AGLB_KLEPN
ID AGLB_KLEPN Reviewed; 440 AA.
AC Q9AGA6;
DT 27-MAR-2002, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=6-phospho-alpha-glucosidase {ECO:0000303|PubMed:11322729};
DE EC=3.2.1.122 {ECO:0000269|PubMed:11473129};
GN Name=aglB {ECO:0000303|PubMed:11473129};
OS Klebsiella pneumoniae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-26, FUNCTION,
RP CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS,
RP INDUCTION, SUBUNIT, AND MASS SPECTROMETRY.
RC STRAIN=ATCC 23357 / A-11;
RX PubMed=11473129; DOI=10.1074/jbc.m106504200;
RA Thompson J., Robrish S.A., Immel S., Lichtenthaler F.W., Hall B.G.,
RA Pikis A.;
RT "Metabolism of sucrose and its five linkage-isomeric alpha-D-glucosyl-D-
RT fructoses by Klebsiella pneumoniae. Participation and properties of
RT sucrose-6-phosphate hydrolase and phospho-alpha-glucosidase.";
RL J. Biol. Chem. 276:37415-37425(2001).
RN [2]
RP PROTEIN SEQUENCE OF 1-25, FUNCTION, AND INDUCTION.
RC STRAIN=ATCC 23357 / A-11;
RX PubMed=11322729; DOI=10.1016/s0008-6215(01)00028-3;
RA Thompson J., Robrish S.A., Pikis A., Brust A., Lichtenthaler F.W.;
RT "Phosphorylation and metabolism of sucrose and its five linkage-isomeric
RT alpha-D-glucosyl-D-fructoses by Klebsiella pneumoniae.";
RL Carbohydr. Res. 331:149-161(2001).
CC -!- FUNCTION: Is involved in the catabolism of alpha-glycosides accumulated
CC via a phosphoenolpyruvate-dependent phosphotransferase system (PEP-
CC PTS). Hydrolyzes a wide variety of 6-phospho-alpha-D-glucosides
CC including maltose-6'-phosphate, isomaltose-6'-phosphate, maltitol-6-
CC phosphate, trehalose-6-phosphate and the 6'-phosphorylated derivatives
CC of the five linkage-isomeric alpha-D-glucosyl-D-fructoses: trehalulose-
CC 6'-phosphate, turanose-6'-phosphate, maltulose-6'-phosphate, leucrose-
CC 6'-phosphate, and palatinose-6'-phosphate. However, sucrose-6-phosphate
CC is not a substrate for this enzyme. {ECO:0000269|PubMed:11322729,
CC ECO:0000269|PubMed:11473129}.
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:11473129};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20422;
CC Evidence={ECO:0000269|PubMed:11473129};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000269|PubMed:11473129};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:11473129};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:11473129};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000269|PubMed:11473129};
CC Note=Divalent metal cation. Requires Mn(2+), Co(2+) or Ni(2+).
CC {ECO:0000269|PubMed:11473129};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.23 mM for trehalulose-6'-phosphate
CC {ECO:0000269|PubMed:11473129};
CC KM=1.68 mM for turanose-6'-phosphate {ECO:0000269|PubMed:11473129};
CC KM=1.20 mM for maltulose-6'-phosphate {ECO:0000269|PubMed:11473129};
CC KM=5.63 mM for leucrose-6'-phosphate {ECO:0000269|PubMed:11473129};
CC KM=2.42 mM for palatinose-6'-phosphate {ECO:0000269|PubMed:11473129};
CC KM=3.08 mM for maltose-6'-phosphate {ECO:0000269|PubMed:11473129};
CC KM=4.48 mM for isomaltose-6'-phosphate {ECO:0000269|PubMed:11473129};
CC KM=0.82 mM for maltitol-6-phosphate {ECO:0000269|PubMed:11473129};
CC KM=1.16 mM for trehalose-6-phosphate {ECO:0000269|PubMed:11473129};
CC KM=0.05 mM for p-nitrophenyl-alpha-D-glucopyranoside 6-phosphate
CC {ECO:0000269|PubMed:11473129};
CC Vmax=0.89 umol/min/mg enzyme with trehalulose-6'-phosphate as
CC substrate {ECO:0000269|PubMed:11473129};
CC Vmax=2.41 umol/min/mg enzyme with turanose-6'-phosphate as substrate
CC {ECO:0000269|PubMed:11473129};
CC Vmax=1.15 umol/min/mg enzyme with maltulose-6'-phosphate as substrate
CC {ECO:0000269|PubMed:11473129};
CC Vmax=0.85 umol/min/mg enzyme with leucrose-6'-phosphate as substrate
CC {ECO:0000269|PubMed:11473129};
CC Vmax=0.90 umol/min/mg enzyme with palatinose-6'-phosphate as
CC substrate {ECO:0000269|PubMed:11473129};
CC Vmax=1.31 umol/min/mg enzyme with maltose-6'-phosphate as substrate
CC {ECO:0000269|PubMed:11473129};
CC Vmax=1.55 umol/min/mg enzyme with isomaltose-6'-phosphate as
CC substrate {ECO:0000269|PubMed:11473129};
CC Vmax=1.87 umol/min/mg enzyme with maltitol-6-phosphate as substrate
CC {ECO:0000269|PubMed:11473129};
CC Vmax=0.31 umol/min/mg enzyme with trehalose-6-phosphate as substrate
CC {ECO:0000269|PubMed:11473129};
CC Vmax=2.42 umol/min/mg enzyme with p-nitrophenyl-alpha-D-
CC glucopyranoside 6-phosphate as substrate
CC {ECO:0000269|PubMed:11473129};
CC -!- PATHWAY: Glycan biosynthesis; sucrose metabolism.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:11473129}.
