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Database: UniProt
Entry: A0A179SNE8_9BACI
LinkDB: A0A179SNE8_9BACI
Original site: A0A179SNE8_9BACI 
ID   A0A179SNE8_9BACI        Unreviewed;       501 AA.
AC   A0A179SNE8;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 24.
DE   SubName: Full=Alpha-glucosidase/alpha-galactosidase {ECO:0000313|EMBL:OAS83217.1};
GN   ORFNames=A6K24_08845 {ECO:0000313|EMBL:OAS83217.1};
OS   Metabacillus litoralis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Metabacillus.
OX   NCBI_TaxID=152268 {ECO:0000313|EMBL:OAS83217.1, ECO:0000313|Proteomes:UP000078534};
RN   [1] {ECO:0000313|Proteomes:UP000078534}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C44 {ECO:0000313|Proteomes:UP000078534};
RA   Lyu Z., Lyu W.;
RL   Submitted (APR-2016) to the EMBL/GenBank/DDBJ databases.
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:OAS83217.1}.
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DR   EMBL; LWSG01000042; OAS83217.1; -; Genomic_DNA.
DR   RefSeq; WP_066337455.1; NZ_LWSG01000042.1.
DR   AlphaFoldDB; A0A179SNE8; -.
DR   STRING; 152268.A6K24_08845; -.
DR   OrthoDB; 9808275at2; -.
DR   Proteomes; UP000078534; 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; cd05297; GH4_alpha_glucosidase_galactosidase; 1.
DR   Gene3D; 3.90.1820.10; AglA-like glucosidase; 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:SF6; ALPHA-GALACTOSIDASE; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078534}.
FT   DOMAIN          195..413
FT                   /note="Glycosyl hydrolase family 4 C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF11975"
FT   REGION          475..501
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         149
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   SITE            110
FT                   /note="Increases basicity of active site Tyr"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ   SEQUENCE   501 AA;  56163 MW;  28625C467546902A CRC64;
     MSFKIAFIGA GSIGFTRGLL RDLLAIPEFN QIEVSFTDIN SQNLDMVTQL CQRDIDDNGL
     DIKIFSTTNR REALRDARYI FSVVRIGGLE AFQTDVDIPL KYGIDQCVGD TLCAGGIMYG
     QRGIAEMMEI CKDIREVAEK NCLLLNYANP MAMLTWACNT YGGVRTIGLC HGVQGGHRQI
     ANALGLKKEE VDIICAGINH QTWYISVKHN GEDMTGEILE AFENHPEFSK TEKVRIDMLR
     RFGFYSTESN GHLSEYVPWY RKRAEEINDW IDLGTWINGE TGGYLRVCTE GRNWFETDFP
     NWLKEPAMEY KQENRGEEHG SYIIEALETG RVYRGHFNVV NNGVISNLPD DAIIEAPGYV
     DRNGISMPHV GDLPLGCAAV CNVSISVQRL AVEAAINGDD FLLRQAMMMD PLVGAVCNPK
     EIWQMTDEML VAQERWLPQY SDAIAEAKKR LASGNLLPTK NYEGAARLKV KTVEEMAQNR
     DEATKNAGES DKAKERPSVV K
//
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