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Entry: M8CYV2_THETY
LinkDB: M8CYV2_THETY
Original site: M8CYV2_THETY 
ID   M8CYV2_THETY            Unreviewed;       436 AA.
AC   M8CYV2;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   24-JAN-2024, entry version 33.
DE   SubName: Full=Alpha-galactosidase/6-phospho-beta-glucosidase, family 4 of glycosyl hydrolases {ECO:0000313|EMBL:EMT39493.1};
DE            EC=3.2.1.86 {ECO:0000313|EMBL:EMT39493.1};
GN   ORFNames=TthWC1_0923 {ECO:0000313|EMBL:EMT39493.1};
OS   Thermoanaerobacter thermohydrosulfuricus WC1.
OC   Bacteria; Bacillota; Clostridia; Thermoanaerobacterales;
OC   Thermoanaerobacteraceae; Thermoanaerobacter.
OX   NCBI_TaxID=1198630 {ECO:0000313|EMBL:EMT39493.1, ECO:0000313|Proteomes:UP000013242};
RN   [1] {ECO:0000313|EMBL:EMT39493.1, ECO:0000313|Proteomes:UP000013242}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WC1 {ECO:0000313|EMBL:EMT39493.1,
RC   ECO:0000313|Proteomes:UP000013242};
RX   PubMed=23555660;
RA   Verbeke T.J., Zhang X., Henrissat B., Spicer V., Rydzak T., Krokhin O.V.,
RA   Fristensky B., Levin D.B., Sparling R.;
RT   "Genomic Evaluation of Thermoanaerobacter spp. for the Construction of
RT   Designer Co-Cultures to Improve Lignocellulosic Biofuel Production.";
RL   PLoS ONE 8:E59362-E59362(2013).
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:EMT39493.1}.
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DR   EMBL; AMYG01000027; EMT39493.1; -; Genomic_DNA.
DR   RefSeq; WP_004399748.1; NZ_KB731281.1.
DR   AlphaFoldDB; M8CYV2; -.
DR   PATRIC; fig|1198630.3.peg.944; -.
DR   HOGENOM; CLU_045951_0_1_9; -.
DR   Proteomes; UP000013242; 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|ARBA:ARBA00022723,
KW   ECO:0000256|PIRSR:PIRSR601088-3};
KW   NAD {ECO:0000256|ARBA:ARBA00023027, ECO:0000256|RuleBase:RU361152};
KW   Nickel {ECO:0000256|PIRSR:PIRSR601088-3}.
FT   DOMAIN          197..411
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         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            113
FT                   /note="Increases basicity of active site Tyr"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ   SEQUENCE   436 AA;  48701 MW;  1BEB080DA0ACFC57 CRC64;
     MFKKNLKIAV IGGGSSYTPE LIEGFIKRYN ELPVKDLYLV DIEEGKEKLE IVGGLAKRMV
     EKAGVGINIH LTLDRREAIK DADFVVTQFR VGGMDARIRD EKIPLKYDVI GQETTGPGGF
     AKAQRTIPVI LDICKDVEEL APNAWLINFT NPSGVITETI LKYTNVKAIG LCNVPIGMVY
     GVAKMLEVDP KRVYIDFAGL NHLVWGTHIY LDGEDITEKL IDSFAGGKSL SMKNIPELPW
     DPDFIKSLGM YPCPYHRYYY LTDKMLEKQK EEAATVGTRG EVVKKLEQEL FELYKDPNLN
     IKPPQLEKRG GAYYSDAACS LICSIYNDKK DIHVVNVRNN GTIADLPDDV VIETNAIIDR
     NGAHPINIGH VPAKIRGLMQ AVKAYEELTI EAGVKGDYYT ALQALTIHPL IPSATVAKKI
     LDDILEQNKE YLPQYK
//
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