ID A0A071MA04_9ENTR Unreviewed; 435 AA.
AC A0A071MA04;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=6-phospho-alpha-glucosidase {ECO:0000313|EMBL:KEA53361.1};
GN ORFNames=DT73_08355 {ECO:0000313|EMBL:KEA53361.1};
OS Mangrovibacter sp. MFB070.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Mangrovibacter.
OX NCBI_TaxID=1224318 {ECO:0000313|EMBL:KEA53361.1, ECO:0000313|Proteomes:UP000027726};
RN [1] {ECO:0000313|EMBL:KEA53361.1, ECO:0000313|Proteomes:UP000027726}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MFB070 {ECO:0000313|EMBL:KEA53361.1,
RC ECO:0000313|Proteomes:UP000027726};
RA Joseph T.C., Varghese A.M., Baby A., Reghunathan D., V M., Lalitha K.V.;
RT "Draft Genome Sequence of Mangrovibacter spp. MFB070 a Nitrogen-fixing
RT Bacterium Isolated from an Aquaculture Farm.";
RL Submitted (APR-2014) 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:KEA53361.1}.
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DR EMBL; JJMI01000019; KEA53361.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A071MA04; -.
DR eggNOG; COG1486; Bacteria.
DR Proteomes; UP000027726; 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; 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 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:UP000027726}.
FT DOMAIN 190..410
FT /note="Glycosyl hydrolase family 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11975"
FT ACT_SITE 165
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT ACT_SITE 258
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT BINDING 88
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 142
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 195
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT BINDING 278
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT SITE 104
FT /note="Increases basicity of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ SEQUENCE 435 AA; 48337 MW; BDF4BE0C17C646FA CRC64;
MVIAGGGSTF TPGIVLMLLA NQDRFPLRAL KFYDNDGARQ EVIAEACKVI LQEQAPDIAF
SYTTDPKEAF TDVDFVMAHI RVGKYPMREQ DEKIPLRHGV LGQETCGPGG IAYGMRSIGG
VLELVDYMEQ YSPNAWMLNY SNPAAIVAEA TRRLRPNAKI LNICDMPIGI EGRMAQIVGL
KDRKQMRVRY YGLNHFGWWT QIEDLAGNDL MPQLKAYVAQ HGYVPPAKDT HTEASWNDTF
AKAKDVQALD SATLPNTYLK YYLFPDYVVA HSNPERTRAN EVMDHREKQV FGACRAIIEA
GNSSAGELEI DEHASYIVDL AAAIAFNTQE RMLLIVPNNG AIANFDADAM VEIPCLVGKN
GPEPLTVGEI PHFQKGMMGQ QVAVEKLVVD AWEQHSYQKL WQAITLSKTV PSATVAKAIL
DDLIEANKAY WPELN
//
