TPS1_CANAL
ID TPS1_CANAL Reviewed; 478 AA.
AC Q92410; A0A1D8PT23; Q59PS4;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=Alpha,alpha-trehalose-phosphate synthase [UDP-forming];
DE EC=2.4.1.15 {ECO:0000269|PubMed:28743811, ECO:0000305|PubMed:9683476};
DE AltName: Full=Trehalose-6-phosphate synthase;
DE AltName: Full=UDP-glucose-glucosephosphate glucosyltransferase;
GN Name=TPS1 {ECO:0000303|PubMed:9683476}; OrderedLocusNames=CAALFM_CR05720WA;
GN ORFNames=CaO19.13961, CaO19.6640;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=9683476; DOI=10.1128/jb.180.15.3809-3815.1998;
RA Zaragoza O., Blazquez M.A., Gancedo C.;
RT "Disruption of the Candida albicans TPS1 gene encoding trehalose-6-
RT phosphate synthase impairs formation of hyphae and decreases infectivity.";
RL J. Bacteriol. 180:3809-3815(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [5] {ECO:0007744|PDB:5HUT, ECO:0007744|PDB:5HUU, ECO:0007744|PDB:5HUV, ECO:0007744|PDB:5HVL}
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS) IN COMPLEXES WITH
RP UDP-ALPHA-D-GLUCOSE; D-GLUCOSE-6-PHOSPHATE AND UDP, FUNCTION, ACTIVITY
RP REGULATION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, AND MUTAGENESIS OF
RP TYR-89; LYS-285; ASP-379 AND GLU-387.
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.
CC {ECO:0000269|PubMed:28743811, ECO:0000269|PubMed:9683476}.
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:0000269|PubMed:28743811, ECO:0000305|PubMed:9683476};
CC -!- ACTIVITY REGULATION: Inhibited by validoxylamine A, a non-reactive
CC trehalose analog. {ECO:0000269|PubMed:28743811}.
CC -!- PATHWAY: Carbohydrate biosynthesis. {ECO:0000305}.
CC -!- INDUCTION: By heat shock.
CC -!- DISRUPTION PHENOTYPE: Abolishes hyphal formation and impairs biofilm
CC formation (PubMed:28743811). Sensitive to thermal stress
CC (PubMed:28743811). {ECO:0000269|PubMed:28743811}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase 20 family.
CC {ECO:0000305}.
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DR EMBL; Y07918; CAA69223.1; -; Genomic_DNA.
DR EMBL; CP017630; AOW31288.1; -; Genomic_DNA.
DR RefSeq; XP_711706.1; XM_706614.2.
DR PDB; 5HUT; X-ray; 1.90 A; A/B=1-478.
DR PDB; 5HUU; X-ray; 2.37 A; A/B=1-478.
DR PDB; 5HUV; X-ray; 2.00 A; A/B=1-478.
DR PDB; 5HVL; X-ray; 1.80 A; A/B=1-478.
DR PDBsum; 5HUT; -.
DR PDBsum; 5HUU; -.
DR PDBsum; 5HUV; -.
DR PDBsum; 5HVL; -.
DR AlphaFoldDB; Q92410; -.
DR SMR; Q92410; -.
DR BioGRID; 1229305; 2.
DR STRING; 237561.Q92410; -.
DR CAZy; GT20; Glycosyltransferase Family 20.
DR PRIDE; Q92410; -.
DR GeneID; 3646699; -.
DR KEGG; cal:CAALFM_CR05720WA; -.
DR CGD; CAL0000182821; TPS1.
DR VEuPathDB; FungiDB:CR_05720W_A; -.
DR eggNOG; KOG1050; Eukaryota.
DR HOGENOM; CLU_002351_7_2_1; -.
DR InParanoid; Q92410; -.
DR OMA; YYGFSNR; -.
DR OrthoDB; 772297at2759; -.
DR BRENDA; 2.4.1.15; 1096.
DR PHI-base; PHI:130; -.
DR PRO; PR:Q92410; -.
