TPS1_EMENI
ID TPS1_EMENI Reviewed; 504 AA.
AC O59921; C8VG92; Q5B1Q7;
DT 06-JUN-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Alpha,alpha-trehalose-phosphate synthase [UDP-forming];
DE EC=2.4.1.15 {ECO:0000250|UniProtKB:Q00764};
DE AltName: Full=Trehalose-6-phosphate synthase;
DE AltName: Full=UDP-glucose-glucosephosphate glucosyltransferase;
GN Name=tpsA; ORFNames=AN5523;
OS Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS M139) (Aspergillus nidulans).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Nidulantes.
OX NCBI_TaxID=227321;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA d'Enfert C., Wolschek M., Kubicek C.;
RT "Characterization of the Aspergillus nidulans tpsA gene encoding trehalose-
RT 6-phosphate synthase.";
RL Submitted (JAN-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=16372000; DOI=10.1038/nature04341;
RA Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT fumigatus and A. oryzae.";
RL Nature 438:1105-1115(2005).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA Oliver S.G., Turner G.;
RT "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT effort.";
RL Fungal Genet. Biol. 46:S2-13(2009).
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.
CC {ECO:0000250|UniProtKB:Q00764}.
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:0000250|UniProtKB:Q00764};
CC -!- PATHWAY: Carbohydrate biosynthesis. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 20 family.
CC {ECO:0000305}.
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DR EMBL; AF043230; AAC18060.1; -; Genomic_DNA.
DR EMBL; AACD01000094; EAA62683.1; -; Genomic_DNA.
DR EMBL; BN001305; CBF81745.1; -; Genomic_DNA.
DR RefSeq; XP_663127.1; XM_658035.1.
DR AlphaFoldDB; O59921; -.
DR SMR; O59921; -.
DR STRING; 162425.CADANIAP00003562; -.
DR CAZy; GT20; Glycosyltransferase Family 20.
DR PRIDE; O59921; -.
DR EnsemblFungi; CBF81745; CBF81745; ANIA_05523.
DR EnsemblFungi; EAA62683; EAA62683; AN5523.2.
DR GeneID; 2871815; -.
DR KEGG; ani:AN5523.2; -.
DR VEuPathDB; FungiDB:AN5523; -.
DR eggNOG; KOG1050; Eukaryota.
DR HOGENOM; CLU_002351_7_2_1; -.
DR InParanoid; O59921; -.
DR OMA; YYGFSNR; -.
DR OrthoDB; 772297at2759; -.
DR Proteomes; UP000000560; Chromosome V.
DR Proteomes; UP000005890; Unassembled WGS sequence.
DR GO; GO:0005946; C:alpha,alpha-trehalose-phosphate synthase complex (UDP-forming); ISS:AspGD.
DR GO; GO:0003825; F:alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity; IMP:AspGD.
DR GO; GO:0030437; P:ascospore formation; IEA:EnsemblFungi.
DR GO; GO:0044262; P:cellular carbohydrate metabolic process; IMP:AspGD.
DR GO; GO:0034605; P:cellular response to heat; IDA:AspGD.
DR GO; GO:0070301; P:cellular response to hydrogen peroxide; IDA:AspGD.
DR GO; GO:0005992; P:trehalose biosynthetic process; IMP:AspGD.
DR GO; GO:0005993; P:trehalose catabolic process; IEA:EnsemblFungi.
DR GO; GO:0070413; P:trehalose metabolism in response to stress; IBA:GO_Central.
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 3: Inferred from homology;
KW Glycosyltransferase; Reference proteome; Transferase.
FT CHAIN 1..504
FT /note="Alpha,alpha-trehalose-phosphate synthase [UDP-
FT forming]"
FT /id="PRO_0000122497"
FT REGION 482..504
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 490..504
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 97
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 151
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 287
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 287
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 292
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 292
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 325
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 386..394
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 390..394
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
SQ SEQUENCE 504 AA; 56801 MW; 2CC239AF768BCA94 CRC64;
MPGVEKSSQN ESRLLLVSNR LPITIKRSED GKYDFSMSSG GLVSGLSGLS KTTTFQWYGW
PGLEVPEEEI PTLKNRLKEE YNAIPVFIDD ELADRHYNGF SNSILWPLFH YHPGEITFDE
SAWEAYKEAN RLFAQAVASQ VQDGDLIWVH DYHLMLLPEM LREEIGNTKK NIKIGFFLHT
PFPSSEIYRI LPVRNELLLG LLHCDLIGFH TYDYTRHFLS ACSRLLGLPT TPNGIEFQGK
IIACGAFPIG IDPEKFKEGL KKEKVQKRIA TLEQKFQGVK LMVGVDRLDY IKGVPQKLHA
LEVFLSDHPE WVGKVVLVQV AVPSRQDVEE YQNLRAVVNE LVGRINGKFG TVEFMPIHFL
HKSVNFDELI ALYAVSDACV VSSTRDGMNL VSYEYIATQE KRHGSLVLSE FAGAAQSLNG
SIIVNPWNTE ELAAAYHEAV TMSDEQRALN FSKLDKYVNK YTSAFWGQSF VTELTRISEQ
AAGKLPTKET PVNGETSKLE TSSQ
