AMY_BACLI
ID AMY_BACLI Reviewed; 512 AA.
AC P06278; Q45283; Q84I71;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 160.
DE RecName: Full=Alpha-amylase;
DE EC=3.2.1.1 {ECO:0000269|PubMed:11997021, ECO:0000269|PubMed:12915728, ECO:0000269|PubMed:14632998};
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE AltName: Full=BLA;
DE Flags: Precursor;
GN Name=amyS; Synonyms=amyL;
OS Bacillus licheniformis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1402;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 27811 / BCRC 10494 / FERM P-1038;
RX PubMed=2418011; DOI=10.1093/oxfordjournals.jbchem.a135381;
RA Yuuki T., Nomura T., Tezuka H., Tsuboi A., Yamagata H., Tsukagoshi N.,
RA Udaka S.;
RT "Complete nucleotide sequence of a gene coding for heat- and pH-stable
RT alpha-amylase of Bacillus licheniformis: comparison of the amino acid
RT sequences of three bacterial liquefying alpha-amylases deduced from the DNA
RT sequences.";
RL J. Biochem. 98:1147-1156(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3009417; DOI=10.1128/jb.166.2.635-643.1986;
RA Gray G.L., Mainzer S.E., Rey M.W., Lamsa M.H., Kindle K.L., Carmona C.,
RA Requadt C.;
RT "Structural genes encoding the thermophilic alpha-amylases of Bacillus
RT stearothermophilus and Bacillus licheniformis.";
RL J. Bacteriol. 166:635-643(1986).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], CATALYTIC ACTIVITY, AND SUBCELLULAR
RP LOCATION.
RX PubMed=14632998; DOI=10.1046/j.1365-2672.2003.02082.x;
RA Shahhoseini M., Ziaee A.A., Ghaemi N.;
RT "Expression and secretion of an alpha-amylase gene from a native strain of
RT Bacillus licheniformis in Escherichia coli by T7 promoter and putative
RT signal peptide of the gene.";
RL J. Appl. Microbiol. 95:1250-1254(2003).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-121.
RC STRAIN=ATCC 14580 / DSM 13 / NBRC 12200 / NCIMB 9375 / NCTC 10341 / Gibson
RC 46;
RX PubMed=6334606; DOI=10.1111/j.1432-1033.1984.tb08594.x;
RA Sibakov M., Palva I.;
RT "Isolation and the 5'-end nucleotide sequence of Bacillus licheniformis
RT alpha-amylase gene.";
RL Eur. J. Biochem. 145:567-572(1984).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-104.
RX PubMed=6609154; DOI=10.1128/jb.158.1.369-372.1984;
RA Stephens M.A., Ortlepp S.A., Ollington J.F., McConnell D.J.;
RT "Nucleotide sequence of the 5' region of the Bacillus licheniformis alpha-
RT amylase gene: comparison with the B. amyloliquefaciens gene.";
RL J. Bacteriol. 158:369-372(1984).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-33.
RX PubMed=2265757; DOI=10.1016/0378-1119(90)90338-r;
RA Jorgensen L., Hansen C.K., Poulsen G.B., Diderichsen B.;
RT "In vivo genetic engineering: homologous recombination as a tool for
RT plasmid construction.";
RL Gene 96:37-41(1990).
RN [7]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-29.
RX PubMed=2540150; DOI=10.1128/jb.171.5.2435-2442.1989;
RA Laoide B.M., Chambliss G.H., McConnell D.J.;
RT "Bacillus licheniformis alpha-amylase gene, amyL, is subject to promoter-
RT independent catabolite repression in Bacillus subtilis.";
RL J. Bacteriol. 171:2435-2442(1989).
RN [8]
RP PROTEIN SEQUENCE OF 30-47.
RX PubMed=6172418; DOI=10.1128/jb.149.1.372-373.1982;
RA Kuhn H., Fietzek P.P., Lampen J.O.;
RT "N-terminal amino acid sequence of Bacillus licheniformis alpha-amylase:
RT comparison with Bacillus amyloliquefaciens and Bacillus subtilis enzymes.";
RL J. Bacteriol. 149:372-373(1982).
RN [9]
RP MAPPING OF SUBSTRATE-BINDING SITE, AND CATALYTIC ACTIVITY.
RX PubMed=11997021; DOI=10.1016/s0014-5793(02)02649-2;
RA Kandra L., Gyemant G., Remenyik J., Hovanszki G., Liptak A.;
RT "Action pattern and subsite mapping of Bacillus licheniformis alpha-amylase
RT (BLA) with modified maltooligosaccharide substrates.";
RL FEBS Lett. 518:79-82(2002).
