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TREZ_DEIRA
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   03-AUG-2022, entry version 133.
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 / LMG
OS   4051 / NBRC 15346 / NCIMB 9279 / R1 / VKM B-1422).
OC   Bacteria; Deinococcus-Thermus; 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 / LMG 4051 / NBRC 15346 / NCIMB
RC   9279 / R1 / VKM B-1422;
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   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   OMA; FTPMLFM; -.
DR   OrthoDB; 148706at2; -.
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   Gene3D; 1.10.10.760; -; 1.
DR   Gene3D; 2.60.40.10; -; 1.
DR   Gene3D; 2.60.40.1180; -; 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   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; SSF51445; 1.
DR   SUPFAM; SSF81296; SSF81296; 1.
DR   TIGRFAMs; TIGR02402; trehalose_TreZ; 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
 
 
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