PAGL_CLOAB
ID PAGL_CLOAB Reviewed; 445 AA.
AC Q97DP6;
DT 15-FEB-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 96.
DE RecName: Full=Phospho-alpha-glucosidase PagL;
DE EC=3.2.1.-;
GN Name=pagL; OrderedLocusNames=CA_C3426;
OS Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS / VKM B-1787).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=272562;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA Smith D.R.;
RT "Genome sequence and comparative analysis of the solvent-producing
RT bacterium Clostridium acetobutylicum.";
RL J. Bacteriol. 183:4823-4838(2001).
RN [2]
RP PROTEIN SEQUENCE OF 1-29, CHARACTERIZATION, AND KINETIC PARAMETERS.
RC STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX PubMed=14570887; DOI=10.1074/jbc.m310733200;
RA Thompson J., Hess S., Pikis A.;
RT "Genes malh and pagl of Clostridium acetobutylicum ATCC 824 encode
RT NAD+- and Mn2+-dependent phospho-alpha-glucosidase(s).";
RL J. Biol. Chem. 279:1553-1561(2004).
CC -!- FUNCTION: Phospho-alpha-glucosidase that catalyzes the hydrolysis of p-
CC nitrophenyl-alpha-D-glucopyranoside 6-phosphate, but is not able to
CC cleave 'natural' phospho-alpha-glucosides produced via the
CC phosphoenolpyruvate-dependent sugar phosphotransferase system (PEP-
CC PTS).
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Note=Binds 1 NAD(+) per subunit.;
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Note=Binds 1 Mn(2+) ion per subunit.;
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=58.3 uM for p-nitrophenyl-alpha-D-glucopyranoside 6-phosphate
CC {ECO:0000269|PubMed:14570887};
CC Vmax=4.4 umol/min/mg enzyme with p-nitrophenyl 6-phospho-alpha-D-
CC glucoside as substrate {ECO:0000269|PubMed:14570887};
CC -!- SUBUNIT: Homotetramer.
CC -!- INDUCTION: By maltose and methyl-alpha-D-glucoside.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family. {ECO:0000305}.
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DR EMBL; AE001437; AAK81356.1; -; Genomic_DNA.
DR PIR; A97321; A97321.
DR RefSeq; NP_350016.1; NC_003030.1.
DR RefSeq; WP_010966696.1; NC_003030.1.
DR AlphaFoldDB; Q97DP6; -.
DR SMR; Q97DP6; -.
DR STRING; 272562.CA_C3426; -.
DR CAZy; GH4; Glycoside Hydrolase Family 4.
DR EnsemblBacteria; AAK81356; AAK81356; CA_C3426.
DR GeneID; 44999921; -.
DR KEGG; cac:CA_C3426; -.
DR PATRIC; fig|272562.8.peg.3608; -.
DR eggNOG; COG1486; Bacteria.
DR HOGENOM; CLU_045951_2_0_9; -.
DR OMA; IEANEDY; -.
DR OrthoDB; 277080at2; -.
DR SABIO-RK; Q97DP6; -.
DR Proteomes; UP000000814; Chromosome.
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 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 Direct protein sequencing; Glycosidase; Hydrolase; Manganese;
KW Metal-binding; NAD; Reference proteome.
FT CHAIN 1..445
FT /note="Phospho-alpha-glucosidase PagL"
FT /id="PRO_0000169865"
FT ACT_SITE 172
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 264
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 4..71
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 148
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 201
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 110
FT /note="Increases basicity of active site Tyr"
FT /evidence="ECO:0000250"
SQ SEQUENCE 445 AA; 51156 MW; 49FA5F7EE968BF39 CRC64;
MKKYSICIVG GGSRYTPDML AMLCNQKERF PLRKIVLYDN ESERQETVGN YAKILFKEYY
PELEEVIWTT DEKEAFEDID FALMQIRAGR LKMREKDEKI SLKHGCLGQE TCGAGGFAYG
LRSVPAVIDL IKSIRTYSPK CWILNYSNPA AIVAEATKRV FPNDYRIINI CDMPIAIMDI
YAAVLGLKRR DLEPKYFGLN HFGWFTHILD KKTGENYLPK LREILKTPVD VQTEPLFQEK
SWKSTFEFMS QMINDYDEYL PNTYLQYYLY PAKMRNKENP EYTRANEVMD GNEKETYERM
HKIISLGKIH GTKYELTSDV GCHAEYIVDL ATAIANNTNE IFLIITENKG TINNVSKDMM
VEVPCRVGSN GVEPLVVGSI PAFYKGLMEN QYAYEKLSVD ACLEGSYQKA LQALVLNRTV
VNTDVAKELL KDLIEANKGY WNELH
