ID A0A1F8M8E0_9CHLR Unreviewed; 460 AA.
AC A0A1F8M8E0;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 18.
DE SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:OGN94891.1};
GN ORFNames=A2Z71_06250 {ECO:0000313|EMBL:OGN94891.1};
OS Chloroflexi bacterium RBG_13_50_21.
OC Bacteria; Chloroflexota.
OX NCBI_TaxID=1797623 {ECO:0000313|EMBL:OGN94891.1, ECO:0000313|Proteomes:UP000177581};
RN [1] {ECO:0000313|EMBL:OGN94891.1, ECO:0000313|Proteomes:UP000177581}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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 -!- 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:OGN94891.1}.
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DR EMBL; MGMQ01000098; OGN94891.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F8M8E0; -.
DR STRING; 1797623.A2Z71_06250; -.
DR Proteomes; UP000177581; Unassembled WGS sequence.
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 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}.
FT DOMAIN 190..435
FT /note="Glycosyl hydrolase family 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11975"
FT ACT_SITE 166
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT ACT_SITE 243
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 144
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 165
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT BINDING 195
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT SITE 106
FT /note="Increases basicity of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ SEQUENCE 460 AA; 50851 MW; F3C9726E9F226B66 CRC64;
MKLSVIGGCG VRAPRLVSSA LHRQIQTGLT ELWLMDIDET RLRLIGGLCQ KLAILAESPV
RIFCTQDARA ALDGADYIVT TIRVGGEYGR VLDEKIALRQ GVLGQETTGA GGFAMAMRSI
PTLLEYAGLA EKYAPHAWLF NFTNPAGLVT QAMHKRGFVR SVGICDSANL AQHDVARWFG
IPPAQVHAEV FGLNHLSWAR SLRVDGRDVL PELLANPSFC AESSQRIFDT ALLERIGLFL
NEYLYYYYYA EQALSQIQQD SKTRGEEILE LNQALLRKLN SVSYKDDPQA AIRAYFTYER
RRSSTYMHYA MPGGLSLEQA DRMVSEEFKG IPEEDEGYAG MTLDIIAALQ TGNPLRTALN
IPNQGAISGM AADDIVEVSA RISGKEISPI HMGSIPSLPA SLMQTVKQYE RLAVDAILNR
SIRLAVQALM SHPLVLSFPR ATRLVEEYLK AHAAFVGEWN
//
