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Database: UniProt
Entry: A0A1V4J1S2_9CLOT
LinkDB: A0A1V4J1S2_9CLOT
Original site: A0A1V4J1S2_9CLOT 
ID   A0A1V4J1S2_9CLOT        Unreviewed;       452 AA.
AC   A0A1V4J1S2;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 19.
DE   SubName: Full=Putative 6-phospho-beta-glucosidase {ECO:0000313|EMBL:OPJ66099.1};
DE            EC=3.2.1.86 {ECO:0000313|EMBL:OPJ66099.1};
GN   Name=licH {ECO:0000313|EMBL:OPJ66099.1};
GN   ORFNames=CLCHR_02000 {ECO:0000313|EMBL:OPJ66099.1};
OS   Clostridium chromiireducens.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=225345 {ECO:0000313|EMBL:OPJ66099.1, ECO:0000313|Proteomes:UP000191056};
RN   [1] {ECO:0000313|EMBL:OPJ66099.1, ECO:0000313|Proteomes:UP000191056}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23318 {ECO:0000313|EMBL:OPJ66099.1,
RC   ECO:0000313|Proteomes:UP000191056};
RA   Poehlein A., Daniel R.;
RT   "Genome sequence of Clostridium chromiireducens DSM 23318.";
RL   Submitted (MAR-2017) 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}.
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:OPJ66099.1}.
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DR   EMBL; MZGT01000002; OPJ66099.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V4J1S2; -.
DR   STRING; 225345.CLCHR_02000; -.
DR   OrthoDB; 9808275at2; -.
DR   Proteomes; UP000191056; Unassembled WGS sequence.
DR   GO; GO:0008706; F:6-phospho-beta-glucosidase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0103047; F:methyl beta-D-glucoside 6-phosphate glucohydrolase activity; IEA:UniProtKB-EC.
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:UP000191056}.
FT   DOMAIN          198..418
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   452 AA;  51051 MW;  D95401FC4C0E1D12 CRC64;
     MRKEKIKIVT IGGGSSYTPE LIEGFIKRKA ELPIKEIWLV DIEDGKEKLE IVGAMAQRMV
     KAAGLDWEVN LTLDRRKALK DADFVSTQFR VGLLDARIKD ERIPLSHGMI GQETNGAGGM
     FKAFRTIPVI LDIIDDMREL CPDAWLVNFT NPSGMVTEAA IKYGGWDRTV GLCNVPINCI
     EDDAKKLDVP SSELFFKFAG LNHFHWHRVW DKEGNERTAE VIEKLYNPEL AEEKKDAGVA
     NIKDIKFNYE QIKDLGILPC PYHRYYYVTD DMLQEELESF SKGETRAEVV KRTEAELFEL
     YKDPKLDYKP EQLTKRGGTH YSDAACELIA SIYNDKRTTM VVCTKNNGAL EDLPYDSIVE
     VSSIITSHGP EPINFGKFDP APRGMVQIMK GMEETTISAA VTGNYDKALH AFTINPLVPS
     GKVSKIVLDE MLVAHKKHLP QFKDVIEKLE DK
//
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