DR Proteomes; UP000000559; Chromosome R.
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; IDA:CGD.
DR GO; GO:0004805; F:trehalose-phosphatase activity; IEA:EnsemblFungi.
DR GO; GO:0071465; P:cellular response to desiccation; IEA:EnsemblFungi.
DR GO; GO:0034605; P:cellular response to heat; IMP:CGD.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0036180; P:filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR GO; GO:0036168; P:filamentous growth of a population of unicellular organisms in response to heat; IMP:CGD.
DR GO; GO:0005992; P:trehalose biosynthetic process; IMP:CGD.
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; Reference proteome; Stress response;
KW Transferase.
FT CHAIN 1..478
FT /note="Alpha,alpha-trehalose-phosphate synthase [UDP-
FT forming]"
FT /id="PRO_0000122496"
FT BINDING 89
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000269|PubMed:28743811,
FT ECO:0007744|PDB:5HUU"
FT BINDING 143
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000269|PubMed:28743811,
FT ECO:0007744|PDB:5HUU"
FT BINDING 280
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000269|PubMed:28743811,
FT ECO:0007744|PDB:5HUU"
FT BINDING 280
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000269|PubMed:28743811,
FT ECO:0007744|PDB:5HUT"
FT BINDING 285
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000269|PubMed:28743811,
FT ECO:0007744|PDB:5HUU"
FT BINDING 285
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000269|PubMed:28743811,
FT ECO:0007744|PDB:5HUT"
FT BINDING 318
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000269|PubMed:28743811,
FT ECO:0007744|PDB:5HUU"
FT BINDING 357
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000269|PubMed:28743811,
FT ECO:0007744|PDB:5HUU"
FT BINDING 357
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000269|PubMed:28743811,
FT ECO:0007744|PDB:5HUT"
FT BINDING 379..387
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000269|PubMed:28743811,
FT ECO:0007744|PDB:5HUT"
FT BINDING 383..387
FT /ligand="UDP"
FT /ligand_id="ChEBI:CHEBI:58223"
FT /evidence="ECO:0000269|PubMed:28743811,
FT ECO:0007744|PDB:5HUU"
FT MUTAGEN 89
FT /note="Y->F: Abolishes catalytic activity. Mildly impairs
FT biofilm and hyphal formation. Sensitive to thermal stress."
FT /evidence="ECO:0000269|PubMed:28743811"
FT MUTAGEN 285
FT /note="K->A: Abolishes catalytic activity. Impairs biofilm
FT and hyphal formation. Sensitive to thermal stress."
FT /evidence="ECO:0000269|PubMed:28743811"
FT MUTAGEN 379
FT /note="D->A: Abolishes catalytic activity. Impairs biofilm
FT and hyphal formation. Sensitive to thermal stress."
FT /evidence="ECO:0000269|PubMed:28743811"
FT MUTAGEN 387
FT /note="E->A: Abolishes catalytic activity. Impairs biofilm
FT and hyphal formation. Sensitive to thermal stress."
