ID   J9Z921_LEPFM            Unreviewed;       559 AA.
AC   J9Z921;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 44.
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=LFML04_0735 {ECO:0000313|EMBL:AFS52969.1};
OS   Leptospirillum ferriphilum (strain ML-04).
OC   Bacteria; Nitrospirota; Nitrospiria; Nitrospirales; Nitrospiraceae;
OC   Leptospirillum.
OX   NCBI_TaxID=1048260 {ECO:0000313|EMBL:AFS52969.1, ECO:0000313|Proteomes:UP000006177};
RN   [1] {ECO:0000313|EMBL:AFS52969.1, ECO:0000313|Proteomes:UP000006177}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ML-04 {ECO:0000313|EMBL:AFS52969.1,
RC   ECO:0000313|Proteomes:UP000006177};
RX   PubMed=22203551; DOI=10.1007/s12275-011-1099-9;
RA   Mi S., Song J., Lin J., Che Y., Zheng H., Lin J.;
RT   "Complete genome of Leptospirillum ferriphilum ML-04 provides insight into
RT   its physiology and environmental adaptation.";
RL   J. Microbiol. 49:890-901(2011).
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; CP002919; AFS52969.1; -; Genomic_DNA.
DR   RefSeq; WP_014960479.1; NC_018649.1.
DR   AlphaFoldDB; J9Z921; -.
DR   STRING; 1048260.LFML04_0735; -.
DR   KEGG; lfi:LFML04_0735; -.
DR   PATRIC; fig|1048260.3.peg.794; -.
DR   HOGENOM; CLU_006462_2_1_0; -.
DR   Proteomes; UP000006177; 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; 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}.
FT   DOMAIN          18..416
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   559 AA;  65334 MW;  D4479816E49AA982 CRC64;
     MTDESLGKGW YKDAIIYEVH VKSFQDSNSD GWGDFIGLTG KLDYLQKLGV TALWLLPFTD
     SPLKDDGYDI RDYYKVHPPY GSMEDFQGFL EEAHKRGLRV ITELVMNHTS NTHPWFLSAS
     SSRSSPFRDY YVWSDTPDRY KGTRIIFSDT EKSNWTWEPK TRQYYWHRFF HHQPDLNFDN
     PKVQEEMLNV VKFWFSLGVD GLRCDAVPYL YEREGTNCEN LPETHAFIKR LRADIDREFP
     DRMLLAEANQ WPHDVLPYFG NDDEFHMAYH FPLMPRLFIA IAQGDRKPIT DILQQTPPIP
     EGCQWAIFLR NHDELTLEMV SDQERDYLWS TYAEDPRMRL NLGIRRRLAP LMGNDRRKID
     LMHSLLLTLP GTPILYYGDE IGMGDNIHLG DRNGVRTPMQ WSFDRNGGFS NADPSDLYAP
     PIQNPVYGYQ VVNVETQIRY PTSPLNVLRQ MIEVRQSTPV FGRGTMTVLH PKNRHVFACL
     RELGNDVVLV INNLSDRTES VLLDLSRFRG YRPVELFSQT LFPVLERAHF HFTVSPYGYF
     WLALRPPDAP VRSRKKIVR
//