PAGL1_LACP3
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 03-AUG-2022, entry version 94.
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; Firmicutes; 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 / NRRL
RC 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 EnsemblBacteria; ABJ69228; ABJ69228; LSEI_0369.
DR KEGG; lca:LSEI_0369; -.
DR PATRIC; fig|321967.11.peg.390; -.
DR HOGENOM; CLU_045951_2_0_9; -.
DR OMA; METYSPD; -.
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 Gene3D; 3.90.110.10; -; 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; PTHR32092; 1.
DR Pfam; PF02056; Glyco_hydro_4; 1.
DR Pfam; PF11975; Glyco_hydro_4C; 1.
DR PRINTS; PR00732; GLHYDRLASE4.
DR SUPFAM; SSF51735; SSF51735; 1.
DR SUPFAM; SSF56327; SSF56327; 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.
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
