosphate synthase {ECO:0000255|RuleBase:RU362045};
DE AltName: Full=UDP-glucose-glucosephosphate glucosyltransferase {ECO:0000255|RuleBase:RU362045};
GN Name=TPS1 {ECO:0000303|PubMed:16946258};
GN Synonyms=Bctps1 {ECO:0000303|PubMed:16946258};
GN ORFNames=BCIN_02g08340 {ECO:0000312|EMBL:ATZ47566.1};
OS Botryotinia fuckeliana (strain B05.10) (Noble rot fungus) (Botrytis
OS cinerea).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Helotiales; Sclerotiniaceae; Botrytis.
OX NCBI_TaxID=332648 {ECO:0000312|Proteomes:UP000001798};
RN [1] {ECO:0000312|EMBL:ABG25558.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP DISRUPTION PHENOTYPE.
RX PubMed=16946258; DOI=10.1099/mic.0.29044-0;
RA Doehlemann G., Berndt P., Hahn M.;
RT "Trehalose metabolism is important for heat stress tolerance and spore
RT germination of Botrytis cinerea.";
RL Microbiology 152:2625-2634(2006).
RN [2] {ECO:0000312|Proteomes:UP000001798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B05.10 {ECO:0000312|Proteomes:UP000001798};
RX PubMed=21876677; DOI=10.1371/journal.pgen.1002230;
RA Amselem J., Cuomo C.A., van Kan J.A.L., Viaud M., Benito E.P., Couloux A.,
RA Coutinho P.M., de Vries R.P., Dyer P.S., Fillinger S., Fournier E.,
RA Gout L., Hahn M., Kohn L., Lapalu N., Plummer K.M., Pradier J.-M.,
RA Quevillon E., Sharon A., Simon A., ten Have A., Tudzynski B., Tudzynski P.,
RA Wincker P., Andrew M., Anthouard V., Beever R.E., Beffa R., Benoit I.,
RA Bouzid O., Brault B., Chen Z., Choquer M., Collemare J., Cotton P.,
RA Danchin E.G., Da Silva C., Gautier A., Giraud C., Giraud T., Gonzalez C.,
RA Grossetete S., Gueldener U., Henrissat B., Howlett B.J., Kodira C.,
RA Kretschmer M., Lappartient A., Leroch M., Levis C., Mauceli E.,
RA Neuveglise C., Oeser B., Pearson M., Poulain J., Poussereau N.,
RA Quesneville H., Rascle C., Schumacher J., Segurens B., Sexton A., Silva E.,
RA Sirven C., Soanes D.M., Talbot N.J., Templeton M., Yandava C., Yarden O.,
RA Zeng Q., Rollins J.A., Lebrun M.-H., Dickman M.;
RT "Genomic analysis of the necrotrophic fungal pathogens Sclerotinia
RT sclerotiorum and Botrytis cinerea.";
RL PLoS Genet. 7:E1002230-E1002230(2011).
RN [3] {ECO:0000312|Proteomes:UP000001798}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B05.10 {ECO:0000312|Proteomes:UP000001798};
RX PubMed=26913498; DOI=10.1111/mpp.12384;
RA van Kan J.A.L., Stassen J.H.M., Mosbach A., van der Lee T.A.J., Faino L.,
RA Farmer A.D., Papasotiriou D.G., Zhou S., Seidl M.F., Cottam E., Edel D.,
RA Hahn M., Schwartz D.C., Dietrich R.A., Widdison S., Scalliet G.;
RT "A gapless genome sequence of the fungus Botrytis cinerea.";
RL Mol. Plant Pathol. 18:75-89(2017).
CC -!- FUNCTION: Synthase catalytic subunit of the trehalose synthase complex
CC that catalyzes the production of trehalose from glucose-6-phosphate and
CC UDP-alpha-D-glucose in a two step process (PubMed:16946258). The
CC disaccharide trehalose serves as a storage carbohydrate that is
CC mobilized during conidial germination (PubMed:16946258). Trehalose also
CC serves as a protectant for cell integrity during stress
CC (PubMed:16946258). {ECO:0000269|PubMed:16946258}.
