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Database: UniProt
Entry: A0A0D4DI93_9ACTN
LinkDB: A0A0D4DI93_9ACTN
Original site: A0A0D4DI93_9ACTN 
ID   A0A0D4DI93_9ACTN        Unreviewed;       595 AA.
AC   A0A0D4DI93;
DT   27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT   27-MAY-2015, sequence version 1.
DT   10-OCT-2018, entry version 20.
DE   RecName: Full=Malto-oligosyltrehalose trehalohydrolase {ECO:0000256|PIRNR:PIRNR006337};
DE            Short=MTHase {ECO:0000256|PIRNR:PIRNR006337};
DE            EC=3.2.1.141 {ECO:0000256|PIRNR:PIRNR006337};
DE   AltName: Full=4-alpha-D-((1->4)-alpha-D-glucano)trehalose trehalohydrolase {ECO:0000256|PIRNR:PIRNR006337};
DE   AltName: Full=Maltooligosyl trehalose trehalohydrolase {ECO:0000256|PIRNR:PIRNR006337};
GN   ORFNames=T261_1994 {ECO:0000313|EMBL:AJT63679.1};
OS   Streptomyces lydicus.
OC   Bacteria; Actinobacteria; Streptomycetales; Streptomycetaceae;
OC   Streptomyces.
OX   NCBI_TaxID=47763 {ECO:0000313|EMBL:AJT63679.1, ECO:0000313|Proteomes:UP000032413};
RN   [1] {ECO:0000313|Proteomes:UP000032413}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A02 {ECO:0000313|Proteomes:UP000032413};
RA   Wu H., Yan J., Liu W., Liu T., Dong D., Li J., Liu H., Lu C.,
RA   Zhang D., Zhang T., Tian Z.;
RT   "Complete genome sequence of the natamycin-producing actinomycete
RT   Streptomyces lydicus A02.";
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY: Hydrolysis of (1->4)-alpha-D-glucosidic
CC       linkage in 4-alpha-D-((1->4)-alpha-D-glucanosyl)(n) trehalose to
CC       yield trehalose and (1->4)-alpha-D-glucan.
CC       {ECO:0000256|PIRNR:PIRNR006337}.
CC   -!- PATHWAY: Glycan biosynthesis; trehalose biosynthesis.
CC       {ECO:0000256|PIRNR:PIRNR006337}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|PIRSR:PIRSR006337-1}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|PIRNR:PIRNR006337, ECO:0000256|SAAS:SAAS00964676}.
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DR   EMBL; CP007699; AJT63679.1; -; Genomic_DNA.
DR   RefSeq; WP_046925441.1; NZ_CP007699.2.
DR   EnsemblBacteria; AJT63679; AJT63679; T261_1994.
DR   KEGG; sld:T261_1994; -.
DR   PATRIC; fig|1403539.3.peg.2101; -.
DR   KO; K01236; -.
DR   UniPathway; UPA00299; -.
DR   Proteomes; UP000032413; Chromosome.
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; 2.60.40.10; -; 1.
DR   InterPro; IPR022567; DUF3459.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR014756; Ig_E-set.
DR   InterPro; IPR012768; Trehalose_TreZ.
DR   Pfam; PF00128; Alpha-amylase; 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   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000032413};
KW   Glycosidase {ECO:0000256|PIRNR:PIRNR006337};
KW   Hydrolase {ECO:0000256|PIRNR:PIRNR006337,
KW   ECO:0000313|EMBL:AJT63679.1}.
FT   DOMAIN      107    451       Aamy. {ECO:0000259|SMART:SM00642}.
FT   ACT_SITE    249    249       Nucleophile. {ECO:0000256|PIRSR:
FT                                PIRSR006337-1}.
FT   ACT_SITE    286    286       Proton donor. {ECO:0000256|PIRSR:
FT                                PIRSR006337-1}.
FT   SITE        384    384       Transition state stabilizer.
FT                                {ECO:0000256|PIRSR:PIRSR006337-3}.
SQ   SEQUENCE   595 AA;  64415 MW;  1D3E6C2C6ED05F23 CRC64;
     MLFELWAPGA GRVVLQWAGG RAGEPPLPLE RDGERDGWWR AEAPAHDGDR YAYRIDGGPP
     LPDPRAARLP EGPGGPGAVV DHGRFAWRHS WPGRPLPGAV LYELHIGTYT AEGTFDAAAE
     RLHHLAHLGI THVSLMPVCP FPGTHGWGYD GIAPWAVHEP YGGPDGLKRF VDAAHGHGLG
     VVLDVVHNHL GPSGNHLPSF GPYFTDTHHT PWGAAVNLDA PGSDEVRRYF IGSALAWLRD
     YRIDGLRLDA VHALHDSRAR HFLAELSAAV DALAGRLRRP LFLIAESDRN DPATTAPHAS
     GGHGLHAQWN DDFHHALHTA LTGESHGYYA DFARAPVAAL AKTLTGGFFH DGTYSSFRGR
     THGAPLDPRR TPPYRLLAYA QTHDQIGNRA LGDRLTAALS PGLLACAAAL VLCSPFTPML
     FMGEEWGART PWQYFTDHPD PELAEAVRAG RRREFAAHDW SGTDADWPDP QDPATRDRCV
     LNWSEPDRAP HAALLAWYRT VLGLRRELPA PAGPDPAATH VTYDEDARWL LLRNGSVRVA
     VNLARDTVAD IPVGTEGEPA PELRVLAAWG EADGAGGAGM VRVGAESVVI LGEIP
//
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