ID M5P6F0_9BACI Unreviewed; 453 AA.
AC M5P6F0;
DT 29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 29-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 37.
DE SubName: Full=6-phospho-alpha-glucosidase {ECO:0000313|EMBL:EME75028.1};
GN ORFNames=BSONL12_08562 {ECO:0000313|EMBL:EME75028.1};
OS Bacillus sonorensis L12.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1274524 {ECO:0000313|EMBL:EME75028.1, ECO:0000313|Proteomes:UP000011907};
RN [1] {ECO:0000313|EMBL:EME75028.1, ECO:0000313|Proteomes:UP000011907}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=L12 {ECO:0000313|EMBL:EME75028.1,
RC ECO:0000313|Proteomes:UP000011907};
RX PubMed=23538904;
RA Adimpong D.B., Sorensen K.I., Nielsen D.S., Thorsen L., Rasmussen T.B.,
RA Derkx P.M., Jespersen L.;
RT "Draft Whole-Genome Sequence of Bacillus sonorensis Strain L12, a Source of
RT Nonribosomal Lipopeptides.";
RL Genome Announc. 1:E0009713-E0009713(2013).
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000256|RuleBase:RU361152};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000256|RuleBase:RU361152};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family.
CC {ECO:0000256|ARBA:ARBA00010141, ECO:0000256|RuleBase:RU361152}.
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:EME75028.1}.
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DR EMBL; AOFM01000006; EME75028.1; -; Genomic_DNA.
DR RefSeq; WP_006637714.1; NZ_AOFM01000006.1.
DR AlphaFoldDB; M5P6F0; -.
DR STRING; 1274524.BSONL12_08562; -.
DR GeneID; 79845330; -.
DR PATRIC; fig|1274524.3.peg.1854; -.
DR eggNOG; COG1486; Bacteria.
DR OrthoDB; 9808275at2; -.
DR Proteomes; UP000011907; Unassembled WGS sequence.
DR GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016616; F:oxidoreductase activity, acting on the CH-OH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd05298; GH4_GlvA_pagL_like; 1.
DR Gene3D; 3.90.110.10; Lactate dehydrogenase/glycoside hydrolase, family 4, C-terminal; 1.
DR Gene3D; 3.40.50.720; NAD(P)-binding Rossmann-like Domain; 1.
DR InterPro; IPR001088; Glyco_hydro_4.
DR InterPro; IPR022616; Glyco_hydro_4_C.
DR InterPro; IPR015955; Lactate_DH/Glyco_Ohase_4_C.
DR InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR PANTHER; PTHR32092; 6-PHOSPHO-BETA-GLUCOSIDASE-RELATED; 1.
DR PANTHER; PTHR32092:SF14; MALTOSE-6'-PHOSPHATE GLUCOSIDASE; 1.
DR Pfam; PF02056; Glyco_hydro_4; 1.
DR Pfam; PF11975; Glyco_hydro_4C; 1.
DR PRINTS; PR00732; GLHYDRLASE4.
DR SUPFAM; SSF56327; LDH C-terminal domain-like; 1.
DR SUPFAM; SSF51735; NAD(P)-binding Rossmann-fold domains; 1.
PE 3: Inferred from homology;
KW Cobalt {ECO:0000256|PIRSR:PIRSR601088-3};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361152};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361152};
KW Iron {ECO:0000256|PIRSR:PIRSR601088-3};
KW Manganese {ECO:0000256|PIRSR:PIRSR601088-3};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR601088-3};
KW NAD {ECO:0000256|RuleBase:RU361152};
KW Nickel {ECO:0000256|PIRSR:PIRSR601088-3}.
FT DOMAIN 195..416
FT /note="Glycosyl hydrolase family 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11975"
FT ACT_SITE 171
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT ACT_SITE 266
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 170
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT BINDING 200
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT BINDING 286
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT SITE 109
FT /note="Increases basicity of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ SEQUENCE 453 AA; 51224 MW; E2B03A8CA7720AD0 CRC64;
MKTYKLAIAG GGSTYTPGII RSLMERLEDL PLSEIRFYDI DGERQSKVVI AAKAVISEYT
DKIVIVDTTD PETAFTDADF VFAQMRVGKY KMRELDEKIP LSHDVVGQET CGPGGLAYGL
RTISPMVELI DFVEQYAKET CWIVNYSNPA SIVAEAVRKL RPKARVLNIC DMPVATMRNM
SAILGVNRED LVVDYFGLNH FGWFTKVEVY GVDRLPELRE HIHKHGLLTE DISKIDYRHA
DASWIKTFKN IKLIMDFFPE YIPNPYLQYY LLPDLIVETS NKEYTRANEV MNGREKTLFE
TVKQYEETGV LSDQFHVGVH GIFIVDVTVS LAKNLGKRYL VMVENNGTIP NLPDDAMVEV
PCLINADGPA PEYVGDIPYF YKAMIDQQLA SEKILVEAIT EGSYEKALQA FTLNKTLPSS
KVAKAVLDDL IEANKAYWPE LKSKYRDGVL IHS
//
