PAGL2_LACP3
ID PAGL2_LACP3 Reviewed; 461 AA.
AC Q034G9;
DT 24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT 14-NOV-2006, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=6-phospho-alpha-glucosidase 2;
DE EC=3.2.1.122;
GN OrderedLocusNames=LSEI_2684;
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 IDENTIFICATION.
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 -!- 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 -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC Note=Binds 1 divalent metal ion per subunit. Mn(2+). {ECO:0000250};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540; Evidence={ECO:0000250};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000250};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP000423; ABJ71403.1; -; Genomic_DNA.
DR RefSeq; WP_011674973.1; NC_008526.1.
DR RefSeq; YP_807845.1; NC_008526.1.
DR AlphaFoldDB; Q034G9; -.
DR SMR; Q034G9; -.
DR STRING; 321967.LSEI_2684; -.
DR CAZy; GH4; Glycoside Hydrolase Family 4.
DR EnsemblBacteria; ABJ71403; ABJ71403; LSEI_2684.
DR KEGG; lca:LSEI_2684; -.
DR PATRIC; fig|321967.11.peg.2628; -.
DR HOGENOM; CLU_045951_2_0_9; -.
DR OMA; KYPMREK; -.
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 3: Inferred from homology;
KW Carbohydrate metabolism; Glycosidase; Hydrolase; Manganese; Metal-binding;
KW NAD.
FT CHAIN 1..461
FT /note="6-phospho-alpha-glucosidase 2"
FT /id="PRO_0000389205"
FT ACT_SITE 173
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 267
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 7..73
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 150
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 172
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 287
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 112
FT /note="Increases basicity of active site Tyr"
FT /evidence="ECO:0000250"
SQ SEQUENCE 461 AA; 52030 MW; F96D99955DA75E84 CRC64;
MNQNKQFSIV IAGGGSTYTA GIVMMLLENA ERFPLRALKL YDIDEERQAT IAEAIAIELK
EKAPAIDFTW TTDPQTAFTD VDFCFAHIRS GGYKMREQDE KIPLKHHVVG QETCGPGGIA
YGMRSIGDII ELIDFIEKYS PDCWMLNYSN PASIVAEACR RLRPDAKILN ICDMPVGTQR
RMSQIIGLQP KDLEVRYFGM NHFGWWTSVK DKAGNEYLPQ IRDYVAHHGY LTQIEVDTQH
MDASWQATHK KAQDLLAVDP HYLPNTYLKY YLYPDYVVAH SDPDYTRANE VEDGREKCVF
SAAQKIIDAG TSDVGSFPID SHASFIVDLA CAIAFNTHER MLLIVENNGA VANIDDNIMV
EVPCIVGKDG AEPLTQGKIP MFQRGMILNQ AMVEKLVVDA WINHDYQELW QALTLSKTLP
SAQVAKEVLD DLIEANREYW PELKHDEHEV HLISESAVSE I
