AGLA_THEMA
ID AGLA_THEMA Reviewed; 480 AA.
AC O33830;
DT 15-DEC-1998, integrated into UniProtKB/Swiss-Prot.
DT 30-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Alpha-glucosidase;
DE EC=3.2.1.20;
DE AltName: Full=Maltase;
GN Name=aglA; OrderedLocusNames=TM_1834;
OS Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826
OS / MSB8).
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=243274;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=9453151; DOI=10.1111/j.1574-6968.1998.tb12793.x;
RA Bibel M., Brettl C., Gosslar U., Kriegshaeuser G., Liebl W.;
RT "Isolation and analysis of genes for amylolytic enzymes of the
RT hyperthermophilic bacterium Thermotoga maritima.";
RL FEMS Microbiol. Lett. 158:9-15(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10360571; DOI=10.1038/20601;
RA Nelson K.E., Clayton R.A., Gill S.R., Gwinn M.L., Dodson R.J., Haft D.H.,
RA Hickey E.K., Peterson J.D., Nelson W.C., Ketchum K.A., McDonald L.A.,
RA Utterback T.R., Malek J.A., Linher K.D., Garrett M.M., Stewart A.M.,
RA Cotton M.D., Pratt M.S., Phillips C.A., Richardson D.L., Heidelberg J.F.,
RA Sutton G.G., Fleischmann R.D., Eisen J.A., White O., Salzberg S.L.,
RA Smith H.O., Venter J.C., Fraser C.M.;
RT "Evidence for lateral gene transfer between Archaea and Bacteria from
RT genome sequence of Thermotoga maritima.";
RL Nature 399:323-329(1999).
RN [3]
RP CHARACTERIZATION, SUBUNIT, COFACTOR, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=10972187; DOI=10.1007/pl00010711;
RA Raasch C., Streit W., Schanzer J., Bibel M., Gosslar U., Liebl W.;
RT "Thermotoga maritima AglA, an extremely thermostable NAD+-, Mn2+-, and
RT thiol-dependent alpha-glucosidase.";
RL Extremophiles 4:189-200(2000).
RN [4]
RP MUTAGENESIS OF GLY-10; GLY-12 AND SER-13, AND KINETIC PARAMETERS.
RX PubMed=12062450; DOI=10.1016/s0014-5793(02)02641-8;
RA Raasch C., Armbrecht M., Streit W., Hoecker B., Straeter N., Liebl W.;
RT "Identification of residues important for NAD+ binding by the Thermotoga
RT maritima alpha-glucosidase AglA, a member of glycoside hydrolase family
RT 4.";
RL FEBS Lett. 517:267-271(2002).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF COMPLEX WITH NAD(+) AND MALTOSE.
RX PubMed=12588867; DOI=10.1074/jbc.m211626200;
RA Lodge J.A., Maier T., Liebl W., Hoffmann V., Straeter N.;
RT "Crystal structure of Thermotoga maritima alpha-glucosidase AglA defines a
RT new clan of NAD+-dependent glycosidases.";
RL J. Biol. Chem. 278:19151-19158(2003).
CC -!- FUNCTION: Alpha-glycosidase with a very broad specificity. Hydrolyzes
CC maltose and other small maltooligosaccharides but is inactive against
CC the polymeric substrate starch. AglA is not specific with respect to
CC the configuration at the C-4 position of its substrates because
CC glycosidic derivatives of D-galactose are also hydrolyzed. Does not
CC cleave beta-glycosidic bonds.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Hydrolysis of terminal, non-reducing (1->4)-linked alpha-D-
CC glucose residues with release of alpha-D-glucose.; EC=3.2.1.20;
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000269|PubMed:10972187};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000269|PubMed:10972187};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:10972187};
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:10972187};
CC Name=Ni(2+); Xref=ChEBI:CHEBI:49786;
CC Evidence={ECO:0000269|PubMed:10972187};
CC Note=Binds 1 Mn(2+) ion per subunit. Can also use Co(2+) and Ni(2+)
CC ions, albeit less efficiently than manganese ion.
