TPS1A_ASPFU
ID TPS1A_ASPFU Reviewed; 515 AA.
AC Q4WLM9;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 1 {ECO:0000305};
DE EC=2.4.1.15 {ECO:0000305|PubMed:20439478};
DE AltName: Full=UDP-glucose-glucosephosphate glucosyltransferase {ECO:0000255|RuleBase:RU362045};
GN Name=tpsA {ECO:0000303|PubMed:20439478};
GN ORFNames=AFUA_6G12950 {ECO:0000312|EMBL:EAL89135.1};
OS Neosartorya fumigata (strain ATCC MYA-4609 / Af293 / CBS 101355 / FGSC
OS A1100) (Aspergillus fumigatus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Fumigati.
OX NCBI_TaxID=330879 {ECO:0000312|Proteomes:UP000002530};
RN [1] {ECO:0000312|Proteomes:UP000002530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC MYA-4609 / Af293 / CBS 101355 / FGSC A1100
RC {ECO:0000312|Proteomes:UP000002530};
RX PubMed=16372009; DOI=10.1038/nature04332;
RA Nierman W.C., Pain A., Anderson M.J., Wortman J.R., Kim H.S., Arroyo J.,
RA Berriman M., Abe K., Archer D.B., Bermejo C., Bennett J.W., Bowyer P.,
RA Chen D., Collins M., Coulsen R., Davies R., Dyer P.S., Farman M.L.,
RA Fedorova N., Fedorova N.D., Feldblyum T.V., Fischer R., Fosker N.,
RA Fraser A., Garcia J.L., Garcia M.J., Goble A., Goldman G.H., Gomi K.,
RA Griffith-Jones S., Gwilliam R., Haas B.J., Haas H., Harris D.E.,
RA Horiuchi H., Huang J., Humphray S., Jimenez J., Keller N., Khouri H.,
RA Kitamoto K., Kobayashi T., Konzack S., Kulkarni R., Kumagai T., Lafton A.,
RA Latge J.-P., Li W., Lord A., Lu C., Majoros W.H., May G.S., Miller B.L.,
RA Mohamoud Y., Molina M., Monod M., Mouyna I., Mulligan S., Murphy L.D.,
RA O'Neil S., Paulsen I., Penalva M.A., Pertea M., Price C., Pritchard B.L.,
RA Quail M.A., Rabbinowitsch E., Rawlins N., Rajandream M.A., Reichard U.,
RA Renauld H., Robson G.D., Rodriguez de Cordoba S., Rodriguez-Pena J.M.,
RA Ronning C.M., Rutter S., Salzberg S.L., Sanchez M., Sanchez-Ferrero J.C.,
RA Saunders D., Seeger K., Squares R., Squares S., Takeuchi M., Tekaia F.,
RA Turner G., Vazquez de Aldana C.R., Weidman J., White O., Woodward J.R.,
RA Yu J.-H., Fraser C.M., Galagan J.E., Asai K., Machida M., Hall N.,
RA Barrell B.G., Denning D.W.;
RT "Genomic sequence of the pathogenic and allergenic filamentous fungus
RT Aspergillus fumigatus.";
RL Nature 438:1151-1156(2005).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, DEVELOPMENTAL STAGE, AND DISRUPTION
RP PHENOTYPE.
RX PubMed=20439478; DOI=10.1128/iai.00813-09;
RA Al-Bader N., Vanier G., Liu H., Gravelat F.N., Urb M., Hoareau C.M.,
RA Campoli P., Chabot J., Filler S.G., Sheppard D.C.;
RT "Role of trehalose biosynthesis in Aspergillus fumigatus development,
RT stress response, and virulence.";
RL Infect. Immun. 78:3007-3018(2010).
RN [3] {ECO:0007744|PDB:5HVM}
RP X-RAY CRYSTALLOGRAPHY (2.81 ANGSTROMS) IN COMPLEX WITH UDP AND INHIBITOR.
