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Database: UniProt
Entry: A0A0N0NDA3_9ACTN
LinkDB: A0A0N0NDA3_9ACTN
Original site: A0A0N0NDA3_9ACTN 
ID   A0A0N0NDA3_9ACTN        Unreviewed;       572 AA.
AC   A0A0N0NDA3;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   27-MAR-2024, entry version 23.
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=OV320_3997 {ECO:0000313|EMBL:KPI29658.1};
OS   Actinobacteria bacterium OV320.
OC   Bacteria; Actinomycetota; Actinomycetes.
OX   NCBI_TaxID=1592329 {ECO:0000313|EMBL:KPI29658.1, ECO:0000313|Proteomes:UP000037870};
RN   [1] {ECO:0000313|EMBL:KPI29658.1, ECO:0000313|Proteomes:UP000037870}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OV320 {ECO:0000313|EMBL:KPI29658.1,
RC   ECO:0000313|Proteomes:UP000037870};
RA   Brown S.D., Utturkar S.M., Klingeman D.M., Pelletier D.;
RT   "Draft genome sequences for four actinobacteria strains OK006 OK074 OV450
RT   and OV320.";
RL   Submitted (AUG-2015) 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:KPI29658.1}.
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DR   EMBL; LJCX01000024; KPI29658.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0N0NDA3; -.
DR   PATRIC; fig|1592329.3.peg.3228; -.
DR   Proteomes; UP000037870; 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; 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, ECO:0000313|EMBL:KPI29658.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037870}.
FT   DOMAIN          31..433
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   572 AA;  65997 MW;  6D45AF21C5CAE611 CRC64;
     MIVNEPVQDT FEDTPAKDRD PEWFKRAVFY EVLVRSFQDS NGDGVGDLKG ITAKLDYLQW
     LGVDCLWLPP FFKSPLRDGG YDVSDYTAVL PEFGDLADFV EFVDAAHQRG MRVIIDFVMN
     HTSDQHPWFQ ESRKDPDGPY GDYYMWADDD KQYGDARIIF VDTEVSNWTF DPVRKQYFFH
     RFFSHQPDLN YENPAVQEEM ISALRFWLDL GIDGFRLDAV PYLYAEEGTN CENLPATHEF
     LKRVRKEIDA HYPDTVILAE ANQWPEDVVD YFGDYASGGD ECHMAFHFPV MPRIFMAVRR
     ESRYPVSEIL AKTPAIPSRC QWGIFLRNHD ELTLEMVTDE ERDYMYAEYA KDPRMRANIG
     IRRRLAPLLD NDRNQIELFT ALLLSLPGSP ILYYGDEIGM GDNIWLGDRD AVRTPMQWTP
     DRNAGFSSCD PGRLVLPTIM DPVYGYQVTN VEASMSSPSS LLHWTRRMIE IRKQNPAFGL
     GTYTELQSSN PAVLAFLREA PLTKEGEDDL VLCVHNFSRF AQPTELDLSR FKGRYPVELF
     GGVRFPAVGD LPYLLTMAGH GFYWFRLRRD AA
//
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