ID TREZ_DEIRA Reviewed; 600 AA.
AC Q9RX51;
DT 20-APR-2010, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 27-MAR-2024, entry version 139.
DE RecName: Full=Malto-oligosyltrehalose trehalohydrolase;
DE Short=MTHase;
DE EC=3.2.1.141;
DE AltName: Full=4-alpha-D-((1->4)-alpha-D-glucano)trehalose trehalohydrolase;
DE AltName: Full=Maltooligosyl trehalose trehalohydrolase;
GN Name=treZ; OrderedLocusNames=DR_0464;
OS Deinococcus radiodurans (strain ATCC 13939 / DSM 20539 / JCM 16871 / CCUG
OS 27074 / LMG 4051 / NBRC 15346 / NCIMB 9279 / VKM B-1422 / R1).
OC Bacteria; Deinococcota; Deinococci; Deinococcales; Deinococcaceae;
OC Deinococcus.
OX NCBI_TaxID=243230;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 13939 / DSM 20539 / JCM 16871 / CCUG 27074 / LMG 4051 / NBRC
RC 15346 / NCIMB 9279 / VKM B-1422 / R1;
RX PubMed=10567266; DOI=10.1126/science.286.5444.1571;
RA White O., Eisen J.A., Heidelberg J.F., Hickey E.K., Peterson J.D.,
RA Dodson R.J., Haft D.H., Gwinn M.L., Nelson W.C., Richardson D.L.,
RA Moffat K.S., Qin H., Jiang L., Pamphile W., Crosby M., Shen M.,
RA Vamathevan J.J., Lam P., McDonald L.A., Utterback T.R., Zalewski C.,
RA Makarova K.S., Aravind L., Daly M.J., Minton K.W., Fleischmann R.D.,
RA Ketchum K.A., Nelson K.E., Salzberg S.L., Smith H.O., Venter J.C.,
RA Fraser C.M.;
RT "Genome sequence of the radioresistant bacterium Deinococcus radiodurans
RT R1.";
RL Science 286:1571-1577(1999).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.1 ANGSTROMS) OF 14-600 IN COMPLEX WITH MALTOSE AND
RP TREHALOSE, AND SUBUNIT.
RX PubMed=15784255; DOI=10.1016/j.jmb.2005.02.011;
RA Timmins J., Leiros H.K., Leonard G., Leiros I., McSweeney S.;
RT "Crystal structure of maltooligosyltrehalose trehalohydrolase from
RT Deinococcus radiodurans in complex with disaccharides.";
RL J. Mol. Biol. 347:949-963(2005).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=hydrolysis of (1->4)-alpha-D-glucosidic linkage in 4-alpha-D-
CC [(1->4)-alpha-D-glucanosyl]n trehalose to yield trehalose and (1->4)-
CC alpha-D-glucan.; EC=3.2.1.141;
CC -!- PATHWAY: Glycan biosynthesis; trehalose biosynthesis.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:15784255}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; AE000513; AAF10042.1; -; Genomic_DNA.
DR PIR; H75516; H75516.
DR RefSeq; NP_294187.1; NC_001263.1.
DR RefSeq; WP_010887109.1; NC_001263.1.
DR PDB; 2BHU; X-ray; 1.10 A; A=1-600.
DR PDB; 2BHY; X-ray; 1.50 A; A=1-600.
DR PDB; 2BHZ; X-ray; 1.20 A; A=1-600.
DR PDB; 2BXY; X-ray; 1.75 A; A=1-600.
DR PDB; 2BXZ; X-ray; 1.75 A; A=1-600.
DR PDB; 2BY0; X-ray; 1.55 A; A=1-600.
DR PDB; 2BY1; X-ray; 1.55 A; A=1-600.
DR PDB; 2BY2; X-ray; 1.50 A; A=1-600.
DR PDB; 2BY3; X-ray; 1.50 A; A=1-600.
DR PDBsum; 2BHU; -.
DR PDBsum; 2BHY; -.
DR PDBsum; 2BHZ; -.
DR PDBsum; 2BXY; -.
DR PDBsum; 2BXZ; -.
DR PDBsum; 2BY0; -.
DR PDBsum; 2BY1; -.
DR PDBsum; 2BY2; -.
DR PDBsum; 2BY3; -.
DR AlphaFoldDB; Q9RX51; -.
DR SMR; Q9RX51; -.
DR STRING; 243230.DR_0464; -.
DR DrugBank; DB02379; Beta-D-Glucose.
DR DrugBank; DB03323; Maltose.
DR CAZy; CBM48; Carbohydrate-Binding Module Family 48.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PaxDb; 243230-DR_0464; -.
DR EnsemblBacteria; AAF10042; AAF10042; DR_0464.
DR KEGG; dra:DR_0464; -.
DR PATRIC; fig|243230.17.peg.641; -.