CC -!- INDUCTION: By the five linkage-isomeric alpha-D-glucosyl-D-fructoses,
CC or by maltose or maltitol. {ECO:0000269|PubMed:11322729,
CC ECO:0000269|PubMed:11473129}.
CC -!- MASS SPECTROMETRY: Mass=49254; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:11473129};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family. {ECO:0000305}.
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DR EMBL; AF337811; AAK01457.1; -; Genomic_DNA.
DR RefSeq; WP_002923306.1; NZ_WYAM01000023.1.
DR PDB; 6DUX; X-ray; 2.25 A; A/B=2-440.
DR PDB; 6DVV; X-ray; 2.25 A; A/B=2-440.
DR PDBsum; 6DUX; -.
DR PDBsum; 6DVV; -.
DR AlphaFoldDB; Q9AGA6; -.
DR SMR; Q9AGA6; -.
DR CAZy; GH4; Glycoside Hydrolase Family 4.
DR PRIDE; Q9AGA6; -.
DR OrthoDB; 277080at2; -.
DR BRENDA; 3.2.1.122; 2814.
DR SABIO-RK; Q9AGA6; -.
DR UniPathway; UPA00238; -.
DR GO; GO:0050081; F:maltose-6'-phosphate glucosidase activity; IDA:CACAO.
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:0005985; P:sucrose metabolic process; IEA:UniProtKB-UniPathway.
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 3D-structure; Carbohydrate metabolism; Cobalt; Direct protein sequencing;
KW Glycosidase; Hydrolase; Manganese; Metal-binding; NAD; Nickel.
FT CHAIN 1..440
FT /note="6-phospho-alpha-glucosidase"
FT /id="PRO_0000169856"
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"
FT STRAND 4..9
FT /evidence="ECO:0007829|PDB:6DUX"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:6DUX"
FT TURN 26..29
FT /evidence="ECO:0007829|PDB:6DUX"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:6DUX"
FT HELIX 42..59
FT /evidence="ECO:0007829|PDB:6DUX"
FT STRAND 63..69
FT /evidence="ECO:0007829|PDB:6DUX"
FT HELIX 71..75
FT /evidence="ECO:0007829|PDB:6DUX"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:6DUX"
FT HELIX 89..102
FT /evidence="ECO:0007829|PDB:6DUX"
FT STRAND 109..112
FT /evidence="ECO:0007829|PDB:6DUX"
FT HELIX 113..136
FT /evidence="ECO:0007829|PDB:6DUX"
FT STRAND 141..144
FT /evidence="ECO:0007829|PDB:6DUX"
FT HELIX 149..159
FT /evidence="ECO:0007829|PDB:6DUX"
FT STRAND 165..167
FT /evidence="ECO:0007829|PDB:6DUX"
FT HELIX 171..183
FT /evidence="ECO:0007829|PDB:6DUX"
FT HELIX 188..190
FT /evidence="ECO:0007829|PDB:6DUX"
FT STRAND 191..198
FT /evidence="ECO:0007829|PDB:6DUX"
FT STRAND 201..209
FT /evidence="ECO:0007829|PDB:6DUX"
FT HELIX 216..226
FT /evidence="ECO:0007829|PDB:6DUX"
FT HELIX 240..252
FT /evidence="ECO:0007829|PDB:6DUX"
FT STRAND 258..260
FT /evidence="ECO:0007829|PDB:6DUX"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:6DUX"
FT HELIX 265..268
FT /evidence="ECO:0007829|PDB:6DUX"
FT HELIX 270..275
FT /evidence="ECO:0007829|PDB:6DUX"
FT HELIX 283..289
FT /evidence="ECO:0007829|PDB:6DUX"
FT HELIX 291..305
FT /evidence="ECO:0007829|PDB:6DUX"
FT HELIX 308..310
FT /evidence="ECO:0007829|PDB:6DUX"
FT HELIX 318..320
FT /evidence="ECO:0007829|PDB:6DUX"
FT HELIX 321..331
FT /evidence="ECO:0007829|PDB:6DUX"
FT STRAND 335..342
FT /evidence="ECO:0007829|PDB:6DUX"
FT STRAND 354..363
FT /evidence="ECO:0007829|PDB:6DUX"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:6DUX"
FT HELIX 377..399
FT /evidence="ECO:0007829|PDB:6DUX"
FT HELIX 402..411
FT /evidence="ECO:0007829|PDB:6DUX"
FT HELIX 418..431
FT /evidence="ECO:0007829|PDB:6DUX"
FT TURN 432..435
FT /evidence="ECO:0007829|PDB:6DUX"
SQ SEQUENCE 440 AA; 49255 MW; 5D7287435E4DDC45 CRC64;
MKKFSVVIAG GGSTFTPGIV LMLLANQDRF PLRSLKFYDN DGARQETIAE ACKVILKEQA
PEIEFSYTTD PQAAFTDVDF VMAHIRVGKY PMREQDEKIP LRHGVLGQET CGPGGIAYGM
RSIGGVLELV DYMEKYSPNA WMLNYSNPAA IVAEATRRLR PNAKILNICD MPIGIEGRMA
QIVGLKDRKQ MRVRYYGLNH FGWWTSIEDL DGNDLMPKLR EYVAKYGYVP PSNDPHTEAS
WNDTFAKAKD VQALDPQTMP NTYLKYYLFP DYVVAHSNPE RTRANEVMDH REKNVFSACR
AIIAAGKSTA GDLEIDEHAS YIVDLATAIA FNTQERMLLI VPNNGAIHNF DADAMVEIPC
LVGHNGPEPL TVGDIPHFQK GLMSQQVAVE KLVVDAWEQR SYHKLWQAIT LSKTVPSASV
AKAILDDLIA ANKDYWPELH
