TRET_PYRHO
ID TRET_PYRHO Reviewed; 415 AA.
AC O58762;
DT 08-MAR-2011, integrated into UniProtKB/Swiss-Prot.
DT 08-MAR-2011, sequence version 2.
DT 25-MAY-2022, entry version 99.
DE RecName: Full=Trehalose synthase {ECO:0000250|UniProtKB:Q7LYW5};
DE EC=2.4.1.245;
DE AltName: Full=Trehalose-synthesizing glycosyltransferase {ECO:0000303|PubMed:15737605};
GN Name=treT {ECO:0000250|UniProtKB:Q7LYW5}; OrderedLocusNames=PH1035;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1] {ECO:0000312|EMBL:BAA30133.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3
RC {ECO:0000269|PubMed:15737605};
RX PubMed=15737605; DOI=10.1016/j.bbrc.2005.01.149;
RA Ryu S.I., Park C.S., Cha J., Woo E.J., Lee S.B.;
RT "A novel trehalose-synthesizing glycosyltransferase from Pyrococcus
RT horikoshii: molecular cloning and characterization.";
RL Biochem. Biophys. Res. Commun. 329:429-436(2005).
CC -!- FUNCTION: Synthesizes trehalose from ADP-, UDP- or GDP-glucose and
CC glucose. {ECO:0000269|PubMed:15737605}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=an NDP-alpha-D-glucose + D-glucose = a ribonucleoside 5'-
CC diphosphate + alpha,alpha-trehalose + H(+); Xref=Rhea:RHEA:47416,
CC ChEBI:CHEBI:4167, ChEBI:CHEBI:15378, ChEBI:CHEBI:16551,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:76533; EC=2.4.1.245;
CC Evidence={ECO:0000269|PubMed:15737605};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000250|UniProtKB:Q7LYW5};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 5.5. Stable from pH 5 to pH 8.
CC {ECO:0000269|PubMed:15737605};
CC Temperature dependence:
CC Not thermostable. Approximately 25% of maximum activity remains after
CC 1 hour incubation at 55 degrees Celsius.
CC {ECO:0000269|PubMed:15737605};
CC -!- SUBUNIT: Homodimer. {ECO:0000250|UniProtKB:Q7LYW5}.
CC -!- SIMILARITY: Belongs to the glycosyltransferase group 1 family.
CC Glycosyltransferase 4 subfamily. {ECO:0000305}.
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DR EMBL; BA000001; BAA30133.1; -; Genomic_DNA.
DR PIR; G71096; G71096.
DR PDB; 2X6Q; X-ray; 2.20 A; A/B=2-415.
DR PDB; 2X6R; X-ray; 2.20 A; A/B=2-415.
DR PDB; 2XA1; X-ray; 2.47 A; A/B=2-415.
DR PDB; 2XA2; X-ray; 2.50 A; A/B=2-415.
DR PDB; 2XA9; X-ray; 2.50 A; A/B=2-415.
DR PDB; 2XMP; X-ray; 2.50 A; A/B=2-415.
DR PDBsum; 2X6Q; -.
DR PDBsum; 2X6R; -.
DR PDBsum; 2XA1; -.
DR PDBsum; 2XA2; -.
DR PDBsum; 2XA9; -.
DR PDBsum; 2XMP; -.
DR AlphaFoldDB; O58762; -.
DR SMR; O58762; -.
DR STRING; 70601.3257450; -.
DR CAZy; GT4; Glycosyltransferase Family 4.
DR DNASU; 1443358; -.
DR EnsemblBacteria; BAA30133; BAA30133; BAA30133.
DR KEGG; pho:PH1035; -.
DR eggNOG; arCOG01407; Archaea.
DR BRENDA; 2.4.1.245; 5244.
DR EvolutionaryTrace; O58762; -.
DR Proteomes; UP000000752; Chromosome.
DR GO; GO:0102986; F:trehalose synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0006006; P:glucose metabolic process; IEA:UniProtKB-KW.
DR InterPro; IPR001296; Glyco_trans_1.
DR Pfam; PF00534; Glycos_transf_1; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Glucose metabolism;
KW Glycosyltransferase; Magnesium; Transferase.
