TPSP_THETK
ID TPSP_THETK Reviewed; 731 AA.
AC G4RK44; Q704C6;
DT 11-DEC-2013, integrated into UniProtKB/Swiss-Prot.
DT 14-DEC-2011, sequence version 1.
DT 03-AUG-2022, entry version 50.
DE RecName: Full=Bifunctional trehalose-6-phosphate synthase/phosphatase {ECO:0000303|PubMed:23626675};
DE Includes:
DE RecName: Full=Alpha,alpha-trehalose-phosphate synthase [UDP-forming];
DE EC=2.4.1.15 {ECO:0000269|PubMed:23626675};
DE AltName: Full=Trehalose-6-phosphate synthase {ECO:0000303|PubMed:23626675};
DE Includes:
DE RecName: Full=Trehalose-6-phosphate phosphatase {ECO:0000303|PubMed:23626675};
DE EC=3.1.3.12 {ECO:0000269|PubMed:23626675};
GN Name=tpsp {ECO:0000312|EMBL:CCC81939.1}; OrderedLocusNames=TTX_1304;
OS Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435
OS / Kra 1).
OC Archaea; Crenarchaeota; Thermoprotei; Thermoproteales; Thermoproteaceae;
OC Thermoproteus.
OX NCBI_TaxID=768679;
RN [1] {ECO:0000312|EMBL:CAF18468.1}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND IDENTIFICATION.
RC STRAIN=ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1
RC {ECO:0000269|PubMed:15028704};
RX PubMed=15028704; DOI=10.1128/jb.186.7.2179-2194.2004;
RA Siebers B., Tjaden B., Michalke K., Doerr C., Ahmed H., Zaparty M.,
RA Gordon P., Sensen C.W., Zibat A., Klenk H.-P., Schuster S.C., Hensel R.;
RT "Reconstruction of the central carbohydrate metabolism of Thermoproteus
RT tenax using genomic and biochemical data.";
RL J. Bacteriol. 186:2179-2194(2004).
RN [2] {ECO:0000312|EMBL:CCC81939.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1;
RX PubMed=22003381; DOI=10.1371/journal.pone.0024222;
RA Siebers B., Zaparty M., Raddatz G., Tjaden B., Albers S.V., Bell S.D.,
RA Blombach F., Kletzin A., Kyrpides N., Lanz C., Plagens A., Rampp M.,
RA Rosinus A., von Jan M., Makarova K.S., Klenk H.P., Schuster S.C.,
RA Hensel R.;
RT "The complete genome sequence of Thermoproteus tenax: a physiologically
RT versatile member of the Crenarchaeota.";
RL PLoS ONE 6:E24222-E24222(2011).
RN [3] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL
RP PROPERTIES, AND PATHWAY.
RC STRAIN=ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1
RC {ECO:0000269|PubMed:23626675};
RX PubMed=23626675; DOI=10.1371/journal.pone.0061354;
RA Zaparty M., Hagemann A., Brasen C., Hensel R., Lupas A.N., Brinkmann H.,
RA Siebers B.;
RT "The first prokaryotic trehalose synthase complex identified in the
RT hyperthermophilic crenarchaeon Thermoproteus tenax.";
RL PLoS ONE 8:E61354-E61354(2013).
CC -!- FUNCTION: Bifunctional enzyme which catalyzes the transfer of glucose
CC from UDP-alpha-D-glucose to glucose-6-phosphate to form trehalose-6-
CC phosphate (Tre6P) and removes the phosphate from Tre6P to produce free
CC trehalose. {ECO:0000269|PubMed:23626675}.
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:23626675};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=alpha,alpha-trehalose 6-phosphate + H2O = alpha,alpha-
CC trehalose + phosphate; Xref=Rhea:RHEA:23420, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:16551, ChEBI:CHEBI:43474, ChEBI:CHEBI:58429; EC=3.1.3.12;
CC Evidence={ECO:0000269|PubMed:23626675};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:P31678, ECO:0000269|PubMed:23626675};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Temperature dependence:
CC Active at 80 degrees Celsius. {ECO:0000269|PubMed:23626675};
CC -!- PATHWAY: Glycan biosynthesis; trehalose biosynthesis.
CC {ECO:0000269|PubMed:23626675}.
CC -!- SUBUNIT: May interact with the putative glycosyltransferase (GT)
CC TTX_1305. TTX_1305 is required for the trehalose-6-phosphate synthase
CC activity of tpsp. {ECO:0000269|PubMed:23626675}.
CC -!- MISCELLANEOUS: Part of an operon with putative glycosyltransferase
CC TTX_1305 and putative membrane protein TTX_1304.1.
CC -!- SIMILARITY: In the N-terminal section; belongs to the
CC glycosyltransferase 20 family. {ECO:0000255}.
CC -!- SIMILARITY: In the C-terminal section; belongs to the trehalose
CC phosphatase family. {ECO:0000255}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAF18468.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AJ621287; CAF18468.1; ALT_INIT; Genomic_DNA.
DR EMBL; FN869859; CCC81939.1; -; Genomic_DNA.
DR RefSeq; WP_014127194.1; NC_016070.1.