RN [10]
RP MUTAGENESIS OF HIS-64; HIS-162; HIS-276; HIS-322; HIS-435 AND HIS-479.
RC STRAIN=ATCC 6598 / NRS 745;
RX PubMed=2394736; DOI=10.1016/s0021-9258(18)55421-1;
RA Declerck N., Joyet P., Gaillardin C., Masson J.-M.;
RT "Use of amber suppressors to investigate the thermostability of Bacillus
RT licheniformis alpha-amylase. Amino acid replacements at 6 histidine
RT residues reveal a critical position at His-133.";
RL J. Biol. Chem. 265:15481-15488(1990).
RN [11]
RP MUTAGENESIS OF ALA-238.
RC STRAIN=ATCC 6598 / NRS 745;
RX PubMed=8771184; DOI=10.1093/protein/8.10.1029;
RA Declerck N., Joyet P., Trosset J.Y., Garnier J., Gaillardin C.;
RT "Hyperthermostable mutants of Bacillus licheniformis alpha-amylase:
RT multiple amino acid replacements and molecular modelling.";
RL Protein Eng. 8:1029-1037(1995).
RN [12]
RP MUTAGENESIS OF ASP-150; ASN-155; ARG-175; ASP-193; ASN-201; GLN-207;
RP ASN-217; ASN-219; ASN-221; ASP-229; ASP-233; ALA-298; GLU-300; GLN-359 AND
RP GLU-365.
RC STRAIN=ATCC 6598 / NRS 745;
RX PubMed=10966804; DOI=10.1006/jmbi.2000.4025;
RA Declerck N., Machius M., Wiegand G., Huber R., Gaillardin C.;
RT "Probing structural determinants specifying high thermostability in
RT Bacillus licheniformis alpha-amylase.";
RL J. Mol. Biol. 301:1041-1057(2000).
RN [13]
RP MUTAGENESIS OF GLN-293 AND ASN-294.
RC STRAIN=ATCC 6598 / NRS 745;
RX PubMed=12736372; DOI=10.1093/proeng/gzg032;
RA Declerck N., Machius M., Joyet P., Wiegand G., Huber R., Gaillardin C.;
RT "Hyperthermostabilization of Bacillus licheniformis alpha-amylase and
RT modulation of its stability over a 50 degrees C temperature range.";
RL Protein Eng. 16:287-293(2003).
RN [14]
RP CATALYTIC ACTIVITY, AND MUTAGENESIS OF TRP-292 AND VAL-315.
RC STRAIN=ATCC 27811 / BCRC 10494 / FERM P-1038;
RX PubMed=12915728; DOI=10.1093/protein/gzg060;
RA Rivera M.H., Lopez-Munguia A., Soberon X., Saab-Rincon G.;
RT "Alpha-amylase from Bacillus licheniformis mutants near to the catalytic
RT site: effects on hydrolytic and transglycosylation activity.";
RL Protein Eng. 16:505-514(2003).
RN [15]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 30-512.
RC STRAIN=ATCC 27811 / BCRC 10494 / FERM P-1038;
RX PubMed=7877175; DOI=10.1006/jmbi.1994.0106;
RA Machius M., Wiegand G., Huber R.;
RT "Crystal structure of calcium-depleted Bacillus licheniformis alpha-amylase
RT at 2.2-A resolution.";
RL J. Mol. Biol. 246:545-559(1995).
RN [16]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 30-512 IN COMPLEX WITH CALCIUM
RP AND SODIUM, AND COFACTOR.
RX PubMed=9551551; DOI=10.1016/s0969-2126(98)00032-x;
RA Machius M., Declerck N., Huber R., Wiegand G.;
RT "Activation of Bacillus licheniformis alpha-amylase through a
RT disorder-->order transition of the substrate-binding site mediated by a
RT calcium-sodium-calcium metal triad.";
RL Structure 6:281-292(1998).
RN [17]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 330-512.
RX PubMed=10924103; DOI=10.1021/bi0000317;
RA Brzozowski A.M., Lawson D.M., Turkenburg J.P., Bisgaard-Frantzen H.,
RA Svendsen A., Borchert T.V., Dauter Z., Wilson K.S., Davies G.J.;
RT "Structural analysis of a chimeric bacterial alpha-amylase. High-resolution
RT analysis of native and ligand complexes.";
RL Biochemistry 39:9099-9107(2000).
