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Database: UniProt
Entry: A0A2M8LVL7_9ACTN
LinkDB: A0A2M8LVL7_9ACTN
Original site: A0A2M8LVL7_9ACTN 
ID   A0A2M8LVL7_9ACTN        Unreviewed;       565 AA.
AC   A0A2M8LVL7;
DT   25-APR-2018, integrated into UniProtKB/TrEMBL.
DT   25-APR-2018, sequence version 1.
DT   27-MAR-2024, entry version 15.
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   Name=treS {ECO:0000313|EMBL:PJE96004.1};
GN   ORFNames=CUT44_19570 {ECO:0000313|EMBL:PJE96004.1};
OS   Streptomyces carminius.
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Streptomyces.
OX   NCBI_TaxID=2665496 {ECO:0000313|EMBL:PJE96004.1, ECO:0000313|Proteomes:UP000230407};
RN   [1] {ECO:0000313|EMBL:PJE96004.1, ECO:0000313|Proteomes:UP000230407}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TRM SA0054 {ECO:0000313|EMBL:PJE96004.1,
RC   ECO:0000313|Proteomes:UP000230407};
RA   Wang Y., Luo X., Wan C., Zhang L.;
RT   "Streptomyces carmine sp. nov., a novel actinomycete isolated from Sophora
RT   alopecuroides in Xinjiang, China.";
RL   Submitted (NOV-2017) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PJE96004.1}.
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DR   EMBL; PGGW01000060; PJE96004.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2M8LVL7; -.
DR   Proteomes; UP000230407; 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:0016740; F:transferase activity; 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   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000230407};
KW   Transferase {ECO:0000313|EMBL:PJE96004.1}.
FT   DOMAIN          31..433
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   565 AA;  65231 MW;  4223532EA48318EE CRC64;
     MTVNEPVIDT FEDTPAKDRD PDWFKRAVFY EVLVRSFQDS NGDGIGDLKG LTARLDYLQW
     LGVDCLWLPP FFKSPLKDGG YDVADYASVL PEFGDLADFV EFVDAAHQRG MRIIIDMVMN
     HTSDQHPWFQ ESRRDPDGPY GDYYVWADDD KQYPDARIIF VDTEASNWTF DPVRKQYYWH
     RFFSHQPDLN YENPQVQEEM ISALRFWLDL GIDGFRLDAV PYLYAEEGTN CENLPATHEF
     LRRVRAEIDA HYPDTVLLAE ANQWPEDVVD YFGDYSKGGD ECHMAFHFPV MPRIFMAVRR
     ESRYPVSEIL AKTPAIPSGC QWGIFLRNHD ELTLEMVTDE ERDYMYAEYA KDPRMRANIG
     IRRRLATLLD NDRNQIELFT ALLLSLPGSP ILYYGDEIGM GDNIWLGDRD AVRTPMQWTP
     DRNAGFSSCD PGRLFLPAIM DPVYGYQVTN VEAAMSSPSS LLHWTRRMIE IRKQNPAFGL
     GSYTELPSSN PAVLAFLREY EDDLVLCVHN FSRFPQPTEL DLQAFSGRHP VELIGGVRFP
     PVGELPYLLT LAGHGFYWFR LRKQA
//
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