DR eggNOG; COG0296; Bacteria.
DR HOGENOM; CLU_020726_0_0_0; -.
DR InParanoid; Q9RX51; -.
DR OrthoDB; 9800174at2; -.
DR BRENDA; 3.2.1.141; 1856.
DR UniPathway; UPA00299; -.
DR EvolutionaryTrace; Q9RX51; -.
DR Proteomes; UP000002524; Chromosome I.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0033942; F:4-alpha-D-(1->4)-alpha-D-glucanotrehalose trehalohydrolase activity; IEA:UniProtKB-EC.
DR GO; GO:0005992; P:trehalose biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd11325; AmyAc_GTHase; 1.
DR CDD; cd02853; E_set_MTHase_like_N; 1.
DR Gene3D; 1.10.10.760; E-set domains of sugar-utilizing enzymes; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR Gene3D; 2.60.40.10; Immunoglobulins; 1.
DR InterPro; IPR022567; DUF3459.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR004193; Glyco_hydro_13_N.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR014756; Ig_E-set.
DR InterPro; IPR012768; Trehalose_TreZ.
DR InterPro; IPR044901; Trehalose_TreZ_E-set_sf.
DR NCBIfam; TIGR02402; trehalose_TreZ; 1.
DR PANTHER; PTHR43651; 1,4-ALPHA-GLUCAN-BRANCHING ENZYME; 1.
DR PANTHER; PTHR43651:SF11; MALTO-OLIGOSYLTREHALOSE TREHALOHYDROLASE; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF02922; CBM_48; 1.
DR Pfam; PF11941; DUF3459; 1.
DR PIRSF; PIRSF006337; Trehalose_TreZ; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF81296; E set domains; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Carbohydrate metabolism; Cytoplasm; Glycosidase; Hydrolase;
KW Reference proteome.
FT CHAIN 1..600
FT /note="Malto-oligosyltrehalose trehalohydrolase"
FT /id="PRO_0000393750"
FT REGION 1..34
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..23
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 275
FT /note="Nucleophile"
FT /evidence="ECO:0000305"
FT ACT_SITE 308
FT /note="Proton donor"
FT /evidence="ECO:0000305"
FT BINDING 273..278
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q55088"
FT BINDING 328..332
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:15784255"
FT BINDING 376
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:15784255"
FT BINDING 399..404
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:Q55088"
FT SITE 400
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000305"
FT HELIX 21..23
FT /evidence="ECO:0007829|PDB:2BHU"
FT STRAND 25..29
FT /evidence="ECO:0007829|PDB:2BHU"
FT HELIX 31..33
FT /evidence="ECO:0007829|PDB:2BHU"
FT STRAND 36..41
FT /evidence="ECO:0007829|PDB:2BHU"
FT STRAND 46..52
FT /evidence="ECO:0007829|PDB:2BHU"
FT STRAND 55..58
FT /evidence="ECO:0007829|PDB:2BHU"
FT STRAND 60..63
FT /evidence="ECO:0007829|PDB:2BHU"
FT STRAND 66..72
FT /evidence="ECO:0007829|PDB:2BHU"
FT STRAND 78..83
FT /evidence="ECO:0007829|PDB:2BHU"
FT STRAND 86..88
FT /evidence="ECO:0007829|PDB:2BHU"
FT HELIX 109..111
FT /evidence="ECO:0007829|PDB:2BXZ"
FT HELIX 124..126
FT /evidence="ECO:0007829|PDB:2BHU"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:2BHU"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:2BHU"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:2BHU"
FT HELIX 143..148
FT /evidence="ECO:0007829|PDB:2BHU"
FT HELIX 150..156
FT /evidence="ECO:0007829|PDB:2BHU"
FT STRAND 160..163
FT /evidence="ECO:0007829|PDB:2BHU"
FT STRAND 170..172
