ID A0A151YV88_9BACL Unreviewed; 448 AA.
AC A0A151YV88;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE SubName: Full=6-phospho-alpha-glucosidase {ECO:0000313|EMBL:KYQ85637.1};
GN ORFNames=AYX07_12765 {ECO:0000313|EMBL:KYQ85637.1};
OS Thermoactinomyces sp. AS95.
OC Bacteria; Bacillota; Bacilli; Bacillales; Thermoactinomycetaceae;
OC Thermoactinomyces.
OX NCBI_TaxID=1811386 {ECO:0000313|EMBL:KYQ85637.1, ECO:0000313|Proteomes:UP000076382};
RN [1] {ECO:0000313|EMBL:KYQ85637.1, ECO:0000313|Proteomes:UP000076382}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AS95 {ECO:0000313|EMBL:KYQ85637.1,
RC ECO:0000313|Proteomes:UP000076382};
RA Bezuidt O.K., Makhalanyane T.P., Pierneef R., Mohamed G.A., Kharroub K.,
RA Cowan D.A.;
RT "Draft genome sequence of Thermoactinomyces sp. AS95.";
RL Submitted (FEB-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000256|ARBA:ARBA00001936};
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:KYQ85637.1}.
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DR EMBL; LSVF01000009; KYQ85637.1; -; Genomic_DNA.
DR RefSeq; WP_037996264.1; NZ_LSVF01000009.1.
DR AlphaFoldDB; A0A151YV88; -.
DR STRING; 1811386.AYX07_12765; -.
DR OrthoDB; 9808275at2; -.
DR Proteomes; UP000076382; 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 CDD; cd05298; GH4_GlvA_pagL_like; 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; 6-PHOSPHO-BETA-GLUCOSIDASE-RELATED; 1.
DR PANTHER; PTHR32092:SF14; MALTOSE-6'-PHOSPHATE GLUCOSIDASE; 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:UP000076382}.
FT DOMAIN 195..413
FT /note="Glycosyl hydrolase family 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11975"
FT ACT_SITE 170
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT ACT_SITE 261
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 169
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT BINDING 200
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT BINDING 281
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT SITE 109
FT /note="Increases basicity of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ SEQUENCE 448 AA; 50726 MW; 23339AA21FDF99BA CRC64;
MKKFSIVIAG GGSTFTPGIV LMLLENLNQF PIQKLKLYDN DAARQSTIAE ACKIILKEKA
PGIEFLATTD PEAAFTDVDF VMAHIRVGKY AMRELDEKIP LKHGVFGQET CGPGGIAYGM
RSIGGVLELI DYMEKYSPDA WMLNYSNPAA IVAEATRRLR PDSKVLNICD MPIGIENRMA
QILGLKSRKE MKVRYYGLNH FGWWTDIRDQ NGNDLIPKLK EHVRKHGYTV PKDDADASWS
DTFLKARDVY ALDPDTLPNT YLKYYFYPDY VFEHSNPEYT RANEVMEGRE KFVFGECQKI
IENQSTQGSK LHVDEHASYI VDLARAIAFN TQERMLLIVE NQGAISNFDP TAMVEIPCIV
GSNGPERIAI GEIPQFQKGL MEQQVSVEKL VVEAWITRSY QKLWQALTLS KTVPSAKVAK
AILDDLIEAN KDYWPKLHKE DVVVREDL
//
