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Database: UniProt/TrEMBL
Entry: D6EX50_STRLI
LinkDB: D6EX50_STRLI
Original site: D6EX50_STRLI 
ID   D6EX50_STRLI            Unreviewed;       572 AA.
AC   D6EX50;
DT   13-JUL-2010, integrated into UniProtKB/TrEMBL.
DT   13-JUL-2010, sequence version 1.
DT   24-JAN-2024, entry version 58.
DE   RecName: Full=maltose alpha-D-glucosyltransferase {ECO:0000256|ARBA:ARBA00012619};
DE            EC=5.4.99.16 {ECO:0000256|ARBA:ARBA00012619};
DE   AltName: Full=Maltose alpha-D-glucosyltransferase {ECO:0000256|ARBA:ARBA00031378};
GN   ORFNames=SSPG_00511 {ECO:0000313|EMBL:EFD64871.2};
OS   Streptomyces lividans TK24.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=457428 {ECO:0000313|EMBL:EFD64871.2};
RN   [1] {ECO:0000313|EMBL:EFD64871.2}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TK24 {ECO:0000313|EMBL:EFD64871.2};
RG   The Broad Institute Genome Sequencing Platform;
RG   Broad Institute Microbial Sequencing Center;
RA   Fischbach M., Godfrey P., Ward D., Young S., Kodira C.D., Zeng Q.,
RA   Koehrsen M., Alvarado L., Berlin A.M., Borenstein D., Chen Z., Engels R.,
RA   Freedman E., Gellesch M., Goldberg J., Griggs A., Gujja S., Heiman D.I.,
RA   Hepburn T.A., Howarth C., Jen D., Larson L., Lewis B., Mehta T., Park D.,
RA   Pearson M., Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C.,
RA   Sykes S.N., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA   Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA   Galagan J., Nusbaum C., Birren B.;
RT   "The genome sequence of Streptomyces lividans strain TK24.";
RL   Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=D-maltose = alpha,alpha-trehalose; Xref=Rhea:RHEA:15145,
CC         ChEBI:CHEBI:16551, ChEBI:CHEBI:17306; EC=5.4.99.16;
CC         Evidence={ECO:0000256|ARBA:ARBA00001595};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. TreS
CC       subfamily. {ECO:0000256|ARBA:ARBA00005496}.
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DR   EMBL; GG657756; EFD64871.2; -; Genomic_DNA.
DR   RefSeq; WP_003971807.1; NZ_GG657756.1.
DR   AlphaFoldDB; D6EX50; -.
DR   HOGENOM; CLU_006462_2_1_11; -.
DR   Proteomes; UP000002769; Unassembled WGS sequence.
DR   GO; GO:0047471; F:maltose alpha-D-glucosyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd11334; AmyAc_TreS; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR032091; Malt_amylase_C.
DR   InterPro; IPR045857; O16G_dom_2.
DR   InterPro; IPR012810; TreS/a-amylase_N.
DR   NCBIfam; TIGR02456; treS_nterm; 1.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   PANTHER; PTHR10357:SF219; MALTOSE ALPHA-D-GLUCOSYLTRANSFERASE; 1.
DR   Pfam; PF00128; Alpha-amylase; 2.
DR   Pfam; PF16657; Malt_amylase_C; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT   DOMAIN          31..433
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   572 AA;  65708 MW;  45CFBE9FF337A36F CRC64;
     MTVNEPVPDT FEDTPAGDRH PDWFKRAVFY EVLVRSFQDS NGDGVGDLKG LTAKLDYLQW
     LGVDCLWLPP FFKSPLRDGG YDVSDYTAVL PEFGDLADFV EFVDAAHQRG MRVIIDFVMN
     HTSDQHPWFQ ESRKNPDGPY GDYYVWADDD TRYADARIIF VDTEASNWTY DPVRGQYYWH
     RFFSHQPDLN YENPAVQEEM LAALKFWLDL GVDGYRLDAV PYLYAEEGTN CENLPASHAF
     LKRVRREIDA QYPDTVLLAE ANQWPEDVVD YFGDYSTGGD ECHMAFHFPV MPRIFMAVRR
     ESRYPVSEIL AKTPAIPSGC QWGIFLRNHD ELTLEMVTDE ERDYMYAEYA KDPRMRANIG
     IRRRLATLLD NDRDQIELFT ALLLALPGSP ILYYGDEIGM GDNIWLGDRD AVRTPMQWTP
     DRNAGFSTCD PGRLYLPAIM DPVYGYQVTN VEASMASPSS LLHWTRRMIE IRKQNPAFGL
     GTYTELPSSN PAVLAFLREY EDDLVLCVNN FARFAQPTEL DLREFAGRHP VELFGGVRFP
     AIGELPYLLT LGGHGFYWFR LTRVASRIGR RA
//
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