TPS1B_ASPFU
ID TPS1B_ASPFU Reviewed; 479 AA.
AC Q4WHW0;
DT 02-JUN-2021, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 91.
DE RecName: Full=Alpha,alpha-trehalose-phosphate synthase [UDP-forming] 2 {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=tpsB {ECO:0000303|PubMed:20439478};
GN ORFNames=AFUA_2G04010 {ECO:0000312|EMBL:EAL87495.1};
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, INDUCTION, AND
RP DISRUPTION 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:5HVO}
RP X-RAY CRYSTALLOGRAPHY (2.47 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 -!- INDUCTION: Induced by thermal stress (PubMed:20439478). Repressed by
CC oxidative stress (PubMed:20439478). {ECO:0000269|PubMed:20439478}.
CC -!- DISRUPTION PHENOTYPE: Simultaneous disruption of tpsA abolishes
CC trehalose biosynthesis during hyphal and conidia formation, and delays
CC germination (PubMed:20439478). Simultaneous disruption of tpsA 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; AAHF01000008; EAL87495.1; -; Genomic_DNA.
DR RefSeq; XP_749533.1; XM_744440.1.
DR PDB; 5HVO; X-ray; 2.47 A; A/B/C/D=1-479.
DR PDBsum; 5HVO; -.
DR AlphaFoldDB; Q4WHW0; -.
DR SMR; Q4WHW0; -.
DR STRING; 746128.CADAFUBP00002057; -.
DR EnsemblFungi; EAL87495; EAL87495; AFUA_2G04010.
DR GeneID; 3506931; -.
DR KEGG; afm:AFUA_2G04010; -.
DR VEuPathDB; FungiDB:Afu2g04010; -.
DR eggNOG; KOG1050; Eukaryota.
DR HOGENOM; CLU_002351_7_2_1; -.
DR InParanoid; Q4WHW0; -.
DR OMA; HFSHTPW; -.
DR OrthoDB; 772297at2759; -.
DR Proteomes; UP000002530; Chromosome 2.
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; Glycosyltransferase; Nucleotide-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..479
FT /note="Alpha,alpha-trehalose-phosphate synthase [UDP-
FT forming] 2"
FT /id="PRO_0000453074"
FT BINDING 96
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:Q92410"
FT BINDING 150
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:5HVO"
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:5HVO"
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 363..364
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000269|PubMed:28743811,
FT ECO:0007744|PDB:5HVO"
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:5HVO"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:5HVO"
FT STRAND 21..25
FT /evidence="ECO:0007829|PDB:5HVO"
FT STRAND 33..36
FT /evidence="ECO:0007829|PDB:5HVO"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:5HVO"
FT HELIX 66..68
FT /evidence="ECO:0007829|PDB:5HVO"
FT HELIX 69..80
FT /evidence="ECO:0007829|PDB:5HVO"
FT STRAND 82..84
FT /evidence="ECO:0007829|PDB:5HVO"
FT HELIX 89..96
FT /evidence="ECO:0007829|PDB:5HVO"
FT HELIX 97..103
FT /evidence="ECO:0007829|PDB:5HVO"
FT HELIX 104..108
FT /evidence="ECO:0007829|PDB:5HVO"
FT HELIX 119..139
FT /evidence="ECO:0007829|PDB:5HVO"
FT STRAND 145..150
FT /evidence="ECO:0007829|PDB:5HVO"
FT HELIX 151..153
FT /evidence="ECO:0007829|PDB:5HVO"
FT HELIX 156..164
FT /evidence="ECO:0007829|PDB:5HVO"
FT TURN 165..168
FT /evidence="ECO:0007829|PDB:5HVO"
FT STRAND 173..177
FT /evidence="ECO:0007829|PDB:5HVO"
FT HELIX 185..188
FT /evidence="ECO:0007829|PDB:5HVO"
FT HELIX 194..201
FT /evidence="ECO:0007829|PDB:5HVO"
FT STRAND 205..211
FT /evidence="ECO:0007829|PDB:5HVO"
FT HELIX 212..225
FT /evidence="ECO:0007829|PDB:5HVO"
FT STRAND 234..237
FT /evidence="ECO:0007829|PDB:5HVO"
FT STRAND 240..246
FT /evidence="ECO:0007829|PDB:5HVO"
FT HELIX 253..260
FT /evidence="ECO:0007829|PDB:5HVO"
FT HELIX 263..275
FT /evidence="ECO:0007829|PDB:5HVO"
FT TURN 276..278
FT /evidence="ECO:0007829|PDB:5HVO"
FT STRAND 279..288
FT /evidence="ECO:0007829|PDB:5HVO"
FT HELIX 290..292
FT /evidence="ECO:0007829|PDB:5HVO"
FT HELIX 294..307
FT /evidence="ECO:0007829|PDB:5HVO"
FT HELIX 309..311
FT /evidence="ECO:0007829|PDB:5HVO"
FT TURN 312..314
FT /evidence="ECO:0007829|PDB:5HVO"
FT STRAND 315..322
FT /evidence="ECO:0007829|PDB:5HVO"
FT HELIX 329..349
FT /evidence="ECO:0007829|PDB:5HVO"
FT STRAND 356..360
FT /evidence="ECO:0007829|PDB:5HVO"
FT HELIX 366..375
FT /evidence="ECO:0007829|PDB:5HVO"
FT STRAND 377..381
FT /evidence="ECO:0007829|PDB:5HVO"
FT STRAND 384..387
FT /evidence="ECO:0007829|PDB:5HVO"
FT HELIX 391..397
FT /evidence="ECO:0007829|PDB:5HVO"
FT TURN 400..402
FT /evidence="ECO:0007829|PDB:5HVO"
FT STRAND 405..409
FT /evidence="ECO:0007829|PDB:5HVO"
FT HELIX 414..417
FT /evidence="ECO:0007829|PDB:5HVO"
FT STRAND 421..424
FT /evidence="ECO:0007829|PDB:5HVO"
FT HELIX 429..440
FT /evidence="ECO:0007829|PDB:5HVO"
FT HELIX 444..460
FT /evidence="ECO:0007829|PDB:5HVO"
FT HELIX 463..475
FT /evidence="ECO:0007829|PDB:5HVO"
SQ SEQUENCE 479 AA; 53801 MW; A9B44BEF54D455D4 CRC64;
MSSTNGSEGD HRLLIVSNRL PITIRRSEGG KYEFSMSSGG LVTGLSGLSK TTTFQWYGWP
GLEVPEDELG SVKKRLKDEF NATPVFMDDK LADRHYNGFS NSILWPLLHY HPGEIVFDEG
AWDAYREANL LFAKTIVKEA QDGDLIWVQD YHLMLLPELL RAELRAAGKK ANKIGFFLHT
PFPSSEIYRI LPVRGQLLRG VLHCDLIGFH TYDYARHFLS SCSHLLGLVT TPSSVKYEGR
SVAVGAFPIG IDPDKFTDGL KSPKVQNRIA SLENKFQGTK LMVSVDRLDY IKGIPQKLHA
LEVFLQNHPE WVGKVVLVQV AVPSRQDVEE YQNLRAVVNE LVGRINGKFG TVDYMPIHFM
HKSVSFDELI ALYAASDACV VSSTRDGMNL VSFEYIATQQ KRKGVLILSE FAGAAQSLNG
SLVVNPWNTE ELARAYHEAV SMSDEQRARK FEKLYKYISK YTSAFWGKSF VAELLQCSS