FT /evidence="ECO:0007829|PDB:2BHU"
FT STRAND 181..185
FT /evidence="ECO:0007829|PDB:2BHU"
FT HELIX 187..189
FT /evidence="ECO:0007829|PDB:2BHU"
FT HELIX 192..204
FT /evidence="ECO:0007829|PDB:2BHU"
FT STRAND 208..213
FT /evidence="ECO:0007829|PDB:2BHU"
FT STRAND 220..222
FT /evidence="ECO:0007829|PDB:2BHU"
FT HELIX 225..228
FT /evidence="ECO:0007829|PDB:2BHU"
FT HELIX 230..232
FT /evidence="ECO:0007829|PDB:2BHU"
FT STRAND 233..238
FT /evidence="ECO:0007829|PDB:2BHU"
FT STRAND 240..245
FT /evidence="ECO:0007829|PDB:2BHU"
FT HELIX 250..267
FT /evidence="ECO:0007829|PDB:2BHU"
FT STRAND 270..274
FT /evidence="ECO:0007829|PDB:2BHU"
FT HELIX 277..279
FT /evidence="ECO:0007829|PDB:2BHU"
FT STRAND 284..286
FT /evidence="ECO:0007829|PDB:2BHU"
FT HELIX 288..297
FT /evidence="ECO:0007829|PDB:2BHU"
FT STRAND 304..308
FT /evidence="ECO:0007829|PDB:2BHU"
FT HELIX 315..318
FT /evidence="ECO:0007829|PDB:2BHU"
FT STRAND 323..326
FT /evidence="ECO:0007829|PDB:2BHU"
FT HELIX 329..339
FT /evidence="ECO:0007829|PDB:2BHU"
FT HELIX 344..348
FT /evidence="ECO:0007829|PDB:2BHU"
FT HELIX 353..362
FT /evidence="ECO:0007829|PDB:2BHU"
FT STRAND 363..365
FT /evidence="ECO:0007829|PDB:2BHU"
FT STRAND 367..371
FT /evidence="ECO:0007829|PDB:2BHU"
FT STRAND 378..381
FT /evidence="ECO:0007829|PDB:2BHU"
FT HELIX 389..391
FT /evidence="ECO:0007829|PDB:2BHU"
FT STRAND 392..396
FT /evidence="ECO:0007829|PDB:2BHU"
FT HELIX 399..403
FT /evidence="ECO:0007829|PDB:2BHU"
FT HELIX 411..413
FT /evidence="ECO:0007829|PDB:2BHU"
FT HELIX 419..430
FT /evidence="ECO:0007829|PDB:2BHU"
FT STRAND 431..437
FT /evidence="ECO:0007829|PDB:2BHU"
FT HELIX 440..442
FT /evidence="ECO:0007829|PDB:2BHU"
FT HELIX 456..469
FT /evidence="ECO:0007829|PDB:2BHU"
FT TURN 470..472
FT /evidence="ECO:0007829|PDB:2BHZ"
FT HELIX 474..477
FT /evidence="ECO:0007829|PDB:2BHZ"
FT HELIX 487..491
FT /evidence="ECO:0007829|PDB:2BHU"
FT HELIX 498..501
FT /evidence="ECO:0007829|PDB:2BHU"
FT HELIX 503..521
FT /evidence="ECO:0007829|PDB:2BHU"
FT TURN 523..526
FT /evidence="ECO:0007829|PDB:2BHU"
FT HELIX 530..532
FT /evidence="ECO:0007829|PDB:2BHU"
FT STRAND 533..538
FT /evidence="ECO:0007829|PDB:2BHU"
FT STRAND 541..548
FT /evidence="ECO:0007829|PDB:2BHU"
FT STRAND 551..558
FT /evidence="ECO:0007829|PDB:2BHU"
FT STRAND 560..562
FT /evidence="ECO:0007829|PDB:2BHU"
FT HELIX 566..568
FT /evidence="ECO:0007829|PDB:2BHU"
FT STRAND 578..582
FT /evidence="ECO:0007829|PDB:2BHU"
FT STRAND 587..591
FT /evidence="ECO:0007829|PDB:2BHU"
FT STRAND 596..600
FT /evidence="ECO:0007829|PDB:2BHU"
SQ SEQUENCE 600 AA; 66910 MW; 594091EC093F8A44 CRC64;
MTQTQPVTPT PPASFQTQHD PRTRLGATPL PGGAGTRFRL WTSTARTVAV RVNGTEHVMT
SLGGGIYELE LPVGPGARYL FVLDGVPTPD PYARFLPDGV HGEAEVVDFG TFDWTDADWH
GIKLADCVFY EVHVGTFTPE GTYRAAAEKL PYLKELGVTA IQVMPLAAFD GQRGWGYDGA
AFYAPYAPYG RPEDLMALVD AAHRLGLGVF LDVVYNHFGP SGNYLSSYAP SYFTDRFSSA
WGMGLDYAEP HMRRYVTGNA RMWLRDYHFD GLRLDATPYM TDDSETHILT ELAQEIHELG
GTHLLLAEDH RNLPDLVTVN HLDGIWTDDF HHETRVTLTG EQEGYYAGYR GGAEALAYTI
RRGWRYEGQF WAVKGEEHER GHPSDALEAP NFVYCIQNHD QIGNRPLGER LHQSDGVTLH
EYRGAAALLL PMTPLLFQGQ EWAASTPFQF FSDHAGELGQ AVSEGRKKEF GGFSGFSGED
VPDPQAEQTF LNSKLNWAER EGGEHARTLR LYRDLLRLRR EDPVLHNRQR ENLTTGHDGD
VLWVRTVTGA GERVLLWNLG QDTRAVAEVK LPFTVPRRLL LHTEGREDLT LGAGEAVLVG
//