RX PubMed=28743811; DOI=10.1128/mbio.00643-17;
RA Miao Y., Tenor J.L., Toffaletti D.L., Maskarinec S.A., Liu J., Lee R.E.,
RA Perfect J.R., Brennan R.G.;
RT "Structural and In Vivo Studies on Trehalose-6-Phosphate Synthase from
RT Pathogenic Fungi Provide Insights into Its Catalytic Mechanism, Biological
RT Necessity, and Potential for Novel Antifungal Drug Design.";
RL MBio 8:e00643-e00643(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:20439478). The
CC disaccharide trehalose serves as a storage carbohydrate that is
CC mobilized during conidial germination (PubMed:20439478). Regulates the
CC level of trehalose as a protectant for cell integrity during thermal
CC and oxidative stress (PubMed:20439478). {ECO:0000269|PubMed:20439478}.
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:20439478};
CC -!- PATHWAY: Carbohydrate biosynthesis. {ECO:0000305}.
CC -!- DEVELOPMENTAL STAGE: Increases during conidiation.
CC {ECO:0000269|PubMed:20439478}.
CC -!- DISRUPTION PHENOTYPE: Simultaneous disruption of tpsB abolishes
CC trehalose biosynthesis during hyphal and conidia formation, and delays
CC germination (PubMed:20439478). Simultaneous disruption of tpsB results
CC in abnormal cell wall formation, sensitivity to caspofungin, calcofluor
CC white, thermal stress and oxidative stress, and hypervirulence in a
CC mouse model of aspergillosis (PubMed:20439478).
CC {ECO:0000269|PubMed:20439478}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 20 family.
CC {ECO:0000305}.
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DR EMBL; AAHF01000006; EAL89135.1; -; Genomic_DNA.
DR RefSeq; XP_751173.1; XM_746080.1.
DR PDB; 5HVM; X-ray; 2.81 A; A/B=1-515.
DR PDBsum; 5HVM; -.
DR AlphaFoldDB; Q4WLM9; -.
DR SMR; Q4WLM9; -.
DR STRING; 746128.CADAFUBP00000174; -.
DR EnsemblFungi; EAL89135; EAL89135; AFUA_6G12950.
DR GeneID; 3508480; -.
DR KEGG; afm:AFUA_6G12950; -.
DR VEuPathDB; FungiDB:Afu6g12950; -.
DR eggNOG; KOG1050; Eukaryota.
DR HOGENOM; CLU_002351_7_2_1; -.
DR InParanoid; Q4WLM9; -.
DR OMA; YYGFSNR; -.
DR OrthoDB; 772297at2759; -.
DR BRENDA; 2.4.1.15; 508.
DR Proteomes; UP000002530; Chromosome 6.
DR GO; GO:0005946; C:alpha,alpha-trehalose-phosphate synthase complex (UDP-forming); IBA:GO_Central.
DR GO; GO:0003825; F:alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity; IBA:GO_Central.
DR GO; GO:0000166; F:nucleotide binding; IEA:UniProtKB-KW.
DR GO; GO:0102986; F:trehalose synthase activity; IMP:UniProtKB.
DR GO; GO:0044262; P:cellular carbohydrate metabolic process; IMP:AspGD.
DR GO; GO:0034605; P:cellular response to heat; IBA:GO_Central.
DR GO; GO:0005992; P:trehalose biosynthetic process; IMP:AspGD.