RN [18]
RP X-RAY CRYSTALLOGRAPHY (1.83 ANGSTROMS) OF 30-512 OF MUTANT
RP VAL-162/PHE-219/VAL-238/SER-293/TYR-294 IN COMPLEX WITH CALCIUM AND SODIUM,
RP AND COFACTOR.
RC STRAIN=ATCC 6598 / NRS 745;
RX PubMed=12540849; DOI=10.1074/jbc.m212618200;
RA Machius M., Declerck N., Huber R., Wiegand G.;
RT "Kinetic stabilization of Bacillus licheniformis alpha-amylase through
RT introduction of hydrophobic residues at the surface.";
RL J. Biol. Chem. 278:11546-11553(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in
CC polysaccharides containing three or more (1->4)-alpha-linked D-
CC glucose units.; EC=3.2.1.1; Evidence={ECO:0000269|PubMed:11997021,
CC ECO:0000269|PubMed:12915728, ECO:0000269|PubMed:14632998};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551};
CC Note=Binds 3 Ca(2+) ions per subunit. {ECO:0000269|PubMed:12540849,
CC ECO:0000269|PubMed:9551551};
CC -!- COFACTOR:
CC Name=Na(+); Xref=ChEBI:CHEBI:29101;
CC Evidence={ECO:0000269|PubMed:12540849, ECO:0000269|PubMed:9551551};
CC Note=Binds 1 sodium ion per subunit. {ECO:0000269|PubMed:12540849,
CC ECO:0000269|PubMed:9551551};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Active up to pH 11.;
CC Temperature dependence:
CC Active up to 100 degrees Celsius.;
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:14632998}.
CC -!- BIOTECHNOLOGY: Used in the food industry for high temperature
CC liquefaction of starch-containing mashes and in the detergent industry
CC to remove starch. Sold under the name Termamyl by Novozymes.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; X03236; CAA26981.1; -; Genomic_DNA.
DR EMBL; M38570; AAA22226.1; -; Genomic_DNA.
DR EMBL; M13256; AAA22240.1; -; Genomic_DNA.
DR EMBL; AF438149; AAO26743.1; -; Genomic_DNA.
DR EMBL; K01984; AAA22193.1; -; Genomic_DNA.
DR EMBL; M62637; AAA22232.1; -; Genomic_DNA.
DR EMBL; M26412; AAA22237.1; -; Genomic_DNA.
DR PIR; A91997; ALBSL.
DR RefSeq; WP_017474613.1; NZ_UAQA01000026.1.
DR RefSeq; WP_025807921.1; NZ_NPCV01000044.1.
DR PDB; 1BLI; X-ray; 1.90 A; A=30-512.
DR PDB; 1BPL; X-ray; 2.20 A; A=30-218, B=219-512.
DR PDB; 1E3X; X-ray; 1.90 A; A=330-512.
DR PDB; 1E3Z; X-ray; 1.93 A; A=330-512.
DR PDB; 1E40; X-ray; 2.20 A; A=330-512.
DR PDB; 1E43; X-ray; 1.70 A; A=330-512.
DR PDB; 1OB0; X-ray; 1.83 A; A=30-512.
DR PDB; 1VJS; X-ray; 1.70 A; A=30-512.
DR PDBsum; 1BLI; -.
DR PDBsum; 1BPL; -.
DR PDBsum; 1E3X; -.
DR PDBsum; 1E3Z; -.
DR PDBsum; 1E40; -.
DR PDBsum; 1E43; -.
DR PDBsum; 1OB0; -.
DR PDBsum; 1VJS; -.
DR AlphaFoldDB; P06278; -.
DR PCDDB; P06278; -.
DR SMR; P06278; -.
DR BindingDB; P06278; -.
DR ChEMBL; CHEMBL4215; -.
DR Allergome; 8255; Bac li aA.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR PRIDE; P06278; -.
DR BRENDA; 3.2.1.1; 669.
DR EvolutionaryTrace; P06278; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004556; F:alpha-amylase activity; IDA:CACAO.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 2.60.40.1180; -; 1.
DR InterPro; IPR013776; A-amylase_thermo.
DR InterPro; IPR015237; Alpha-amylase_C_pro.
DR InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR InterPro; IPR013780; Glyco_hydro_b.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR Pfam; PF00128; Alpha-amylase; 1.
DR Pfam; PF09154; DUF1939; 1.
