ID A0PWJ0_MYCUA Unreviewed; 597 AA.
AC A0PWJ0;
DT 09-JAN-2007, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2007, sequence version 1.
DT 27-MAR-2024, entry version 97.
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 Name=treS {ECO:0000313|EMBL:ABL06709.1};
GN OrderedLocusNames=MUL_4797 {ECO:0000313|EMBL:ABL06709.1};
OS Mycobacterium ulcerans (strain Agy99).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium ulcerans group.
OX NCBI_TaxID=362242 {ECO:0000313|EMBL:ABL06709.1, ECO:0000313|Proteomes:UP000000765};
RN [1] {ECO:0000313|EMBL:ABL06709.1, ECO:0000313|Proteomes:UP000000765}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Agy99 {ECO:0000313|EMBL:ABL06709.1,
RC ECO:0000313|Proteomes:UP000000765};
RX PubMed=17210928; DOI=10.1101/gr.5942807;
RA Stinear T.P., Seemann T., Pidot S., Frigui W., Reysset G., Garnier T.,
RA Meurice G., Simon D., Bouchier C., Ma L., Tichit M., Porter J.L., Ryan J.,
RA Johnson P.D., Davies J.K., Jenkin G.A., Small P.L., Jones L.M., Tekaia F.,
RA Laval F., Daffe M., Parkhill J., Cole S.T.;
RT "Reductive evolution and niche adaptation inferred from the genome of
RT Mycobacterium ulcerans, the causative agent of Buruli ulcer.";
RL Genome Res. 17:192-200(2007).
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; CP000325; ABL06709.1; -; Genomic_DNA.
DR AlphaFoldDB; A0PWJ0; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR KEGG; mul:MUL_4797; -.
DR eggNOG; COG0366; Bacteria.
DR HOGENOM; CLU_006462_2_1_11; -.
DR Proteomes; UP000000765; 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..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..15
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 597 AA; 68332 MW; D7059B7C680E6055 CRC64;
MELMNEATNT IEHNPAEGSH VEGGMVEHPD AKDFGNAAPL PADPTWFKHA VFYEVLVRAF
YDGTADGSGD LRGLMQRLDY LQWLGIDCIW LPPFYDSPLR DGGYDIRDFY KVLPEFGTVG
DFVALVDAAH RRGIRVITDL VMNHTSESHP WFQESRHDPD GPYGDYYVWS DSSEKYTDAR
IIFVDTEESN WTFDPVRRQF YWHRFFSHQP DLNYDNPAVQ EAMIDVLRFW LGLGIDGFRL
DAVPYLFERE GTNCENLPET HAFLKRVRKV VDDEFPGRLL LAEANQWPAD VVEYFGEAST
GGDECHMAFH FPLMPRIFMA VRRESRFPIS EILAKTPPIP DMAQWGIFLR NHDELTLEMV
TDEERDYMYA EYAKDPRMKA NVGIRRRLAP LLENDRNQIQ LFNALLLSLP GSPVLYYGDE
IGMGDVIWLG DRDGVRTPMQ WTPDRNAGFS TANPGRLYLP PSQDSVYGYQ AVNVEAQRDT
STSLLNWTRT MLAVRRRHNA FAVGTFQELG GSNPSILAYV REAPGPAGED GDVVLCVNNL
SRFPQPIELN LQQWNSYTPV ELTGQVEFRK IGHLPYLLTL PGHGFYWFQL SASEEER
//
