ID A0A343J8X4_9CLOT Unreviewed; 454 AA.
AC A0A343J8X4;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:ASW41982.1};
GN ORFNames=BEN51_00190 {ECO:0000313|EMBL:ASW41982.1};
OS Clostridium isatidis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=182773 {ECO:0000313|EMBL:ASW41982.1, ECO:0000313|Proteomes:UP000264883};
RN [1] {ECO:0000313|EMBL:ASW41982.1, ECO:0000313|Proteomes:UP000264883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15098 {ECO:0000313|EMBL:ASW41982.1,
RC ECO:0000313|Proteomes:UP000264883};
RA Little G.T., Minton N.P.;
RT "Complete Genome Sequence Of The Indigo Reducing Clostridium isatidis
RT DSM15098.";
RL Submitted (AUG-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 -!- SUBUNIT: Homotetramer. {ECO:0000256|ARBA:ARBA00011881}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family.
CC {ECO:0000256|ARBA:ARBA00010141, ECO:0000256|RuleBase:RU361152}.
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DR EMBL; CP016786; ASW41982.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A343J8X4; -.
DR KEGG; cia:BEN51_00190; -.
DR OrthoDB; 9808275at2; -.
DR Proteomes; UP000264883; 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:UP000264883}.
FT DOMAIN 198..415
FT /note="Glycosyl hydrolase family 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11975"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 173
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT BINDING 203
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT SITE 113
FT /note="Increases basicity of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ SEQUENCE 454 AA; 50568 MW; 04EC192333E976E2 CRC64;
MSKKPLKIVT IGGGSSYTPE LVEGLIKRYD EMPVSDYWLV DIEEGKEKLE IVGALAKRMV
EKAGVPMNIH LTLDRREALK DADFVTTQLR VGLLDARVKD ERIPLSYGFL GQETNGAGGL
FKALRTVPVI LDIAKDMSEL CPDAWLINFT NPAGIVTEAL LRYGVHKKVV GVCNVPIGME
FGFADALGVD KERITVDFAG LNHMVYAERV YLDGRDVTSQ LIDILTNNNS KSQTMANIAA
LDWDPATIKA FGVLPCPYHR YYYKKQEMLN HELEEFKNGK TRAEVVKEVE KRLFELYKNP
ELKDKPEELS RRGGAHYSDV ACNVINGIYN DKNTIIAVNT RNNGTLKQFE DASAIEVSCY
VGKNGPVPVE TVTDLPIFAQ GLAGQIKAFE RLAAEAAYTG DYNTALAAMV TNPLVADDKK
GRKLLNEMLL AHKDYLPQFK KVIDVLEKVE RAEF
//
