ID   PAGL1_LACP3             Reviewed;         442 AA.
AC   Q03C44;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2006, sequence version 1.
DT   27-MAR-2024, entry version 100.
DE   RecName: Full=6-phospho-alpha-glucosidase 1;
DE            EC=3.2.1.122;
GN   Name=simA; OrderedLocusNames=LSEI_0369;
OS   Lacticaseibacillus paracasei (strain ATCC 334 / BCRC 17002 / CCUG 31169 /
OS   CIP 107868 / KCTC 3260 / NRRL B-441) (Lactobacillus paracasei).
OC   Bacteria; Bacillota; Bacilli; Lactobacillales; Lactobacillaceae;
OC   Lacticaseibacillus.
OX   NCBI_TaxID=321967;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 334 / BCRC 17002 / CCUG 31169 / CIP 107868 / KCTC 3260 /
RC   NRRL B-441;
RX   PubMed=17030793; DOI=10.1073/pnas.0607117103;
RA   Makarova K.S., Slesarev A., Wolf Y.I., Sorokin A., Mirkin B., Koonin E.V.,
RA   Pavlov A., Pavlova N., Karamychev V., Polouchine N., Shakhova V.,
RA   Grigoriev I., Lou Y., Rohksar D., Lucas S., Huang K., Goodstein D.M.,
RA   Hawkins T., Plengvidhya V., Welker D., Hughes J., Goh Y., Benson A.,
RA   Baldwin K., Lee J.-H., Diaz-Muniz I., Dosti B., Smeianov V., Wechter W.,
RA   Barabote R., Lorca G., Altermann E., Barrangou R., Ganesan B., Xie Y.,
RA   Rawsthorne H., Tamir D., Parker C., Breidt F., Broadbent J.R., Hutkins R.,
RA   O'Sullivan D., Steele J., Unlu G., Saier M.H. Jr., Klaenhammer T.,
RA   Richardson P., Kozyavkin S., Weimer B.C., Mills D.A.;
RT   "Comparative genomics of the lactic acid bacteria.";
RL   Proc. Natl. Acad. Sci. U.S.A. 103:15611-15616(2006).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-30, IDENTIFICATION BY MASS SPECTROMETRY, CATALYTIC
RP   ACTIVITY, FUNCTION, SUBUNIT, ACTIVITY REGULATION, SUBSTRATE SPECIFICITY,
RP   COFACTOR, CATALYTIC MECHANISM, AND INDUCTION.
RX   PubMed=18310337; DOI=10.1128/jb.02008-07;
RA   Thompson J., Jakubovics N., Abraham B., Hess S., Pikis A.;
RT   "The sim operon facilitates the transport and metabolism of sucrose isomers
RT   in Lactobacillus casei ATCC 334.";
RL   J. Bacteriol. 190:3362-3373(2008).
CC   -!- FUNCTION: Is probably involved in the catabolism of alpha-glycosides
CC       accumulated via a phosphoenolpyruvate-dependent phosphotransferase
CC       system (PEP-PTS). Hydrolyzes a wide variety of 6-phospho-alpha-D-
CC       glucosides including the five isomeric derivatives of sucrose, i.e.
CC       trehalulose-6'-phosphate, turanose-6'-phosphate, maltulose-6'-
CC       phosphate, leucrose-6'-phosphate, and palatinose-6'-phosphate, but is
CC       not active on sucrose-6-phosphate. Can also hydrolyze maltose-6'-
CC       phosphate and methyl-alpha-glucose-6-phosphate, and poorly, trehalose-
CC       6-phosphate. Fails to hydrolyze beta-O-linked phosphorylated
CC       disaccharides such as cellobiose-6'-phosphate and gentiobiose-6'-
CC       phosphate. Does not seem to be involved in maltose catabolism.
