AGLA_THENE
ID AGLA_THENE Reviewed; 480 AA.
AC O86960;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 25-JAN-2012, sequence version 2.
DT 03-AUG-2022, entry version 69.
DE RecName: Full=Alpha-glucosidase;
DE EC=3.2.1.20;
DE AltName: Full=Maltase;
GN Name=aglA;
OS Thermotoga neapolitana.
OC Bacteria; Thermotogae; Thermotogales; Thermotogaceae; Thermotoga.
OX NCBI_TaxID=2337;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=Z2706-MC24;
RX PubMed=14593916;
RA Berezina O.V., Lunina N.A., Zverlov V.V., Naumoff D.G., Liebl W.,
RA Velikodvorskaya G.A.;
RT "Thermotoga neapolitana gene clusters participating in degradation of
RT starch and maltodextins: molecular structure of the locus.";
RL Mol. Biol. (Mosk.) 37:801-809(2003).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, ACTIVITY REGULATION, AND SUBUNIT.
RC STRAIN=Z2706-MC24;
RX PubMed=14593917;
RA Lunina N.A., Berezina O.V., Veith B., Zverlov V.V., Vorob'eva I.P.,
RA Chekanovskaia L.A., Khromov I.S., Raash G., Libel W., Velikodvorskaia G.A.;
RT "Thermotoga neopolitina gene cluster, participating in degradation of
RT starch and maltodextrins: expression of aglB and aglA gene in Escherichia
RT coli, properties of recombinant enzymes.";
RL Mol. Biol. (Mosk.) 37:810-819(2003).
CC -!- FUNCTION: Is able to hydrolyze diverse types of alpha-glycoside bonds
CC in di- and trisaccharides: alpha-1,4 bonds of maltose and maltotriose,
CC alpha-1,1 bonds of trehalose, alpha-1,2 bonds of sucrose, alpha-1,3
CC bonds of turanose and melizitose, alpha-1,6 bonds of isomaltose and
CC melibiose. AglA is not specific with respect to the configuration at
CC the C-4 position of its substrates because it also possesses alpha-
CC galactosidase activity. Acts on the substrate from the non-reducing end
CC of the chain. The activity of AglA drops with increasing length of the
CC saccharide chain. Does not hydrolyze alpha-, beta-, and gamma-
CC cyclodextrins or polysaccharides (starch, pullulan, amylose,
CC amylopectin, glycogen). Does not cleave beta-glycosidic bonds in di-,
CC oligo-, or polysaccharides. {ECO:0000269|PubMed:14593917}.
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 Evidence={ECO:0000269|PubMed:14593917};
CC -!- COFACTOR:
CC Name=NAD(+); Xref=ChEBI:CHEBI:57540;
CC Evidence={ECO:0000269|PubMed:14593917};
CC Note=Binds 1 NAD(+) per subunit. {ECO:0000269|PubMed:14593917};
CC -!- COFACTOR:
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035;
CC Evidence={ECO:0000269|PubMed:14593917};
CC Note=Binds 1 Mn(2+) ion per subunit. {ECO:0000269|PubMed:14593917};
CC -!- ACTIVITY REGULATION: Inhibited by EDTA in vitro.
CC {ECO:0000269|PubMed:14593917}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7.5. {ECO:0000269|PubMed:14593917};
CC Temperature dependence:
CC Optimum temperature is 85 degrees Celsius. Retains 80% activity after
CC incubation at 85 degrees Celsius for 3 hours.
CC {ECO:0000269|PubMed:14593917};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:14593917}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 4 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA08868.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AJ009832; CAA08868.1; ALT_FRAME; Genomic_DNA.
DR AlphaFoldDB; O86960; -.
DR SMR; O86960; -.
DR CAZy; GH4; Glycoside Hydrolase Family 4.
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; 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.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Glycosidase; Hydrolase; Manganese; Metal-binding;
KW NAD.
FT CHAIN 1..480
FT /note="Alpha-glucosidase"
FT /id="PRO_0000415284"
FT ACT_SITE 175
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT ACT_SITE 260
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 119
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 153
FT /ligand="substrate"
FT /evidence="ECO:0000250"
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"
SQ SEQUENCE 480 AA; 54901 MW; 93A471746B46B21B CRC64;
MPAVKIGIIG AGSAVFSLRL VSDLCKTPGL SGSTVTLMDI DEERLDAVLT IAKKYVEEVG
ADLKFEKTTS VDEAIADADF VINTAMVGGH TYLEKVRRIS EKYGYYRGID AQEFNMVSDY
YTFSNYNQLK YFVDIARKIE RLSPKAWYSA AANPVFEGTT LVTRTVPIKA VGFCHGHYGV
MEIIEKLGLE RKQVDWQVAG VNHGIWLNRF RYNGEDAYPL LPRWISEKSK DWKPENPFND
QLSPAAIDMY KFYGVMPIGD TVRNASWRYH RDLETKKRWY GEPWGGADSE IGWKWYQDTL
GKVTDITKKV AKFIKENPAL KLSDLGSVLG KDLSEKQFVL EVEKILDPEK KSGEQHISFH
DALLNDNRSR FVINIPNKGI IQGIDDDVVV EVPAVVDRDG IHPEKIDPPL PERVVKYYLR
PRIMRMEMAL EAFLTGDIRI IKEVLYRDPR TKSDEQVEKV IEEILSLPEN EEMRKNYLKK