DR PIRSF; PIRSF001021; Alph-amls_thrmst; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; SSF51445; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Calcium; Carbohydrate metabolism; Direct protein sequencing;
KW Glycosidase; Hydrolase; Metal-binding; Secreted; Signal.
FT SIGNAL 1..29
FT /evidence="ECO:0000269|PubMed:6172418"
FT CHAIN 30..512
FT /note="Alpha-amylase"
FT /id="PRO_0000001332"
FT ACT_SITE 260
FT /note="Nucleophile"
FT ACT_SITE 290
FT /note="Proton donor"
FT BINDING 133
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12540849,
FT ECO:0000269|PubMed:9551551, ECO:0007744|PDB:1BLI,
FT ECO:0007744|PDB:1OB0"
FT BINDING 190
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12540849,
FT ECO:0000269|PubMed:9551551, ECO:0007744|PDB:1BLI,
FT ECO:0007744|PDB:1OB0"
FT BINDING 190
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:12540849,
FT ECO:0000269|PubMed:9551551"
FT BINDING 210
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12540849,
FT ECO:0000269|PubMed:9551551, ECO:0007744|PDB:1BLI,
FT ECO:0007744|PDB:1OB0"
FT BINDING 212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12540849,
FT ECO:0000269|PubMed:9551551, ECO:0007744|PDB:1BLI,
FT ECO:0007744|PDB:1OB0"
FT BINDING 212
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:12540849,
FT ECO:0000269|PubMed:9551551"
FT BINDING 223
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12540849,
FT ECO:0000269|PubMed:9551551, ECO:0007744|PDB:1BLI,
FT ECO:0007744|PDB:1OB0"
FT BINDING 223
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:12540849,
FT ECO:0000269|PubMed:9551551"
FT BINDING 229
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:12540849,
FT ECO:0000269|PubMed:9551551, ECO:0007744|PDB:1BLI,
FT ECO:0007744|PDB:1OB0"
FT BINDING 229
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:12540849,
FT ECO:0000269|PubMed:9551551"
FT BINDING 231
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12540849,
FT ECO:0000269|PubMed:9551551, ECO:0007744|PDB:1BLI,
FT ECO:0007744|PDB:1OB0"
FT BINDING 233
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:12540849,
FT ECO:0000269|PubMed:9551551, ECO:0007744|PDB:1BLI,
FT ECO:0007744|PDB:1OB0"
FT BINDING 264
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0007744|PDB:1BLI, ECO:0007744|PDB:1OB0"
FT BINDING 329
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:12540849,
FT ECO:0000269|PubMed:9551551, ECO:0007744|PDB:1BLI,
FT ECO:0007744|PDB:1OB0"
FT BINDING 331
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:12540849,
FT ECO:0000269|PubMed:9551551, ECO:0007744|PDB:1BLI,
FT ECO:0007744|PDB:1OB0"
FT BINDING 435
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:12540849,
FT ECO:0000269|PubMed:9551551, ECO:0007744|PDB:1BLI,
FT ECO:0007744|PDB:1OB0"
FT BINDING 436
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:12540849,
FT ECO:0000269|PubMed:9551551, ECO:0007744|PDB:1BLI,
FT ECO:0007744|PDB:1OB0"
FT BINDING 459
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:12540849,
FT ECO:0000269|PubMed:9551551, ECO:0007744|PDB:1BLI,
FT ECO:0007744|PDB:1OB0"
FT SITE 357
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT MUTAGEN 64
FT /note="H->X: No effect on thermostability."
FT /evidence="ECO:0000269|PubMed:2394736"
FT MUTAGEN 150
FT /note="D->X: Decrease in thermostability."
FT /evidence="ECO:0000269|PubMed:10966804"
FT MUTAGEN 155
FT /note="N->X: Decrease in thermostability."
FT /evidence="ECO:0000269|PubMed:10966804"
FT MUTAGEN 162
FT /note="H->I,V: Increase in thermostability."
FT /evidence="ECO:0000269|PubMed:2394736"
FT MUTAGEN 162
FT /note="H->P: Great decrease in thermostability."
FT /evidence="ECO:0000269|PubMed:2394736"
FT MUTAGEN 162
FT /note="H->V: Great increase in thermostability; when
FT associated with F-219; V-238; S-293 and Y-294."
FT /evidence="ECO:0000269|PubMed:2394736"
FT MUTAGEN 175
FT /note="R->X: No effect on thermostability."