FT CHAIN 1..415
FT /note="Trehalose synthase"
FT /id="PRO_0000405300"
FT STRAND 3..5
FT /evidence="ECO:0007829|PDB:2X6R"
FT HELIX 15..18
FT /evidence="ECO:0007829|PDB:2X6Q"
FT HELIX 19..35
FT /evidence="ECO:0007829|PDB:2X6Q"
FT TURN 36..39
FT /evidence="ECO:0007829|PDB:2X6Q"
FT STRAND 41..47
FT /evidence="ECO:0007829|PDB:2X6Q"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:2X6Q"
FT HELIX 54..67
FT /evidence="ECO:0007829|PDB:2X6Q"
FT STRAND 71..76
FT /evidence="ECO:0007829|PDB:2X6Q"
FT HELIX 81..94
FT /evidence="ECO:0007829|PDB:2X6Q"
FT HELIX 104..119
FT /evidence="ECO:0007829|PDB:2X6Q"
FT HELIX 123..125
FT /evidence="ECO:0007829|PDB:2X6Q"
FT STRAND 126..134
FT /evidence="ECO:0007829|PDB:2X6Q"
FT HELIX 137..142
FT /evidence="ECO:0007829|PDB:2X6Q"
FT STRAND 149..152
FT /evidence="ECO:0007829|PDB:2X6Q"
FT HELIX 162..172
FT /evidence="ECO:0007829|PDB:2X6Q"
FT STRAND 175..182
FT /evidence="ECO:0007829|PDB:2X6Q"
FT HELIX 183..185
FT /evidence="ECO:0007829|PDB:2X6Q"
FT TURN 192..194
FT /evidence="ECO:0007829|PDB:2X6Q"
FT STRAND 195..197
FT /evidence="ECO:0007829|PDB:2X6Q"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:2X6Q"
FT HELIX 214..223
FT /evidence="ECO:0007829|PDB:2X6Q"
FT STRAND 232..236
FT /evidence="ECO:0007829|PDB:2X6Q"
FT HELIX 245..258
FT /evidence="ECO:0007829|PDB:2X6Q"
FT STRAND 263..268
FT /evidence="ECO:0007829|PDB:2X6Q"
FT HELIX 275..288
FT /evidence="ECO:0007829|PDB:2X6Q"
FT STRAND 294..298
FT /evidence="ECO:0007829|PDB:2X6Q"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:2X6Q"
FT HELIX 305..314
FT /evidence="ECO:0007829|PDB:2X6Q"
FT STRAND 316..320
FT /evidence="ECO:0007829|PDB:2X6Q"
FT HELIX 329..336
FT /evidence="ECO:0007829|PDB:2X6Q"
FT STRAND 341..345
FT /evidence="ECO:0007829|PDB:2X6Q"
FT HELIX 347..352
FT /evidence="ECO:0007829|PDB:2X6Q"
FT TURN 355..357
FT /evidence="ECO:0007829|PDB:2X6Q"
FT STRAND 358..364
FT /evidence="ECO:0007829|PDB:2X6Q"
FT HELIX 365..377
FT /evidence="ECO:0007829|PDB:2X6Q"
FT HELIX 379..396
FT /evidence="ECO:0007829|PDB:2X6Q"
FT HELIX 399..411
FT /evidence="ECO:0007829|PDB:2X6Q"
SQ SEQUENCE 415 AA; 48069 MW; 5ED5B806043842FC CRC64;
MMYEVKEFSS GKRKLEDYKS IIGEEEVSKI QEKAEKLKGR SFVHVNSTSF GGGVAEILHS
LVPLLRSIGI EARWFVIEGP TEFFNVTKTF HNALQGNESL KLTEEMKELY LNVNRENSKF
IDLSSFDYVL VHDPQPAALI EFYEKKSPWL WRCHIDLSSP NREFWEFLRR FVEKYDRYIF
HLPEYVQPEL DRNKAVIMPP SIDPLSEKNV ELKQTEILRI LERFDVDPEK PIITQVSRFD
PWKGIFDVIE IYRKVKEKIP GVQLLLVGVM AHDDPEGWIY FEKTLRKIGE DYDVKVLTNL
IGVHAREVNA FQRASDVILQ MSIREGFGLT VTEAMWKGKP VIGRAVGGIK FQIVDGETGF
LVRDANEAVE KVLYLLKHPE VSKEMGAKAK ERVRKNFIIT KHMERYLDIL NSLGG
