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Database: UniProt
Entry: A0A0M4GA82_9BACI
LinkDB: A0A0M4GA82_9BACI
Original site: A0A0M4GA82_9BACI 
ID   A0A0M4GA82_9BACI        Unreviewed;       450 AA.
AC   A0A0M4GA82;
DT   09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT   09-DEC-2015, sequence version 1.
DT   24-JAN-2024, entry version 27.
DE   SubName: Full=6-phospho-alpha-glucosidase {ECO:0000313|EMBL:ALC82390.1};
GN   ORFNames=AM592_12960 {ECO:0000313|EMBL:ALC82390.1};
OS   Bacillus gobiensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1441095 {ECO:0000313|EMBL:ALC82390.1, ECO:0000313|Proteomes:UP000067625};
RN   [1] {ECO:0000313|Proteomes:UP000067625}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FJAT-4402 {ECO:0000313|Proteomes:UP000067625};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA   Shi H., Pan Z., Liu X.;
RT   "Genome sequencing project for genomic taxonomy and phylogenomics of
RT   Bacillus-like bacteria.";
RL   Submitted (AUG-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ALC82390.1, ECO:0000313|Proteomes:UP000067625}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FJAT-4402 {ECO:0000313|EMBL:ALC82390.1,
RC   ECO:0000313|Proteomes:UP000067625};
RX   PubMed=26530456; DOI=10.1099/ijsem.0.000729;
RA   Liu B., Liu G.H., Cetin S., Schumann P., Pan Z.Z., Chen Q.Q.;
RT   "Bacillus gobiensis sp. nov., isolated from a soil sample.";
RL   Int. J. Syst. Evol. Microbiol. 66:379-384(2016).
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}.
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DR   EMBL; CP012600; ALC82390.1; -; Genomic_DNA.
DR   RefSeq; WP_053604176.1; NZ_CP012600.1.
DR   AlphaFoldDB; A0A0M4GA82; -.
DR   STRING; 1441095.AM592_12960; -.
DR   PATRIC; fig|1441095.3.peg.2843; -.
DR   OrthoDB; 9808275at2; -.
DR   Proteomes; UP000067625; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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; IPR019802; GlycHydrolase_4_CS.
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.
DR   PROSITE; PS01324; GLYCOSYL_HYDROL_F4; 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   Membrane {ECO:0000256|SAM:Phobius};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR601088-3};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU361152};
KW   Nickel {ECO:0000256|PIRSR:PIRSR601088-3};
KW   Reference proteome {ECO:0000313|Proteomes:UP000067625};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        6..26
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          197..417
FT                   /note="Glycosyl hydrolase family 4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11975"
FT   ACT_SITE        172
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT   ACT_SITE        265
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT   BINDING         95
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT   BINDING         149
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT   BINDING         171
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   BINDING         202
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT   BINDING         285
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT   SITE            111
FT                   /note="Increases basicity of active site Tyr"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ   SEQUENCE   450 AA;  50670 MW;  24453272D958F180 CRC64;
     MMTKSFSVVI AGGGSTFTPG IVLMLLDNLD QFPIRKLKLY DNDKERQDKI AGACEIFIHE
     KAPEIEFLAT DDPEQAFTDV DFVMAHIRVG KYAMRELDEK IPLKYGVVGQ ETCGPGGIAY
     GMRSIGGVLE IIDYMEKYSP DAWMLNYSNP AAIVAEATRR LRPDSKVLNI CDMPVGIEDR
     MAEIAGLSSR KEMKVRYYGL NHFGWWTEIQ DSEGNDLMPV LKKHIKEFGY TPNANHHPTE
     KSWNDTFTKA RDVYATDPDV LPNTYLQYYF FPQQMAKKSN PDFTRANEVM AGREAFIFSQ
     CQKIVEEGSS KNSEIEIDDH ASYIVDLARA IAYNTGERML LIVENNGAIE NFDSTAMVEI
     PCIVGSNGPE PLAVGKIPQF QKGLMEQQVS VEKLVVEAWV EKSSQKLWQA IILSKTVPGA
     DVAKAILEDL IEANREYWPQ LEEKPLQPII
//
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