FT /evidence="ECO:0000269|PubMed:28743811"
FT STRAND 6..12
FT /evidence="ECO:0007829|PDB:5HVL"
FT STRAND 14..19
FT /evidence="ECO:0007829|PDB:5HVL"
FT STRAND 21..23
FT /evidence="ECO:0007829|PDB:5HUV"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:5HVL"
FT HELIX 33..37
FT /evidence="ECO:0007829|PDB:5HVL"
FT HELIX 39..42
FT /evidence="ECO:0007829|PDB:5HVL"
FT STRAND 43..45
FT /evidence="ECO:0007829|PDB:5HUT"
FT STRAND 47..52
FT /evidence="ECO:0007829|PDB:5HVL"
FT HELIX 59..61
FT /evidence="ECO:0007829|PDB:5HVL"
FT HELIX 62..73
FT /evidence="ECO:0007829|PDB:5HVL"
FT STRAND 74..77
FT /evidence="ECO:0007829|PDB:5HVL"
FT HELIX 82..89
FT /evidence="ECO:0007829|PDB:5HVL"
FT HELIX 90..96
FT /evidence="ECO:0007829|PDB:5HVL"
FT HELIX 97..101
FT /evidence="ECO:0007829|PDB:5HVL"
FT HELIX 105..107
FT /evidence="ECO:0007829|PDB:5HVL"
FT HELIX 112..130
FT /evidence="ECO:0007829|PDB:5HVL"
FT STRAND 138..143
FT /evidence="ECO:0007829|PDB:5HVL"
FT HELIX 144..146
FT /evidence="ECO:0007829|PDB:5HVL"
FT HELIX 149..157
FT /evidence="ECO:0007829|PDB:5HVL"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:5HVL"
FT STRAND 165..169
FT /evidence="ECO:0007829|PDB:5HVL"
FT HELIX 177..180
FT /evidence="ECO:0007829|PDB:5HVL"
FT HELIX 186..193
FT /evidence="ECO:0007829|PDB:5HVL"
FT STRAND 197..203
FT /evidence="ECO:0007829|PDB:5HVL"
FT HELIX 204..217
FT /evidence="ECO:0007829|PDB:5HVL"
FT STRAND 221..224
FT /evidence="ECO:0007829|PDB:5HVL"
FT STRAND 227..230
FT /evidence="ECO:0007829|PDB:5HVL"
FT STRAND 233..239
FT /evidence="ECO:0007829|PDB:5HVL"
FT HELIX 246..252
FT /evidence="ECO:0007829|PDB:5HVL"
FT HELIX 256..268
FT /evidence="ECO:0007829|PDB:5HVL"
FT TURN 269..271
FT /evidence="ECO:0007829|PDB:5HVL"
FT STRAND 272..281
FT /evidence="ECO:0007829|PDB:5HVL"
FT HELIX 283..285
FT /evidence="ECO:0007829|PDB:5HVL"
FT HELIX 287..300
FT /evidence="ECO:0007829|PDB:5HVL"
FT HELIX 302..304
FT /evidence="ECO:0007829|PDB:5HVL"
FT TURN 305..307
FT /evidence="ECO:0007829|PDB:5HVL"
FT STRAND 308..315
FT /evidence="ECO:0007829|PDB:5HVL"
FT HELIX 322..342
FT /evidence="ECO:0007829|PDB:5HVL"
FT STRAND 349..353
FT /evidence="ECO:0007829|PDB:5HVL"
FT HELIX 359..368
FT /evidence="ECO:0007829|PDB:5HVL"
FT STRAND 370..374
FT /evidence="ECO:0007829|PDB:5HVL"
FT STRAND 377..381
FT /evidence="ECO:0007829|PDB:5HVL"
FT HELIX 384..390
FT /evidence="ECO:0007829|PDB:5HVL"
FT TURN 393..395
FT /evidence="ECO:0007829|PDB:5HVL"
FT STRAND 398..402
FT /evidence="ECO:0007829|PDB:5HVL"
FT HELIX 406..409
FT /evidence="ECO:0007829|PDB:5HVL"
FT STRAND 414..417
FT /evidence="ECO:0007829|PDB:5HVL"
FT HELIX 422..434
FT /evidence="ECO:0007829|PDB:5HVL"
FT HELIX 437..453
FT /evidence="ECO:0007829|PDB:5HVL"
FT HELIX 456..469
FT /evidence="ECO:0007829|PDB:5HVL"
SQ SEQUENCE 478 AA; 54457 MW; 86CD64FB5AD7E86F CRC64;
MVQGKVLVVS NRIPVTIKRL DNGSYDYSMS SGGLVTALQG LKKTTEFQWY GWPGLEIPED
EQTKVNDELK 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
ELISLYNISD VCLVSSTRDG MNLVSYEYIA CQQDRKGVLI LSEFAGAAQS LNGALIVNPW
NTEDLSEAIK ESLTLPEEKR EFNFKKLFTY ISKYTSGFWG ESFVKELYKC NPQKSLRD
