ID   G2NQS0_STREK            Unreviewed;       575 AA.
AC   G2NQS0;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 59.
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=SACTE_4634 {ECO:0000313|EMBL:AEN12461.1};
OS   Streptomyces sp. (strain SirexAA-E / ActE).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=862751 {ECO:0000313|EMBL:AEN12461.1, ECO:0000313|Proteomes:UP000001397};
RN   [1] {ECO:0000313|EMBL:AEN12461.1, ECO:0000313|Proteomes:UP000001397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Ovchinnikova G., Davenport K., Detter J.C., Han C., Tapia R.,
RA   Land M., Hauser L., Kyrpides N., Ivanova N., Pagani I., Adams A., Raffa K.,
RA   Adams S., Book A., Currie C., Woyke T.;
RT   "Complete sequence of Streptomyces sp. SirexAA-E.";
RL   Submitted (AUG-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AEN12461.1, ECO:0000313|Proteomes:UP000001397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SirexAA-E / ActE {ECO:0000313|Proteomes:UP000001397};
RX   PubMed=24710170; DOI=10.1371/journal.pone.0094166;
RA   Takasuka T.E., Acheson J.F., Bianchetti C.M., Prom B.M., Bergeman L.F.,
RA   Book A.J., Currie C.R., Fox B.G.;
RT   "Biochemical properties and atomic resolution structure of a
RT   proteolytically processed beta-mannanase from cellulolytic Streptomyces sp.
RT   SirexAA-E.";
RL   PLoS ONE 9:e94166-E94166(2014).
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; CP002993; AEN12461.1; -; Genomic_DNA.
DR   RefSeq; WP_014048418.1; NC_015953.1.
DR   AlphaFoldDB; G2NQS0; -.
DR   STRING; 862751.SACTE_4634; -.
DR   KEGG; ssx:SACTE_4634; -.
DR   PATRIC; fig|862751.12.peg.4807; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_006462_2_3_11; -.
DR   OrthoDB; 9043248at2; -.
DR   Proteomes; UP000001397; Chromosome.
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; 1.
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   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001397}.
FT   DOMAIN          31..433
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   575 AA;  66463 MW;  B2D6E2B8AAD9A551 CRC64;
     MIVNEPVHDL FEDTPAKDRD PDWFKRAVFY EVLVRSFQDS NGDGVGDLKG LTAKLDYLQW
     LGVDCLWLPP FFKSPLRDGG YDVSDYTAVL PEFGDLADFV EFVDAAHQRG MRVIIDFVMN
     HTSDQHDWFQ QSRTDPDGPY GDYYVWADDD KQFPDARIIF VDTETSNWTF DPVRKQYYWH
     RFFSHQPDLN YENPAVQEEI ISALRFWLDL GIDGFRVDAV PYLYQREGTN CENLPETHNF
     LKRVRKEIDA NYPDTVLLAE ANQWPEDVVD YFGDYTAGGD ECHMAFHFPV MPRIFMAVRR
     ESRYPVSEIL AKTPQIPSGC QWGIFLRNHD ELTLEMVTDE ERDYMYAEYA KDPRMRANIG
     IRRRLAPLLD NDRNQIELFT ALLLSLPGSP ILYYGDEIGM GDNIWLGDRD AVRTPMQWTP
     DRNAGFSSSD PGRLYLPTIM DPVYGYQVTN VEASMASPSS LLHWTRRMIE IRKQNPAFGL
     GSYTELPSSN PAVIAFTREY KDDLVLCVHN FSRFAQPTEL DLRDFDGRHP VELIGGVRFP
     AVGQWPYLLT LAGHGFYWFR MRKDTAAALP PRAKS
//