CC {ECO:0000269|PubMed:10972187};
CC -!- ACTIVITY REGULATION: Inhibited by Hg(2+) ion and EDTA.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=0.23 mM for p-nitrophenyl-alpha-D-glucopyranoside
CC {ECO:0000269|PubMed:10972187, ECO:0000269|PubMed:12062450};
CC KM=0.53 mM for p-nitrophenyl-alpha-D-galactopyranoside
CC {ECO:0000269|PubMed:10972187, ECO:0000269|PubMed:12062450};
CC Vmax=9.94 umol/min/mg enzyme with p-nitrophenyl-alpha-D-
CC glucopyranoside as substrate {ECO:0000269|PubMed:10972187,
CC ECO:0000269|PubMed:12062450};
CC Vmax=11.42 umol/min/mg enzyme with p-nitrophenyl-alpha-D-
CC galactopyranoside as substrate {ECO:0000269|PubMed:10972187,
CC ECO:0000269|PubMed:12062450};
CC pH dependence:
CC Optimum pH is 7.5. Active from pH 6.5 to 9.
CC {ECO:0000269|PubMed:10972187};
CC Temperature dependence:
CC Optimum temperature is 90 degrees Celsius. Active from 60 to 105
CC degrees Celsius. Highly thermostable. {ECO:0000269|PubMed:10972187};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:10972187}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family. {ECO:0000305}.
CC -!- CAUTION: In the crystal structure (PubMed:12588867), the metal ion is
CC absent, probably due to the oxidation of the active site Cys-174 to
CC sulfinic acid. In the absence of metal, positions of the coenzyme and
CC the substrate and their interactions are all significantly altered,
CC presumably accounting for the inactivity of this form.
CC {ECO:0000305|PubMed:12588867}.
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DR EMBL; AJ001089; CAA04524.1; -; Genomic_DNA.
DR EMBL; AE000512; AAD36897.1; -; Genomic_DNA.
DR PIR; F72205; F72205.
DR RefSeq; NP_229631.1; NC_000853.1.
DR RefSeq; WP_010865414.1; NZ_CP011107.1.
DR PDB; 1OBB; X-ray; 1.90 A; A/B=1-480.
DR PDBsum; 1OBB; -.
DR AlphaFoldDB; O33830; -.
DR SMR; O33830; -.
DR STRING; 243274.THEMA_05030; -.
DR DrugBank; DB03323; Maltose.
DR CAZy; GH4; Glycoside Hydrolase Family 4.
DR EnsemblBacteria; AAD36897; AAD36897; TM_1834.
DR KEGG; tma:TM1834; -.
DR eggNOG; COG1486; Bacteria.
DR InParanoid; O33830; -.
DR OMA; YVPWYLH; -.
DR OrthoDB; 277080at2; -.
DR BRENDA; 3.2.1.20; 6331.
DR SABIO-RK; O33830; -.
DR EvolutionaryTrace; O33830; -.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0032450; F:maltose alpha-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 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; Glycosidase; Hydrolase;
KW Manganese; Metal-binding; NAD; Nickel; Reference proteome.
FT CHAIN 1..480
FT /note="Alpha-glucosidase"
FT /id="PRO_0000169855"
FT ACT_SITE 175
FT /note="Proton donor"
FT /evidence="ECO:0000305"
FT ACT_SITE 260
FT /note="Proton acceptor"
FT /evidence="ECO:0000305"
FT BINDING 4..70
FT /ligand="NAD(+)"
FT /ligand_id="ChEBI:CHEBI:57540"
FT BINDING 119
FT /ligand="substrate"
FT BINDING 153
FT /ligand="substrate"
FT BINDING 174
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="Mn(2+)"
FT /ligand_id="ChEBI:CHEBI:29035"
FT /evidence="ECO:0000250"
FT MUTAGEN 10
FT /note="G->A: Reduced activity. 300-fold reduction of the
FT binding affinity for NAD(+). No change in substrate
FT affinity."
FT /evidence="ECO:0000269|PubMed:12062450"
FT MUTAGEN 12
FT /note="G->A: No change in activity and substrate affinity.
FT 5-fold reduction of the binding affinity for NAD(+)."
FT /evidence="ECO:0000269|PubMed:12062450"
FT MUTAGEN 13
FT /note="S->A: Highly reduced activity. 10-fold reduction of
FT the binding affinity for NAD(+). No change in substrate
FT affinity."
