ID A0A193KBS9_9VIBR Unreviewed; 437 AA.
AC A0A193KBS9;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 27-MAR-2024, entry version 28.
DE SubName: Full=6-phospho-beta-glucosidase {ECO:0000313|EMBL:ANO32775.1};
GN ORFNames=A6E01_06000 {ECO:0000313|EMBL:ANO32775.1};
OS Vibrio breoganii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=553239 {ECO:0000313|EMBL:ANO32775.1, ECO:0000313|Proteomes:UP000092018};
RN [1] {ECO:0000313|EMBL:ANO32775.1, ECO:0000313|Proteomes:UP000092018}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FF50 {ECO:0000313|EMBL:ANO32775.1,
RC ECO:0000313|Proteomes:UP000092018};
RA Hehemann J.-H., Arevalo P., Datta M.S., Yu X., Corzett C., Henschel A.,
RA Preheim S.P., Timberlake S., Alm E.J., Polz M.F.;
RT "Adaptive Radiation by Waves of Gene Transfer Leads to Fine-Scale Resource
RT Partitioning in Marine Microbes.";
RL Submitted (JUN-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; CP016177; ANO32775.1; -; Genomic_DNA.
DR RefSeq; WP_065209801.1; NZ_MDBA01000032.1.
DR AlphaFoldDB; A0A193KBS9; -.
DR STRING; 553239.A6E01_06000; -.
DR KEGG; vbr:A6E01_06000; -.
DR eggNOG; COG1486; Bacteria.
DR OrthoDB; 9767022at2; -.
DR Proteomes; UP000092018; Chromosome 1.
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; 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 197..412
FT /note="Glycosyl hydrolase family 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11975"
FT BINDING 97
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 151
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 172
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT BINDING 202
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT SITE 113
FT /note="Increases basicity of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ SEQUENCE 437 AA; 48742 MW; 811B9CBFB6123526 CRC64;
MNKNLKITII GAGSSYTPEL IEGLIKRNHE LPIGELWLVD IEDGAEKVRI IGELTRRMLA
KNGMSHINVH VSLDRKPALK DADFVCSQFR AGCLEGRIRD ERIALKYGMI GQETNGLGGF
ANACRTIPIA LEICSEMEEL CPDAWLLNFT NPSGMVTEAI LKHTKVKAVG LCNVPVIMQK
GIAQILGADE QDFVLQVAGL NHFIWARQVL HNGQDKLQDV VDAMLSGNDP LVPQNIPKFE
WPPELLRNMG MIPCAYLRYY YTSEDIMEQE QQEASGEGTR GEVVKAMERR LFDIYQNPEL
NEKPKELEKR GGQYYSEAAC ELMSSIYNDK RTIMHVNTRN NGTIQGLPDD CTVEVSSMIT
KSGPVPLSVA PFPSDTLRLI QVLKEFESLT VEAAVTGNRN AAHRALILNP LVTTGSILEK
ALEETIQANL DYMPQFR
//
