ID A0A1Q9HDX0_9VIBR Unreviewed; 445 AA.
AC A0A1Q9HDX0;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=6-phospho-alpha-glucosidase {ECO:0000313|EMBL:OLQ87908.1};
GN ORFNames=BIY22_06945 {ECO:0000313|EMBL:OLQ87908.1}, F7O85_18940
GN {ECO:0000313|EMBL:KAB1454925.1};
OS Vibrio panuliri.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=1381081 {ECO:0000313|EMBL:OLQ87908.1, ECO:0000313|Proteomes:UP000186313};
RN [1] {ECO:0000313|EMBL:OLQ87908.1, ECO:0000313|Proteomes:UP000186313}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CAIM 703 {ECO:0000313|EMBL:OLQ87908.1,
RC ECO:0000313|Proteomes:UP000186313};
RA Gonzalez-Castillo A., Gomez-Gil B., Enciso-Ibarra K.;
RT "Genomic Taxonomy of the Vibrionaceae.";
RL Submitted (SEP-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KAB1454925.1, ECO:0000313|Proteomes:UP000446972}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LBS 2 {ECO:0000313|EMBL:KAB1454925.1,
RC ECO:0000313|Proteomes:UP000446972};
RA Das S.S.;
RT "Whole genome sequence of Vibrio panuliri LBS 2.";
RL Submitted (SEP-2019) 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:OLQ87908.1}.
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DR EMBL; WAHU01000009; KAB1454925.1; -; Genomic_DNA.
DR EMBL; MJMJ01000023; OLQ87908.1; -; Genomic_DNA.
DR RefSeq; WP_075709080.1; NZ_WAHU01000009.1.
DR AlphaFoldDB; A0A1Q9HDX0; -.
DR STRING; 1381081.BIY22_06945; -.
DR OrthoDB; 9767022at2; -.
DR Proteomes; UP000186313; Unassembled WGS sequence.
DR Proteomes; UP000446972; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
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 Membrane {ECO:0000256|SAM:Phobius};
KW Metal-binding {ECO:0000256|PIRSR:PIRSR601088-3};
KW NAD {ECO:0000256|RuleBase:RU361152};
KW Nickel {ECO:0000256|PIRSR:PIRSR601088-3};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 6..25
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 196..418
FT /note="Glycosyl hydrolase family 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11975"
FT ACT_SITE 171
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT ACT_SITE 268
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 148
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 170
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT BINDING 201
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT BINDING 288
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT SITE 110
FT /note="Increases basicity of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ SEQUENCE 445 AA; 50517 MW; FA0489A4E7E7C71B CRC64;
MKKEFSVVIA GGGSTFTPGI VMMLLENQDR FPIRKLKFYD NFAARQETVA EACKILLQER
APHIEFSYTT DPEEAFTDID FCMAHIRAGL YAMREQDEKI PLRHGCVGQE TCGAGGMAYG
LRSIPAVIEM IDYMEKYSPN AWMLNYSNPA AIVAEACRVM RPNSKVLNIC DMPIGIETRI
AEILGYQDRK QFDIMYYGLN HFGWWKEFKD AKTGEDLMPR IKEYIQEFGY LPPSAMNGSQ
HTDESWKETF IKVRDVYALD PETIPNTYLK YYMYPDYVVE HSNKEFTRAN EVMEGREKEV
FTECRRIIAA GTAVDTTIEV EEHASYIVDL ATAIAFNTKE RMLLIVPNNG AISNFDPTAM
VEIPCIVDNT GAKPLQIGEI PEFQKGMMSQ QVSVEKLVVQ AHVEGSKQRL WQALTLSATI
PSATVAKAIL DDLLEANKEF WVEMK
//
