ID A0A1V1I0B1_9FIRM Unreviewed; 434 AA.
AC A0A1V1I0B1;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:CED93557.1};
GN ORFNames=CRIB_805 {ECO:0000313|EMBL:CED93557.1};
OS Romboutsia ilealis.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Peptostreptococcaceae;
OC Romboutsia.
OX NCBI_TaxID=1115758 {ECO:0000313|EMBL:CED93557.1, ECO:0000313|Proteomes:UP000245622};
RN [1] {ECO:0000313|EMBL:CED93557.1, ECO:0000313|Proteomes:UP000245622}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CRIB {ECO:0000313|EMBL:CED93557.1,
RC ECO:0000313|Proteomes:UP000245622};
RA Hornung B.V.;
RL Submitted (APR-2014) 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; LN555523; CED93557.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V1I0B1; -.
DR Proteomes; UP000245622; Chromosome chr1.
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; 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.
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:UP000245622}.
FT DOMAIN 197..410
FT /note="Glycosyl hydrolase family 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11975"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 172
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 SITE 112
FT /note="Increases basicity of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ SEQUENCE 434 AA; 48795 MW; 69921BBBE32E6A5A CRC64;
MKEGIKIVTI GGGSSYTPEL IEGFIKRYDE LPVKELWLVD IEKGREKLEI VSNLARRMVK
KANIDMKIYS TLDRREALKD ADFVTTQFRV GQLDARIKDE KIPLSHGLIG QETNGAGGLF
KALRTIPVIL DIIKDIQELC SDAWLINFTN PAGIVSEAVF RYTNFKRYIG LCNVPIGMKN
NLAKLLEVDP SRIDMDFAGL NHMVYGLNVK LDGEDITGES IVKYIEGNIT MKNIKDIEFN
KEFIKALGVI PCPYHRYYYK SADMLKSELE EFKEGTIRGQ VVKKLEEELF ELYKDETLDI
KPPQLEKRGG AYYSDAACNL INSIYNNKKD IQVVNTLNNG AISDFKDDEV VEVSCVITKE
GPRPISMGYL PTAISGLVRQ IKSFELLAAK AAVTGDYDTA YLALCINPLT SSDDVAKIVF
DELIDAHSEY LIKK
//
