ID A0A2S3ZSJ0_ARTGL Unreviewed; 431 AA.
AC A0A2S3ZSJ0;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:POH72221.1};
GN ORFNames=CVS27_17175 {ECO:0000313|EMBL:POH72221.1};
OS Arthrobacter glacialis.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Micrococcaceae;
OC Arthrobacter.
OX NCBI_TaxID=1664 {ECO:0000313|EMBL:POH72221.1, ECO:0000313|Proteomes:UP000237061};
RN [1] {ECO:0000313|EMBL:POH72221.1, ECO:0000313|Proteomes:UP000237061}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HLT2-12-2 {ECO:0000313|EMBL:POH72221.1,
RC ECO:0000313|Proteomes:UP000237061};
RA Liu Q., Xin Y.-H.;
RT "Arthrobacter sp. nov., from glaciers in China.";
RL Submitted (JAN-2018) 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}.
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:POH72221.1}.
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DR EMBL; PPXC01000016; POH72221.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2S3ZSJ0; -.
DR Proteomes; UP000237061; 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:UP000237061}.
FT DOMAIN 190..406
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 144
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 164
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT BINDING 194
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 431 AA; 46764 MW; CE616EAF9613703C CRC64;
MKIVVVGGGS TYTPELIDGF ARLRETLPLS EIVLVDPDRE RRELLAGVAQ RMLLRQGHPA
LVTSTDDVGA ASEGAVAVLL QLRVGGQDTR RRDETWPLDC DCIGQETTGA GGLAKALRTV
PVVLDIAERV RAVNPDAWLI DFTNPVGIVS RALLSHGHKA IGLCNVAIGL QRFFAELVGV
GPERIALDHV GLNHLTWERG VRLLDPVTIG GTTPVGSGTN ILPRLLESHA ERIATRLHQP
VQLLQRIQAV PSYYLRYFYE HDTVVREQRK GPSRAEEVAA MESELLRMYA DPATDTKPDL
LSKRGGEFYS EAAVNLVASL LSDRGDTQVV NTLNNGTLPF LPDDFVIETP AIIDSTGAHP
VRTSAVEPRF AGLIAHVAAY EQLALDAAIH GGRDRVADAL LAHPLVGQWD IANTLTDRLI
AENSAFLSWA K
//