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:0000305|PubMed:16946258};
CC -!- PATHWAY: Carbohydrate biosynthesis. {ECO:0000305}.
CC -!- DISRUPTION PHENOTYPE: Decreases cellular trehalose level
CC (PubMed:16946258). Sensitive to thermal stress (PubMed:16946258).
CC Abnormal conidial germination on glucose or fructose carbon sources
CC (PubMed:16946258). {ECO:0000269|PubMed:16946258}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 20 family.
CC {ECO:0000305}.
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DR EMBL; DQ632610; ABG25558.1; -; Genomic_DNA.
DR EMBL; CP009806; ATZ47566.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A384JAD8; -.
DR SMR; A0A384JAD8; -.
DR CAZy; GT20; Glycosyltransferase Family 20.
DR VEuPathDB; FungiDB:Bcin02g08340; -.
DR PHI-base; PHI:650; -.
DR Proteomes; UP000001798; Chromosome bcin02.
DR GO; GO:0005946; C:alpha,alpha-trehalose-phosphate synthase complex (UDP-forming); IEA:EnsemblFungi.
DR GO; GO:0003825; F:alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0102986; F:trehalose synthase activity; IMP:UniProtKB.
DR GO; GO:0030437; P:ascospore formation; IEA:EnsemblFungi.
DR GO; GO:0005992; P:trehalose biosynthetic process; IMP:UniProtKB.
DR GO; GO:0005993; P:trehalose catabolic process; IEA:EnsemblFungi.
DR GO; GO:0070413; P:trehalose metabolism in response to stress; IEA:EnsemblFungi.
DR CDD; cd03788; GT20_TPS; 1.
DR InterPro; IPR001830; Glyco_trans_20.
DR InterPro; IPR012766; Trehalose_OtsA.
DR PANTHER; PTHR10788; PTHR10788; 1.
DR Pfam; PF00982; Glyco_transf_20; 1.
DR TIGRFAMs; TIGR02400; trehalose_OtsA; 1.
PE 1: Evidence at protein level;
KW Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..523
FT /note="Alpha,alpha-trehalose-phosphate synthase [UDP-
FT forming]"
FT /id="PRO_0000453072"
FT REGION 503..523
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 98
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 152
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 288
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 288
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 293
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 293
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 326
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 387..395
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 391..395
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
SQ SEQUENCE 523 AA; 59350 MW; 7661EA6C4C26F11F CRC64;
MPSVAGEEPK ASSRLLLVSN RLPITIKRTE DGQYDFTGSS GGLVTGLSGL AKTTTFQWYG
WPGLEVPDAE AKPLVKRLKD EHGAHPVFVD DELADKHYNG FSNSILWPLF HYHPGEITFD
ESQWMAYKEV NRLFAKTIAK DVQDGDLIWV HDYHLMLLPE MLRDEIGTSK KNVKIGFFLH
TPFPSSEIYR ILPVRESLLL SVLHCDLIGF HTYDYARHFL SSCSRILETQ TTPNGVEFRG
KYVTVAAFPI GIDPEKFIET LKKPKVEERI AQLERKFEGV KLIVGVDRLD YIKGVPQKLH
ALEVFLTEHP EWIGKVVLVQ VAVPSRQDVE EYQNLRAVVN ELVGRINGRF GTVEFMPIHF
LHQSVNFDEL TALYAVSDAC LVSSTRDGMN LVSYEYIATQ RKRHGVMILS EFTGAAQSLN
GALIVNPWNT EELADAIHDA VTMSPEQREI NFKKLEKYVF KYTSSWWGES FVSELQRISE
HAAKKSNSKG TVDKMPDLVE GVQQFNLGEQ REEGRLEPGE FDD
