ID A0A0U4F955_9BACI Unreviewed; 440 AA.
AC A0A0U4F955;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:ALX50134.1};
GN ORFNames=AOX59_17050 {ECO:0000313|EMBL:ALX50134.1};
OS Lentibacillus amyloliquefaciens.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lentibacillus.
OX NCBI_TaxID=1472767 {ECO:0000313|EMBL:ALX50134.1, ECO:0000313|Proteomes:UP000050331};
RN [1] {ECO:0000313|EMBL:ALX50134.1, ECO:0000313|Proteomes:UP000050331}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LAM0015 {ECO:0000313|EMBL:ALX50134.1,
RC ECO:0000313|Proteomes:UP000050331};
RA Wang J.-L., He M.-X.;
RT "Complete genome sequence of strain Lentibacillus amyloliquefaciens
RT LAM0015T isolated from saline sediment.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
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; CP013862; ALX50134.1; -; Genomic_DNA.
DR RefSeq; WP_068447325.1; NZ_CP013862.1.
DR AlphaFoldDB; A0A0U4F955; -.
DR STRING; 1472767.AOX59_17050; -.
DR KEGG; lao:AOX59_17050; -.
DR OrthoDB; 9808275at2; -.
DR Proteomes; UP000050331; Chromosome.
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; cd05296; GH4_P_beta_glucosidase; 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:SF5; 6-PHOSPHO-BETA-GLUCOSIDASE; 1.
DR PANTHER; PTHR32092; 6-PHOSPHO-BETA-GLUCOSIDASE-RELATED; 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 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:UP000050331}.
FT DOMAIN 196..410
FT /note="Glycosyl hydrolase family 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11975"
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 201
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT SITE 111
FT /note="Increases basicity of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ SEQUENCE 440 AA; 48264 MW; A24BD2A5A50C18C5 CRC64;
MAGIKIVTIG GGSSYTPELV EGFIKRYDKL PVKELWLVDV PEGKEKLEIV GALAKRMVED
AGVPIDVHLS LDRREALPGA DFVTTQIRVG QLDARAKDES IPLKYGVIGQ ETNGPGGLFK
GLRTIPVILD ICRDIEVLCP DAWLINFSNP AGMVTEAVLR HSNISKTVGL CNVPVGMRMG
VAEMLDVDSD RVQIDFAGLN HMVYGLNVYL DGKNITENVL EQLVSGEGLT MKNIVDLGWE
KDFIKGLGAL PCPYHRYYYQ TSKMLEAEQK DFAEKGSRAQ VVQQLEKDLF ELYKNPDLSV
KPEQLEERGG AYYSDAACSL INSIYNDKRD IQPVNTRNNG AILGLPADSA VEVNCVITKD
GPRPIAVGDL PVAVRGLIQQ IKSFERVSAE AAVTGDYQKA MLAMTINPLV PSDSIAKAIL
DEMMEAHRDY LPQFLKAATP
//
