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
//