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 1: Evidence at protein level;
KW 3D-structure; Coiled coil; Glycosyltransferase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..515
FT /note="Alpha,alpha-trehalose-phosphate synthase [UDP-
FT forming] 1"
FT /id="PRO_0000453073"
FT REGION 483..515
FT /note="Disordered"
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:0000269|PubMed:28743811,
FT ECO:0007744|PDB:5HVM"
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:0000269|PubMed:28743811,
FT ECO:0007744|PDB:5HVM"
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 364
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000269|PubMed:28743811,
FT ECO:0007744|PDB:5HVM"
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:0000269|PubMed:28743811,
FT ECO:0007744|PDB:5HVM"
FT STRAND 14..20
FT /evidence="ECO:0007829|PDB:5HVM"
FT STRAND 26..28
FT /evidence="ECO:0007829|PDB:5HVM"
FT STRAND 56..60
FT /evidence="ECO:0007829|PDB:5HVM"
FT HELIX 72..80
FT /evidence="ECO:0007829|PDB:5HVM"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:5HVM"
FT HELIX 90..97
FT /evidence="ECO:0007829|PDB:5HVM"
FT HELIX 98..104
FT /evidence="ECO:0007829|PDB:5HVM"
FT HELIX 105..109
FT /evidence="ECO:0007829|PDB:5HVM"
FT HELIX 113..115
FT /evidence="ECO:0007829|PDB:5HVM"
FT HELIX 120..140
FT /evidence="ECO:0007829|PDB:5HVM"
FT STRAND 146..151
FT /evidence="ECO:0007829|PDB:5HVM"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:5HVM"
FT HELIX 157..165
FT /evidence="ECO:0007829|PDB:5HVM"
FT STRAND 168..171
FT /evidence="ECO:0007829|PDB:5HVM"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:5HVM"
FT HELIX 185..188
FT /evidence="ECO:0007829|PDB:5HVM"
FT HELIX 194..201
FT /evidence="ECO:0007829|PDB:5HVM"
FT STRAND 204..211
FT /evidence="ECO:0007829|PDB:5HVM"
FT HELIX 212..225
FT /evidence="ECO:0007829|PDB:5HVM"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:5HVM"
FT STRAND 240..246
FT /evidence="ECO:0007829|PDB:5HVM"
FT HELIX 253..259
FT /evidence="ECO:0007829|PDB:5HVM"
FT HELIX 263..275
FT /evidence="ECO:0007829|PDB:5HVM"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:5HVM"
FT STRAND 279..288
FT /evidence="ECO:0007829|PDB:5HVM"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:5HVM"
FT HELIX 294..307
FT /evidence="ECO:0007829|PDB:5HVM"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:5HVM"
FT TURN 312..314
FT /evidence="ECO:0007829|PDB:5HVM"
FT STRAND 315..322
FT /evidence="ECO:0007829|PDB:5HVM"
FT HELIX 329..349
FT /evidence="ECO:0007829|PDB:5HVM"
FT STRAND 356..360
FT /evidence="ECO:0007829|PDB:5HVM"
FT HELIX 366..375
FT /evidence="ECO:0007829|PDB:5HVM"
FT STRAND 377..381
FT /evidence="ECO:0007829|PDB:5HVM"
FT STRAND 384..387
FT /evidence="ECO:0007829|PDB:5HVM"
FT HELIX 391..397
FT /evidence="ECO:0007829|PDB:5HVM"
FT TURN 400..402
FT /evidence="ECO:0007829|PDB:5HVM"
FT STRAND 405..409
FT /evidence="ECO:0007829|PDB:5HVM"
FT HELIX 414..417
FT /evidence="ECO:0007829|PDB:5HVM"
FT STRAND 421..424
FT /evidence="ECO:0007829|PDB:5HVM"
FT HELIX 429..441
FT /evidence="ECO:0007829|PDB:5HVM"
FT HELIX 444..460
FT /evidence="ECO:0007829|PDB:5HVM"
FT HELIX 463..478
FT /evidence="ECO:0007829|PDB:5HVM"
SQ SEQUENCE 515 AA; 57919 MW; 298105A1BEC07AF7 CRC64;
MPSLENSTQN EARLLLVSNR LPITIKRSED GKYDFSMSSG GLVSGLSGLS KSTTFQWYGW
PGLEVPEEEI PVVKQRLKDE YGAIPVFIDD ELADRHYNGF SNSILWPLFH YHPGEITFDE
SAWEAYKEAN RLFAKAVAKE VQDGDLIWVH DYHLMLLPEM LREEIGDSKE NVKIGFFLHT
PFPSSEIYRI LPVRNELLLG VLHCDLIGFH TYDYTRHFLS ACSRLLGLAT TPNGIEFQGK
VIACGAFPIG IDPEKFQEGL KKEKVQKRIA QLEQKFQGVK LMVGVDRLDY IKGVPQKLHA
LEVFLSDHPE WVGKVVLVQV AVPSRQDVEE YQNLRAVVNE LVGRINGKFG TVEFMPIHFL
HKSVNFDELI ALYAVSDACI VSSTRDGMNL VAYEYIASQQ KRHGVLVLSE FAGAAQSLNG
SIIINPWNTE ELAGAYQEAV TMSDEQRALN FSKLDKYVNK YTSAFWGQSF VTELNRISAH
SAGKFQSRKA KLPESADAEK PMNGSGESEE SQTTQ
