ID   J9WQQ7_MYCIP            Unreviewed;       593 AA.
AC   J9WQQ7;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 42.
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=MIP_07591 {ECO:0000313|EMBL:AFS17097.1};
OS   Mycobacterium indicus pranii (strain DSM 45239 / MTCC 9506).
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=1232724 {ECO:0000313|EMBL:AFS17097.1, ECO:0000313|Proteomes:UP000007329};
RN   [1] {ECO:0000313|EMBL:AFS17097.1, ECO:0000313|Proteomes:UP000007329}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MTCC 9506 {ECO:0000313|EMBL:AFS17097.1};
RX   PubMed=17912347; DOI=10.1371/journal.pone.0000968;
RA   Ahmed N., Saini V., Raghuvanshi S., Khurana J.P., Tyagi A.K., Tyagi A.K.,
RA   Hasnain S.E.;
RT   "Molecular analysis of a leprosy immunotherapeutic bacillus provides
RT   insights into Mycobacterium evolution.";
RL   PLoS ONE 2:E968-E968(2007).
RN   [2] {ECO:0000313|EMBL:AFS17097.1, ECO:0000313|Proteomes:UP000007329}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 45239 / MTCC 9506 {ECO:0000313|Proteomes:UP000007329};
RX   PubMed=22965120; DOI=10.1093/nar/gks793;
RA   Saini V., Raghuvanshi S., Khurana J.P., Ahmed N., Hasnain S.E., Tyagi A.K.,
RA   Tyagi A.K.;
RT   "Massive gene acquisitions in Mycobacterium indicus pranii provide a
RT   perspective on mycobacterial evolution.";
RL   Nucleic Acids Res. 40:10832-10850(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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP002275; AFS17097.1; -; Genomic_DNA.
DR   AlphaFoldDB; J9WQQ7; -.
DR   KEGG; mid:MIP_07591; -.
DR   PATRIC; fig|1232724.3.peg.5144; -.
DR   HOGENOM; CLU_006462_2_1_11; -.
DR   Proteomes; UP000007329; 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
//