FT /evidence="ECO:0000269|PubMed:12062450"
FT CONFLICT 459..479
FT /note="Missing (in Ref. 1)"
FT /evidence="ECO:0000305"
FT STRAND 5..9
FT /evidence="ECO:0007829|PDB:1OBB"
FT TURN 10..12
FT /evidence="ECO:0007829|PDB:1OBB"
FT HELIX 14..25
FT /evidence="ECO:0007829|PDB:1OBB"
FT HELIX 28..30
FT /evidence="ECO:0007829|PDB:1OBB"
FT STRAND 34..38
FT /evidence="ECO:0007829|PDB:1OBB"
FT HELIX 42..58
FT /evidence="ECO:0007829|PDB:1OBB"
FT STRAND 64..69
FT /evidence="ECO:0007829|PDB:1OBB"
FT HELIX 71..75
FT /evidence="ECO:0007829|PDB:1OBB"
FT STRAND 79..83
FT /evidence="ECO:0007829|PDB:1OBB"
FT HELIX 89..102
FT /evidence="ECO:0007829|PDB:1OBB"
FT STRAND 122..124
FT /evidence="ECO:0007829|PDB:1OBB"
FT HELIX 126..142
FT /evidence="ECO:0007829|PDB:1OBB"
FT STRAND 147..150
FT /evidence="ECO:0007829|PDB:1OBB"
FT HELIX 155..165
FT /evidence="ECO:0007829|PDB:1OBB"
FT STRAND 168..173
FT /evidence="ECO:0007829|PDB:1OBB"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:1OBB"
FT HELIX 179..186
FT /evidence="ECO:0007829|PDB:1OBB"
FT HELIX 191..193
FT /evidence="ECO:0007829|PDB:1OBB"
FT STRAND 194..201
FT /evidence="ECO:0007829|PDB:1OBB"
FT STRAND 204..212
FT /evidence="ECO:0007829|PDB:1OBB"
FT HELIX 218..227
FT /evidence="ECO:0007829|PDB:1OBB"
FT HELIX 229..231
FT /evidence="ECO:0007829|PDB:1OBB"
FT HELIX 244..253
FT /evidence="ECO:0007829|PDB:1OBB"
FT HELIX 259..261
FT /evidence="ECO:0007829|PDB:1OBB"
FT HELIX 267..270
FT /evidence="ECO:0007829|PDB:1OBB"
FT HELIX 273..280
FT /evidence="ECO:0007829|PDB:1OBB"
FT TURN 282..285
FT /evidence="ECO:0007829|PDB:1OBB"
FT HELIX 290..316
FT /evidence="ECO:0007829|PDB:1OBB"
FT HELIX 322..324
FT /evidence="ECO:0007829|PDB:1OBB"
FT STRAND 326..329
FT /evidence="ECO:0007829|PDB:1OBB"
FT HELIX 333..346
FT /evidence="ECO:0007829|PDB:1OBB"
FT HELIX 356..365
FT /evidence="ECO:0007829|PDB:1OBB"
FT STRAND 369..376
FT /evidence="ECO:0007829|PDB:1OBB"
FT STRAND 388..397
FT /evidence="ECO:0007829|PDB:1OBB"
FT STRAND 400..403
FT /evidence="ECO:0007829|PDB:1OBB"
FT HELIX 412..417
FT /evidence="ECO:0007829|PDB:1OBB"
FT HELIX 419..435
FT /evidence="ECO:0007829|PDB:1OBB"
FT HELIX 438..446
FT /evidence="ECO:0007829|PDB:1OBB"
FT HELIX 454..465
FT /evidence="ECO:0007829|PDB:1OBB"
FT HELIX 468..470
FT /evidence="ECO:0007829|PDB:1OBB"
FT HELIX 471..477
FT /evidence="ECO:0007829|PDB:1OBB"
SQ SEQUENCE 480 AA; 55047 MW; 4CA5DB3B155CE5A1 CRC64;
MPSVKIGIIG AGSAVFSLRL VSDLCKTPGL SGSTVTLMDI DEERLDAILT IAKKYVEEVG
ADLKFEKTMN LDDVIIDADF VINTAMVGGH TYLEKVRQIG EKYGYYRGID AQEFNMVSDY
YTFSNYNQLK YFVDIARKIE KLSPKAWYLQ AANPIFEGTT LVTRTVPIKA VGFCHGHYGV
MEIVEKLGLE EEKVDWQVAG VNHGIWLNRF RYNGGNAYPL LDKWIEEKSK DWKPENPFND
QLSPAAIDMY RFYGVMPIGD TVRNSSWRYH RDLETKKKWY GEPWGGADSE IGWKWYQDTL
GKVTEITKKV AKFIKENPSV RLSDLGSVLG KDLSEKQFVL EVEKILDPER KSGEQHIPFI
DALLNDNKAR FVVNIPNKGI IHGIDDDVVV EVPALVDKNG IHPEKIEPPL PDRVVKYYLR
PRIMRMEMAL EAFLTGDIRI IKELLYRDPR TKSDEQVEKV IEEILALPEN EEMRKHYLKR
