AGLB_THEMA
ID AGLB_THEMA Reviewed; 473 AA.
AC Q9X2F4;
DT 25-JAN-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 25-MAY-2022, entry version 113.
DE RecName: Full=Cyclomaltodextrinase;
DE EC=3.2.1.54;
DE AltName: Full=Maltodextrin glucosidase;
DE AltName: Full=TMG;
GN Name=aglB; OrderedLocusNames=TM_1835;
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 [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 [2]
RP FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE SPECIFICITY, ACTIVITY REGULATION,
RP AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8;
RX PubMed=12127967; DOI=10.1016/s0006-291x(02)00748-9;
RA Lee M.H., Kim Y.W., Kim T.J., Park C.S., Kim J.W., Moon T.W., Park K.H.;
RT "A novel amylolytic enzyme from Thermotoga maritima, resembling
RT cyclodextrinase and alpha-glucosidase, that liberates glucose from the
RT reducing end of the substrates.";
RL Biochem. Biophys. Res. Commun. 295:818-825(2002).
CC -!- FUNCTION: Is able to hydrolyze various linear maltooligosaccharides
CC (maltotriose to maltoheptaose) and cyclomaltodextrins (CDs), to mainly
CC glucose and maltose, by liberating glucose from the reducing end of the
CC molecules. Shows a very weak activity on starch. Can neither hydrolyze
CC maltose nor degrade pullulan, but rapidly hydrolyzes acarbose, a strong
CC amylase and glucosidase inhibitor, to acarviosine and glucose.
CC {ECO:0000269|PubMed:12127967}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cyclomaltodextrin + H2O = linear maltodextrin;
CC Xref=Rhea:RHEA:23980, Rhea:RHEA-COMP:14584, Rhea:RHEA-COMP:14707,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:17623, ChEBI:CHEBI:18398; EC=3.2.1.54;
CC Evidence={ECO:0000269|PubMed:12127967};
CC -!- ACTIVITY REGULATION: Mn(2+), Co(2+), Zn(2+), Fe(2+), Mg(2+), and Ca(2+)
CC inhibit the hydrolysis activity of the enzyme whereas EGTA and EDTA do
CC not affect the activity. {ECO:0000269|PubMed:12127967}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=20.64 mM for maltotriose (at pH 6.5 and 85 degrees Celsius)
CC {ECO:0000269|PubMed:12127967};
CC KM=11.84 mM for maltotetraose (at pH 6.5 and 85 degrees Celsius)
CC {ECO:0000269|PubMed:12127967};
CC KM=9.95 mM for maltopentaose (at pH 6.5 and 85 degrees Celsius)
CC {ECO:0000269|PubMed:12127967};
CC KM=7.77 mM for maltohexaose (at pH 6.5 and 85 degrees Celsius)
CC {ECO:0000269|PubMed:12127967};
CC KM=7.41 mM for maltoheptaose (at pH 6.5 and 85 degrees Celsius)
CC {ECO:0000269|PubMed:12127967};
CC KM=2.26 mM for pNP-maltopentaose (at pH 6.5 and 85 degrees Celsius)
CC {ECO:0000269|PubMed:12127967};
CC KM=14.53 mM for beta-cyclodextrin (at pH 6.5 and 85 degrees Celsius)
CC {ECO:0000269|PubMed:12127967};
CC pH dependence:
CC Optimum pH is 6.5 with beta-cyclodextrin as substrate.
CC {ECO:0000269|PubMed:12127967};
CC Temperature dependence:
CC Optimum temperature is 85 degrees Celsius with beta-cyclodextrin as
CC substrate. Retains 80% of its activity at 90 degrees Celsius. The
CC half-lives of the enzyme examined at 80, 85, and 90 degrees Celsius
CC are 147, 108, and 23 minutes, respectively.
CC {ECO:0000269|PubMed:12127967};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; AE000512; AAD36898.1; -; Genomic_DNA.
DR PIR; G72205; G72205.
DR RefSeq; NP_229632.1; NC_000853.1.
DR RefSeq; WP_004082380.1; NZ_CP011107.1.
DR AlphaFoldDB; Q9X2F4; -.
DR SMR; Q9X2F4; -.
DR STRING; 243274.THEMA_05025; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR EnsemblBacteria; AAD36898; AAD36898; TM_1835.
DR KEGG; tma:TM1835; -.
DR eggNOG; COG0366; Bacteria.
DR InParanoid; Q9X2F4; -.
DR OMA; TPDWVKH; -.
DR OrthoDB; 148706at2; -.
DR BRENDA; 3.2.1.B8; 10309.
DR Proteomes; UP000008183; Chromosome.
DR GO; GO:0047798; F:cyclomaltodextrinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.1180; -; 1.
DR Gene3D; 3.90.400.10; -; 1.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR045857; O16G_dom_2.
DR Pfam; PF00128; Alpha-amylase; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW Carbohydrate metabolism; Glycosidase; Hydrolase; Reference proteome.
FT CHAIN 1..473
FT /note="Cyclomaltodextrinase"
FT /id="PRO_0000415271"
FT ACT_SITE 210
FT /note="Nucleophile"
FT /evidence="ECO:0000250"
FT ACT_SITE 239
FT /note="Proton donor"
FT /evidence="ECO:0000250"
FT SITE 298
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
SQ SEQUENCE 473 AA; 55181 MW; E1CC229BAE5FA6CE CRC64;
MMYPMPSWVY DSVVYQIFPD RFFIGKGKTV EDKKDLYLKR GGVIEKWGVP PRKLPGAQHV
KIFYGGDLWG IAEKVDYFEE LGINVLYLTP IFLSDTNHKY DTIDYFRVDP QFGGKRAFLH
LLRVLHERSM KLILDGVFNH VGSQHPWFKK AKKNDPEYVN RFFLYKDRHR SWFDVGSLPE
LNVEVEEVKE YILKVVEHYL KLGIDGWRLD CGHDLGPTVN LWINMKVKEF SAEKYLVSEI
WTYPAGWDMV DGLMNYNFRN LVLSYVNGET DSIGFHLERA YRETKNIFGC WNMLDSHDTP
RLATMVPDRD LRKLAVVLQF TYPGVPLVYY GTEIGLTGGE DPECRATMEW NREKWDVDLF
EFYKKMIRLR RTDPGLRFGE FVLLNDSPLA FLRKAPHPLQ NTIVVVNPGE EKVLVLSIPD
GKIMNTTPLV DVFSGERFHV DGGVVKLPLL ARSFRILKPE DLRVGKYRLY KRV
