ID L1MEN7_9CORY Unreviewed; 560 AA.
AC L1MEN7;
DT 06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT 06-MAR-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=HMPREF9997_01852 {ECO:0000313|EMBL:EKX89381.1};
OS Corynebacterium durum F0235.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=1035195 {ECO:0000313|EMBL:EKX89381.1, ECO:0000313|Proteomes:UP000010445};
RN [1] {ECO:0000313|EMBL:EKX89381.1, ECO:0000313|Proteomes:UP000010445}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0235 {ECO:0000313|EMBL:EKX89381.1,
RC ECO:0000313|Proteomes:UP000010445};
RA Weinstock G., Sodergren E., Lobos E.A., Fulton L., Fulton R., Courtney L.,
RA Fronick C., O'Laughlin M., Godfrey J., Wilson R.M., Miner T., Farmer C.,
RA Delehaunty K., Cordes M., Minx P., Tomlinson C., Chen J., Wollam A.,
RA Pepin K.H., Bhonagiri V., Zhang X., Suruliraj S., Warren W., Mitreva M.,
RA Mardis E.R., Wilson R.K.;
RL Submitted (MAY-2012) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EKX89381.1}.
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DR EMBL; AMEM01000024; EKX89381.1; -; Genomic_DNA.
DR AlphaFoldDB; L1MEN7; -.
DR STRING; 1035195.HMPREF9997_01852; -.
DR PATRIC; fig|1035195.3.peg.1674; -.
DR eggNOG; COG0366; Bacteria.
DR HOGENOM; CLU_006462_2_1_11; -.
DR Proteomes; UP000010445; Unassembled WGS sequence.
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:0016740; F:transferase activity; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000010445};
KW Transferase {ECO:0000313|EMBL:EKX89381.1}.
FT DOMAIN 31..445
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 560 AA; 64563 MW; 3EE7C1FDA2791A7C CRC64;
MAKQLEDNAP ASQRVAHRHP HDWYKQAVFY EVLVQAFKDS NGDGIGDFQG LTEMLDYLQW
LGVDCVWLPP VFDSPLLDGG YDVRDFTKIL PDYGIVDDLQ HLVAQAHQRG IRVIMDLVMN
HTSDQHLWFE QSRRNPHGPY GDYYVWSDTP ELYSDARIIF IDTEDSNWSY DPVRGQYYWH
RFFSHQPDLN YENPAVQEEM LNTMRFWLDL GLDGFRLDAV PYLFEENGTN CENLAPTHEF
LKRCRRLVDQ EYPGRVLLAE ANQWPHDVVE YFGDGPIGNE CHMAFHFPLM PRLFMSLKEE
SAQSVVDILA NTPAIPESGQ WGIFLRNHDE LTLEMVNDVE RAFMYEHYAQ NPRMRSNVGI
RRRLASLLQG DLAQLQLLTN LLLSLPGSPV LYYGDEIGMG DNIWLHDRDG VRTPMQWSDQ
RNSGFSDTDP EQLPLPVITN CQFGHQAVNV ENQLRNPGSL LHFTRNLIAV RKEHATFGMG
SFRPVASSNP AIFAFIRQYR DETLLCVSNF AATPQHTELA LEEFVGRTPV ELLGNTAFHT
ITESWTLTLA PRGFYWMSLR
//
