PAGL_LEPBD
ID PAGL_LEPBD Reviewed; 440 AA.
AC C7NB67;
DT 21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
DT 13-OCT-2009, sequence version 1.
DT 03-AUG-2022, entry version 64.
DE RecName: Full=6-phospho-alpha-glucosidase;
DE EC=3.2.1.-;
GN Name=pagL; OrderedLocusNames=Lebu_1525;
OS Leptotrichia buccalis (strain ATCC 14201 / DSM 1135 / JCM 12969 / NCTC
OS 10249 / C-1013-b).
OC Bacteria; Fusobacteria; Fusobacteriales; Leptotrichiaceae; Leptotrichia.
OX NCBI_TaxID=523794;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 14201 / DSM 1135 / JCM 12969 / NCTC 10249 / C-1013-b;
RX PubMed=21304648; DOI=10.4056/sigs.1854;
RA Ivanova N., Gronow S., Lapidus A., Copeland A., Glavina Del Rio T.,
RA Nolan M., Lucas S., Chen F., Tice H., Cheng J.F., Saunders E., Bruce D.,
RA Goodwin L., Brettin T., Detter J.C., Han C., Pitluck S., Mikhailova N.,
RA Pati A., Mavrommatis K., Chen A., Palaniappan K., Land M., Hauser L.,
RA Chang Y.J., Jeffries C.D., Chain P., Rohde C., Goker M., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of Leptotrichia buccalis type strain (C-1013-
RT b).";
RL Stand. Genomic Sci. 1:126-132(2009).
RN [2]
RP PROTEIN SEQUENCE OF 1-25, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, COFACTOR, PH DEPENDENCE, INDUCTION, AND SUBUNIT.
RC STRAIN=ATCC 14201 / DSM 1135 / JCM 12969 / NCTC 10249 / C-1013-b;
RX PubMed=22230464; DOI=10.1111/j.2041-1014.2011.00627.x;
RA Thompson J., Pikis A.;
RT "Metabolism of sugars by genetically diverse species of oral
RT Leptotrichia.";
RL Mol. Oral. Microbiol. 27:34-44(2012).
CC -!- FUNCTION: In vitro, readily hydrolyzes p-nitrophenyl-alpha-D-
CC glucopyranoside 6-phosphate (pNPalphaG6P), a chromogenic analog of the
CC phosphorylated isomers of sucrose. In vivo, is probably involved in the
CC degradation of the 6-phosphate derivatives of the sucrose isomers
CC trehalulose, turanose, maltulose and palatinose, catalyzing their
CC hydrolysis into glucose 6-phosphate (G6P) and fructose, which allows
CC the bacterium to use these sugars as energy sources for growth. Is not
CC able to hydrolyze the C2 or C4 chromogenic stereomers (i.e. pNPalpha-
CC mannopyranoside-6P and pNPalpha-galactopyranoside-6P, respectively).
CC {ECO:0000269|PubMed:22230464}.
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000269|PubMed:22230464};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000269|PubMed:22230464};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:22230464};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000269|PubMed:22230464};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.9-7.3. {ECO:0000269|PubMed:22230464};
CC -!- PATHWAY: Glycan degradation; palatinose degradation.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:22230464}.
CC -!- INDUCTION: Induced by growth on the sucrose isomers trehalulose,
CC turanose, maltulose and palatinose. {ECO:0000269|PubMed:22230464}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family. {ECO:0000305}.
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DR EMBL; CP001685; ACV39398.1; -; Genomic_DNA.
DR RefSeq; WP_015769739.1; NC_013192.1.
DR AlphaFoldDB; C7NB67; -.
DR SMR; C7NB67; -.
DR STRING; 523794.Lebu_1525; -.
DR CAZy; GH4; Glycoside Hydrolase Family 4.
DR PRIDE; C7NB67; -.
DR EnsemblBacteria; ACV39398; ACV39398; Lebu_1525.
DR KEGG; lba:Lebu_1525; -.
DR eggNOG; COG1486; Bacteria.
DR HOGENOM; CLU_045951_2_0_0; -.
DR OMA; METYSPD; -.
DR OrthoDB; 277080at2; -.
DR UniPathway; UPA01004; -.
DR Proteomes; UP000001910; 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: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; Direct protein sequencing; Glycosidase; Hydrolase;
KW Manganese; Metal-binding; NAD; Reference proteome.
FT CHAIN 1..440
FT /note="6-phospho-alpha-glucosidase"
FT /id="PRO_0000415959"
FT ACT_SITE 170
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 263
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT BINDING 4..70
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 147
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 169
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 200
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 109
FT /note="Increases basicity of active site Tyr"
FT /evidence="ECO:0000250"
SQ SEQUENCE 440 AA; 49678 MW; 5EFD0FFE6BB654F0 CRC64;
MKKFSIVVAG GGSTFTPGIV LMLLENLDKF PIRQIKFYDN DAQRQEVIAK ACDIIIKEKA
PDINFVYTTD PETAFTDIDF VMAHIRVGKY AMREKDEKIP LRHGVLGQET CGPGGISYGM
RSIGGVIELV DYMEKYSPNA WMLNYSNPAA IVAEATRRLR PNSKILNICD MPIGIEIRMA
EMLGLKSRKD MVIRYFGLNH FGWWTDIRDK KGNDLMPALR EKVAKIGYNV EIEGENTEAS
WNDTFTKARD VFAIDPTTMP NTYLKYYFFP DYVVEHSNPN HTRANEVMEG REKFVFGECR
AIAEKGTAKD SKLHVDDHAS YIVDLARAIA YDTKERMLLI VENDGAISNF DPTAMVEVPC
IVGSNGPEKI VQGKIPQFQK GLMEQQVSVE KLTVEAWMEG SYQKLWQAIT LSRTVPSASV
AKAILDDLIE ANKDFWPVLK