CC       {ECO:0000269|PubMed:18310337}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=alpha-maltose 6'-phosphate + H2O = D-glucose + D-glucose 6-
CC         phosphate; Xref=Rhea:RHEA:20421, ChEBI:CHEBI:4167, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:57478, ChEBI:CHEBI:61548; EC=3.2.1.122;
CC         Evidence={ECO:0000269|PubMed:18310337};
CC   -!- COFACTOR:
CC       Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC         Evidence={ECO:0000269|PubMed:18310337};
CC       Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC         Evidence={ECO:0000269|PubMed:18310337};
CC       Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC         Evidence={ECO:0000269|PubMed:18310337};
CC       Name=Fe(2+); Xref=ChEBI:CHEBI:29033;
CC         Evidence={ECO:0000269|PubMed:18310337};
CC       Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC         Evidence={ECO:0000269|PubMed:18310337};
CC       Note=Binds 1 divalent metal ion per subunit. Mn(2+) is the most
CC       efficient metal, but can also use Co(2+), Ni(2+) and Fe(2+), and to a
CC       lesser extent Mg(2+). Cannot use Zn(2+). {ECO:0000269|PubMed:18310337};
CC   -!- COFACTOR:
CC       Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC         Evidence={ECO:0000269|PubMed:18310337};
CC       Note=Binds 1 NAD(+) per subunit. {ECO:0000269|PubMed:18310337};
CC   -!- ACTIVITY REGULATION: Is inhibited by EDTA in vitro.
CC       {ECO:0000269|PubMed:18310337}.
CC   -!- SUBUNIT: Homodimer. May also form homotetramer.
CC       {ECO:0000269|PubMed:18310337}.
CC   -!- INDUCTION: By maltulose, leucrose and palatinose, but not by maltose,
CC       glucose or sucrose. {ECO:0000269|PubMed:18310337}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family. {ECO:0000305}.
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DR   EMBL; CP000423; ABJ69228.1; -; Genomic_DNA.
DR   RefSeq; WP_011674086.1; NC_008526.1.
DR   RefSeq; YP_805670.1; NC_008526.1.
DR   AlphaFoldDB; Q03C44; -.
DR   SMR; Q03C44; -.
DR   STRING; 321967.LSEI_0369; -.
DR   CAZy; GH4; Glycoside Hydrolase Family 4.
DR   PaxDb; 321967-LSEI_0369; -.
DR   KEGG; lca:LSEI_0369; -.
DR   PATRIC; fig|321967.11.peg.390; -.
DR   HOGENOM; CLU_045951_2_0_9; -.
DR   Proteomes; UP000001651; Chromosome.
DR   GO; GO:0050081; F:maltose-6'-phosphate glucosidase activity; IEA:UniProtKB-EC.
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:UniProtKB-KW.
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   1: Evidence at protein level;
KW   Carbohydrate metabolism; Cobalt; Direct protein sequencing; Glycosidase;
KW   Hydrolase; Iron; Manganese; Metal-binding; NAD; Nickel; Reference proteome.
FT   CHAIN           1..442
FT                   /note="6-phospho-alpha-glucosidase 1"
FT                   /id="PRO_0000389204"
FT   ACT_SITE        172
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000305"
FT   ACT_SITE        265
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000305"
FT   BINDING         6..72
FT                   /ligand="NAD(+)"
FT                   /ligand_id="ChEBI:CHEBI:57540"
FT                   /evidence="ECO:0000250"
FT   BINDING         95
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         149
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         171
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         202
FT                   /ligand="Mn(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29035"
FT                   /evidence="ECO:0000250"
FT   BINDING         285
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   SITE            111
FT                   /note="Increases basicity of active site Tyr"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   442 AA;  49842 MW;  AE4D60737BACD491 CRC64;
     MDDRKFSVLI AGGGSTYTPG IVLTLLDHIQ KFPLRKLKFY DIDGERQQRV ADACEILVKE
     RAPEVEFLAT TDPEEAFTDV DFVMAQIRVG KYAMRSLDEK IPLKHGVVGQ ETTGPGGIAY
     GLRSIPGVIG LVDYMEKYSP NAWMLNYSNP AAIVAEATRR LRPHSRIINI CDMPIGIMDR
     MAQIVGLKDR NDLVFRYYGL NHFGWWTDVR DKTGKDLMPA LKQYVAKNGY WLGDKDKDTE
     ASWVSTFKKA ADVYALDPST LPNTYLKYYL YPKYVVEHSD PNYTRTDEVE AYREKHVFDE
     CDRIIAAGTA ADTHFKSDDH ATYIVDLCTA IAYDTKQRML AIVPNDGAIE NIDPEAMVEV
     PCLFGANGAE RLAMGKAATF QKGLITEQNC VEKLTVDAFE QQSYTKLWEA MSLCKIVPDA
     SVAKEILDEM VVANKDYWPE LK
//