DR AlphaFoldDB; G4RK44; -.
DR SMR; G4RK44; -.
DR STRING; 768679.TTX_1304; -.
DR CAZy; GT20; Glycosyltransferase Family 20.
DR EnsemblBacteria; CCC81939; CCC81939; TTX_1304.
DR GeneID; 11262184; -.
DR KEGG; ttn:TTX_1304; -.
DR PATRIC; fig|768679.9.peg.1319; -.
DR eggNOG; arCOG02831; Archaea.
DR HOGENOM; CLU_002351_3_3_2; -.
DR OMA; YYGFSNR; -.
DR OrthoDB; 5987at2157; -.
DR BRENDA; 2.4.1.15; 6329.
DR BRENDA; 3.1.3.12; 6329.
DR UniPathway; UPA00299; -.
DR Proteomes; UP000002654; Chromosome.
DR GO; GO:0003825; F:alpha,alpha-trehalose-phosphate synthase (UDP-forming) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004805; F:trehalose-phosphatase activity; IEA:UniProtKB-EC.
DR GO; GO:0005992; P:trehalose biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd03788; GT20_TPS; 1.
DR Gene3D; 3.40.50.1000; -; 1.
DR InterPro; IPR001830; Glyco_trans_20.
DR InterPro; IPR036412; HAD-like_sf.
DR InterPro; IPR006379; HAD-SF_hydro_IIB.
DR InterPro; IPR023214; HAD_sf.
DR InterPro; IPR012766; Trehalose_OtsA.
DR InterPro; IPR003337; Trehalose_PPase.
DR PANTHER; PTHR10788; PTHR10788; 1.
DR Pfam; PF00982; Glyco_transf_20; 1.
DR Pfam; PF02358; Trehalose_PPase; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01484; HAD-SF-IIB; 1.
DR TIGRFAMs; TIGR00685; T6PP; 1.
DR TIGRFAMs; TIGR02400; trehalose_OtsA; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Glycosyltransferase; Hydrolase; Magnesium;
KW Metal-binding; Multifunctional enzyme; Reference proteome; Transferase.
FT CHAIN 1..731
FT /note="Bifunctional trehalose-6-phosphate
FT synthase/phosphatase"
FT /id="PRO_0000424542"
FT REGION 1..464
FT /note="Alpha,alpha-trehalose-phosphate synthase"
FT /evidence="ECO:0000255"
FT REGION 465..731
FT /note="Trehalose-6-phosphate phosphatase"
FT /evidence="ECO:0000255"
FT ACT_SITE 503
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P31678"
FT BINDING 9
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT BINDING 25..26
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT BINDING 89
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT BINDING 143
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT BINDING 276
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT BINDING 281
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT BINDING 314
FT /ligand="D-glucose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:61548"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT BINDING 379..383
FT /ligand="UDP-alpha-D-glucose"
FT /ligand_id="ChEBI:CHEBI:58885"
FT /evidence="ECO:0000250|UniProtKB:P31677"
FT BINDING 503..505
FT /ligand="alpha,alpha-trehalose 6-phosphate"
FT /ligand_id="ChEBI:CHEBI:58429"
FT /evidence="ECO:0000250"
FT BINDING 503
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P31678"
FT BINDING 505
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 684
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250|UniProtKB:P31678"
SQ SEQUENCE 731 AA; 81699 MW; D51D6D0B97A49FE4 CRC64;
MRLIVVSNRL PVTISPSGEI RESVGGLATA MKSFLGAVNG GRELGLEEVV WVGWSGVPSE
RESNDLRERL RGMGLEPVPL SSEEVEGFYE GFSNSTLWPL FHGFSEYATY EEKHWRAYRG
VNEKYAKAVV ALARPGDLVW IHDYHLMLAP AIVREAAEVG VGFFLHIPFP PAELLQLLPS
EWRREILEGL LGSDLVGFHT YEYSANFSRS VVRFLGYKVE MGAIAVGHRR VRVGVFPIGI
DFDRFYNSSQ DPSVVEEMAK LREMLGRAKV VFSIDRLDYT KGVLRRVAAW ERFLREHPEW
RGRAVFVLVV VPSRTGVPMY EEMKRQIDRE VGRINGELGE LNWVPIVYLY RFIPSPTLMA
LYNIADVALI TPLRDGMNLV AKEFVASKRD CRGVLILSEL AGASKELAEA LVINPNDVGG
TAEAIAEALS MSEDEQCRRI RAMQERLRMR DVVRWGTDFI YSLISAKSAR EEVEKALRYM
EELSVDKLKS DFAKAKRRLL LLDYDGTLVP HYPYPHMAVP DGDLLELLSR LAALPETAVY
VVSGRGRDFL DGWLGRLPVG LVAEHGFFLK HPGGEWKSLG KVDPSWRQYA KGIMEDFASN
VPGSFVEVKE AGIAWHYRNA DETIAEKAVV ELIDALSNAL AGSGLSILRG KKVVEVRPAG
YTKGTAAKML LDELSPDFVF VAGDDETDEG MFEVAPQSAY TVKVGPGPTL AKFRVGDYRG
LRSLLEQLRP P
