ID A0A1H9E0D8_9LACT Unreviewed; 448 AA.
AC A0A1H9E0D8;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
DE SubName: Full=Maltose-6-phosphate glucosidase {ECO:0000313|EMBL:SEQ18653.1};
GN ORFNames=SAMN04488558_10646 {ECO:0000313|EMBL:SEQ18653.1};
OS Ignavigranum ruoffiae.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Aerococcaceae; Ignavigranum.
OX NCBI_TaxID=89093 {ECO:0000313|EMBL:SEQ18653.1, ECO:0000313|Proteomes:UP000198833};
RN [1] {ECO:0000313|EMBL:SEQ18653.1, ECO:0000313|Proteomes:UP000198833}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 15695 {ECO:0000313|EMBL:SEQ18653.1,
RC ECO:0000313|Proteomes:UP000198833};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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}.
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DR EMBL; FOEN01000006; SEQ18653.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H9E0D8; -.
DR STRING; 89093.SAMN04488558_10646; -.
DR OrthoDB; 9808275at2; -.
DR Proteomes; UP000198833; 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:UP000198833}.
FT DOMAIN 198..423
FT /note="Glycosyl hydrolase family 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11975"
FT ACT_SITE 173
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT ACT_SITE 271
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 150
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 203
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT BINDING 291
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT SITE 112
FT /note="Increases basicity of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ SEQUENCE 448 AA; 50818 MW; FEA16E7E719AAF7E CRC64;
MQKLKEQSIL VAGGGSTFTP GIVLMLLDNL DTFPIRQIKF YDNNEERQEK VAKACEILIK
ERAPQIKFAY TTDPETAFTD VDFVMAHIRV GLYAMREKDE KIPLKYGVIG QETCGPGGIA
YGMRSIGGVL ELIDYMEKYS PNAWMLNYSN PAAIVAEATR KLKPNSKIIN ICDMPVGIEH
RMAEILGLDS RKDFVVRYYG LNHYGWWTDI RDHDGNDLMP KLIEHVSQYG YITPSEISNH
GNENVEESWM HTFGKAKDVQ ALDPTTLPNT YLKYYLFSQD EVEIADPNYT RANEVMDHRE
KIVFQECNKV VKAGTAKGQN LEADDHASYI VDLARAIAYN TRERMLLIVP NNGSINNFDS
TAMVEIPCIV TSNGPEPLVM GEIPRFQKGM MEQQVAVEKL VVEAWEEGSY QKLWQAITLS
KTVPNARIAK QILDDLIEAN KDFWPELK
//
