ID A0A1I6XUW5_9MICC Unreviewed; 470 AA.
AC A0A1I6XUW5;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 19.
DE SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:SFT41614.1};
GN ORFNames=SAMN04487915_101279 {ECO:0000313|EMBL:SFT41614.1};
OS Arthrobacter sp. ov118.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1761747 {ECO:0000313|EMBL:SFT41614.1, ECO:0000313|Proteomes:UP000199457};
RN [1] {ECO:0000313|EMBL:SFT41614.1, ECO:0000313|Proteomes:UP000199457}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=OV118 {ECO:0000313|EMBL:SFT41614.1,
RC ECO:0000313|Proteomes:UP000199457};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family.
CC {ECO:0000256|ARBA:ARBA00010141, ECO:0000256|RuleBase:RU361152}.
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DR EMBL; FPAY01000001; SFT41614.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I6XUW5; -.
DR STRING; 1761747.SAMN04487915_101279; -.
DR OrthoDB; 9767022at2; -.
DR Proteomes; UP000199457; 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 195..442
FT /note="Glycosyl hydrolase family 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11975"
FT ACT_SITE 168
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT ACT_SITE 249
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT BINDING 92
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 146
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 167
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 SITE 108
FT /note="Increases basicity of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ SEQUENCE 470 AA; 48813 MW; 3A0E2E8965871572 CRC64;
MRLTIVGGGG FRVPLIYRAL AAGPFAGLVR ELVLYDVDAG RLAAIEAVLA SLALQDPPGP
GPRVRAVSAL SEALEGADMV FAAIRPGGTA GRIADERIAL DLGLLGQETT GAGGISYALR
SIPPMLALAA DMRSRCPGAW LLNFTNPAGI VTEALVPVLG QRVIGICDSA GGLVHRAARA
AGAALPEGRL DGVGYYGLNH LGWLYRLQSE GRDALPELLA DPAALAEFEE GRLFPPALLA
GLGCLPNEYL FYYYETERAL AGMRGAGLTR GESIARQQAE LYPRLAAAGP QAFALWEAAR
RSREEGYLAE ARGAGEHRDE TDLAGGGYER VALAAMRALS GGGPADLILN TVNTLPGPDG
NADGNTTGSP APAIPGLPAD AVVEIPCRVT TDGAVPLPQD PPGPAQLGLM RRVKDVERLV
VEAVTTGSRD AALAAFARHP LVDSEVLAGK LLAGYEAAFP GLGHLWRGRP
//
