ID   F6FR14_ISOV2            Unreviewed;       593 AA.
AC   F6FR14;
DT   27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT   27-JUL-2011, sequence version 1.
DT   27-MAR-2024, entry version 54.
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   OrderedLocusNames=Isova_2244 {ECO:0000313|EMBL:AEG44964.1};
OS   Isoptericola variabilis (strain 225).
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales;
OC   Promicromonosporaceae; Isoptericola.
OX   NCBI_TaxID=743718 {ECO:0000313|Proteomes:UP000009236};
RN   [1] {ECO:0000313|EMBL:AEG44964.1, ECO:0000313|Proteomes:UP000009236}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=225 {ECO:0000313|Proteomes:UP000009236};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Mikhailova N., Zeytun A., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Siebers A., Allgaier M., Thelen M.,
RA   Hugenholtz P., Gladden J., Woyke T.;
RT   "Complete sequence of Isoptericola variabilis 225.";
RL   Submitted (MAY-2011) 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; CP002810; AEG44964.1; -; Genomic_DNA.
DR   RefSeq; WP_013839355.1; NC_015588.1.
DR   AlphaFoldDB; F6FR14; -.
DR   STRING; 743718.Isova_2244; -.
DR   KEGG; iva:Isova_2244; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_006462_2_1_11; -.
DR   Proteomes; UP000009236; 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, ECO:0000313|EMBL:AEG44964.1};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Reference proteome {ECO:0000313|Proteomes:UP000009236}.
FT   DOMAIN          51..452
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   593 AA;  67614 MW;  226DC7996B5EC24F CRC64;
     MSTEPISVPR PITRQIPVQA LPPRRQPELP PLERPGLSDD PDWYRKAVFY EVMVRSFSDS
     DGTGSGDLRG IIERLDYLQW LGVDALWLPP FYPSPMRDGG YDVADYTAIA SQYGSLQDFT
     ELIEESHARG MRVVIDLVMN HTSDQHPWFQ ASRSDPEGPY GDFYVWSDDD KRYQDARIIF
     VDTETSNWTF DPVRRQYFWH RFFSHQPDLN FENPRVADAM LDVARFWLQI GVDGFRLDAV
     PYLFEAEGTN CENLPETHAF LRRVRRMIDT EFPGRIMLAE ANQWPQDVVH YFGTEDEPEC
     HMCFHFPVMP RIFYAIRDQR ATQVLDILAD TPDIPASGGQ WSTFLRNHDE LTLEMVSTEE
     RAAMYGWYAH DPRMRANIGI RRRLAPLLDN SRKEIELAHA LLLSLPGSPC LYYGDEIGMG
     DNIWLPDRDA VRTPMQWTPD RNAGFSTADP GKLYLPLIQS LVHHYNHTNV EAQLAQPTSL
     LHWVHGMLGI RKLHPAFGTG NFVARPCDDD AILAFTRASA EEVLLVTANL SATARSATIT
     LPGFEGWSLT DLFGGGRFPA VGHDARVTMT WGSREFYWLL LTPPSHGHRG GEG
//