ID U5SAI8_9LACT Unreviewed; 441 AA.
AC U5SAI8;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE SubName: Full=6-phospho-alpha-glucosidase {ECO:0000313|EMBL:AGY82294.1};
GN ORFNames=Q783_08865 {ECO:0000313|EMBL:AGY82294.1};
OS Carnobacterium inhibens subsp. gilichinskyi.
OC Bacteria; Bacillota; Bacilli; Lactobacillales; Carnobacteriaceae;
OC Carnobacterium.
OX NCBI_TaxID=1266845 {ECO:0000313|EMBL:AGY82294.1, ECO:0000313|Proteomes:UP000017469};
RN [1] {ECO:0000313|EMBL:AGY82294.1, ECO:0000313|Proteomes:UP000017469}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WN1359 {ECO:0000313|EMBL:AGY82294.1,
RC ECO:0000313|Proteomes:UP000017469};
RX PubMed=24285647;
RA Leonard M.T., Panayotova N., Farmerie W.G., Triplett E.W., Nicholson W.L.;
RT "Complete Genome Sequence of Carnobacterium gilichinskyi Strain WN1359T
RT (DSM 27470T).";
RL Genome Announc. 1:e00985-13(2013).
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; CP006812; AGY82294.1; -; Genomic_DNA.
DR RefSeq; WP_023178943.1; NC_022606.1.
DR AlphaFoldDB; U5SAI8; -.
DR STRING; 1266845.Q783_08865; -.
DR KEGG; caw:Q783_08865; -.
DR PATRIC; fig|1266845.5.peg.1665; -.
DR eggNOG; COG1486; Bacteria.
DR HOGENOM; CLU_045951_2_0_9; -.
DR Proteomes; UP000017469; Chromosome.
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..24
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 194..414
FT /note="Glycosyl hydrolase family 4 C-terminal"
FT /evidence="ECO:0000259|Pfam:PF11975"
FT ACT_SITE 170
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT ACT_SITE 264
FT /note="Proton acceptor"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-1"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT BINDING 169
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT BINDING 199
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-3"
FT BINDING 284
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-2"
FT SITE 109
FT /note="Increases basicity of active site Tyr"
FT /evidence="ECO:0000256|PIRSR:PIRSR601088-4"
SQ SEQUENCE 441 AA; 49636 MW; 037F460008FED8A1 CRC64;
MKKFSIVIAG GGSTFTPGIV MMMLDNIDRF PIRTLKLYDN DGERQAILGE ALEILLKEQA
PDIDFSYTTD PETAFTDVDF CMAHIRVGKY AMREQDEKIP LNHGVVGQET CGPGGIAYGM
RSIGGMMEII DYMEKYSPDC WMLNYSNPAA IVAEACRVMR PNAKVLNICD MPVGTLRRMS
QIIDKEPKDL EVRYFGLNHF GWWTSVKDKE GHEYLPQIRE YVAENGYLTK VEVDTQHMDQ
SWQETHKKAK DLLAVNPRYL PNTYLKYYLF PDYEVNHSSC TYSRANEVMD GREKTVFTAA
KKIVEKGTAE NSGFTIDSHA SFIVDLARAI AFNTHERMLM IVENNGAIAN FDDDAMVEVP
CIVGSDGPEP LAQGKIPAFE KALMHQQVTV EKLVVEAYIT GSYQTLWQAL TLSKIIPSAE
VAKNVLDDLI VANKGFWPEL S
//
