ID   H8IJG9_MYCIA            Unreviewed;       593 AA.
AC   H8IJG9;
DT   16-MAY-2012, integrated into UniProtKB/TrEMBL.
DT   16-MAY-2012, sequence version 1.
DT   27-MAR-2024, entry version 50.
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=OCU_50090 {ECO:0000313|EMBL:AFC46228.1};
OS   Mycobacterium intracellulare (strain ATCC 13950 / DSM 43223 / JCM 6384 /
OS   NCTC 13025 / 3600).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=487521 {ECO:0000313|EMBL:AFC46228.1, ECO:0000313|Proteomes:UP000008004};
RN   [1] {ECO:0000313|EMBL:AFC46228.1, ECO:0000313|Proteomes:UP000008004}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 13950 / DSM 43223 / JCM 6384 / NCTC 13025 / 3600
RC   {ECO:0000313|Proteomes:UP000008004};
RX   PubMed=22535933; DOI=10.1128/JB.00295-12;
RA   Kim B.J., Choi B.S., Lim J.S., Choi I.Y., Lee J.H., Chun J., Kook Y.H.,
RA   Kim B.J.;
RT   "Complete genome sequence of Mycobacterium intracellulare strain ATCC
RT   13950T.";
RL   J. Bacteriol. 194:2750-2750(2012).
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; CP003322; AFC46228.1; -; Genomic_DNA.
DR   AlphaFoldDB; H8IJG9; -.
DR   KEGG; mia:OCU_50090; -.
DR   PATRIC; fig|487521.10.peg.5016; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_006462_2_1_11; -.
DR   Proteomes; UP000008004; 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}.
FT   DOMAIN          54..456
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          1..24
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   593 AA;  67879 MW;  F8B1D8084DF3C086 CRC64;
     MDLMNDAKEA VEHHPEGGSH VQDGVVEHPD AEDFNNAAAL PTDPTWFKHA VFYEVLVRAF
     FDANADGAGD LRGLLGQLDY LQWLGIDCIW LPPFYDSPLR DGGYDIRDFY KVLPEFGTVE
     DFVALLNAAH ERGIRVITDL VMNHTSDSHP WFQESRHDPD GPYGDYYVWS DTSERYTDAR
     IIFIDTEESN WTFDPVRKQF YWHRFFSHQP DLNYENPAVQ EAMIDVLRFW LGLGIDGFRL
     DAVPYLFERE GTNCENLPET HAFLKRVRKV VDDEFPGRVL LAEANQWPAD VVEYFGDPST
     GGDECHMAFH FPLMPRIFMA VRRESRFPIS EILAQTPEIP DMAQWGIFLR NHDELTLEMV
     TDEERDYMYS EYAKDPRMKA NVGIRRRLAP LLDNDRNQIE LFTALLLSLP GSPVLYYGDE
     IGMGDVIWLG DRDGVRTPMQ WTPDRNAGFS KANPGRLYLP PSQDSVYGYQ AVNVEAQRDT
     STSLLNFTRT MLAVRRRHEA FAIGSFEELG GSNPSVLAFL RQVSGDGDTV LCVNNLSRFP
     QPIELNLQHW SGRTPVELTG QVEFPRIGHL PYLLTLPGHG FYWFRLSGCE EDA
//