ID A0A1I1C4D0_9PSEU Unreviewed; 426 AA.
AC A0A1I1C4D0;
DT 05-DEC-2018, integrated into UniProtKB/TrEMBL.
DT 05-DEC-2018, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:SFB57504.1};
GN ORFNames=SAMN05216266_12115 {ECO:0000313|EMBL:SFB57504.1};
OS Amycolatopsis marina.
OC Bacteria; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC Pseudonocardiaceae; Amycolatopsis.
OX NCBI_TaxID=490629 {ECO:0000313|EMBL:SFB57504.1, ECO:0000313|Proteomes:UP000243799};
RN [1] {ECO:0000313|Proteomes:UP000243799}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 4.3568 {ECO:0000313|Proteomes:UP000243799};
RA Varghese N., Submissions S.;
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; FOKG01000021; SFB57504.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I1C4D0; -.
DR STRING; 490629.SAMN05216266_12115; -.
DR OrthoDB; 9767022at2; -.
DR Proteomes; UP000243799; 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; 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; 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.
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:UP000243799}.
FT DOMAIN 191..399
FT /note="Glycosyl hydrolase family 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11975"
FT BINDING 90
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 145
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 426 AA; 45576 MW; 90994821AD004AAD CRC64;
MRLTVVGGGS TYTPELVDGI CARRSTLDVE ELVLVDPDER RLEIVGDFSR RLLARAGHPA
LVHTTTSVAE GAEGASAVLL QLRVGGQRAR RSDETFPHAC GCVGQETTGA GGLAKALRTV
PVVLDIADRV REVAGPDAWL VDFTNPVGIV TRALLEAGHR AVGLCNVAIG LQRLSARLLG
VDSASVRLDH VGLNHLSWER RVLVADAHGE TDRLPELLAA HGPELAEHVG APCDWLRRTG
MLPSYYLKYF YAHDEAVRAQ LTERPRADVV SEVEAELLAC YADPALERTP ELLASRGGAY
YSEAAIELVR ALIGAGSAGE HVVNVRNEGT LPFLPDDAVI ETACAVDSSG VRPLPQRPVE
PLLRGLIAQV SAYEHLALDA ALRGGRDRVA DALLAHPLVG QYALADRLAD DLVAANRAVL
PWVRKG
//