FT /evidence="ECO:0000269|PubMed:10966804"
FT MUTAGEN 193
FT /note="D->A,C,E,H,R: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10966804"
FT MUTAGEN 201
FT /note="N->H,K: Increase in thermostability."
FT /evidence="ECO:0000269|PubMed:10966804"
FT MUTAGEN 201
FT /note="N->R: Great increase in thermostability."
FT /evidence="ECO:0000269|PubMed:10966804"
FT MUTAGEN 207
FT /note="Q->X: No effect on thermostability."
FT /evidence="ECO:0000269|PubMed:10966804"
FT MUTAGEN 217
FT /note="N->P: Great increase in thermostability."
FT /evidence="ECO:0000269|PubMed:10966804"
FT MUTAGEN 219
FT /note="N->A,E,Q,P,S: Great decrease in thermostability."
FT /evidence="ECO:0000269|PubMed:10966804"
FT MUTAGEN 219
FT /note="N->F: Great increase in thermostability. Great
FT increase in thermostability; when associated with V-162; V-
FT 238; S-293 and Y-294."
FT /evidence="ECO:0000269|PubMed:10966804"
FT MUTAGEN 219
FT /note="N->L: Increase in thermostability."
FT /evidence="ECO:0000269|PubMed:10966804"
FT MUTAGEN 221
FT /note="N->X: Great decrease in thermostability."
FT /evidence="ECO:0000269|PubMed:10966804"
FT MUTAGEN 229
FT /note="D->X: Great decrease in thermostability."
FT /evidence="ECO:0000269|PubMed:10966804"
FT MUTAGEN 233
FT /note="D->X: Great decrease in thermostability."
FT /evidence="ECO:0000269|PubMed:10966804"
FT MUTAGEN 238
FT /note="A->V: Increase in thermostability. Great increase in
FT thermostability; when associated with V-162; F-219; S-293
FT and Y-294."
FT /evidence="ECO:0000269|PubMed:8771184"
FT MUTAGEN 276
FT /note="H->X: No effect on thermostability."
FT /evidence="ECO:0000269|PubMed:2394736"
FT MUTAGEN 292
FT /note="W->L: Decrease in activity; when associated with Y-
FT 315."
FT /evidence="ECO:0000269|PubMed:12915728"
FT MUTAGEN 293
FT /note="Q->S: Increase in thermostability; when associated
FT with Y-294. Great increase in thermostability; when
FT associated with V-162; F-219; V-238 and Y-294."
FT /evidence="ECO:0000269|PubMed:12736372"
FT MUTAGEN 294
FT /note="N->Y: Increase in thermostability; when associated
FT with S-293. Great increase in thermostability; when
FT associated with V-162; F-219; V-238 and S-293."
FT /evidence="ECO:0000269|PubMed:12736372"
FT MUTAGEN 298
FT /note="A->H,K,L,Q,R: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10966804"
FT MUTAGEN 300
FT /note="E->X: No effect on thermostability."
FT /evidence="ECO:0000269|PubMed:10966804"
FT MUTAGEN 315
FT /note="V->F: Decrease in activity."
FT /evidence="ECO:0000269|PubMed:12915728"
FT MUTAGEN 315
FT /note="V->Y: Increase in activity. Decrease in activity;
FT when associated with L-292."
FT /evidence="ECO:0000269|PubMed:12915728"
FT MUTAGEN 322
FT /note="H->X: No effect on thermostability."
FT /evidence="ECO:0000269|PubMed:2394736"
FT MUTAGEN 359
FT /note="Q->X: No effect on thermostability."
FT /evidence="ECO:0000269|PubMed:10966804"
FT MUTAGEN 365
FT /note="E->H: Loss of activity."
FT /evidence="ECO:0000269|PubMed:10966804"
FT MUTAGEN 435
FT /note="H->X: No effect on thermostability."
FT /evidence="ECO:0000269|PubMed:2394736"
FT MUTAGEN 479
FT /note="H->X: No effect on thermostability."
FT /evidence="ECO:0000269|PubMed:2394736"
FT CONFLICT 4
FT /note="Q -> H (in Ref. 4; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 13
FT /note="T -> P (in Ref. 3; AAO26743 and 4; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="N -> I (in Ref. 6; AAA22232)"
FT /evidence="ECO:0000305"
FT CONFLICT 38
FT /note="Q -> Y (in Ref. 8; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 48
FT /note="G -> R (in Ref. 4; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 62..64
FT /note="AEH -> VED (in Ref. 4; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 68..69
FT /note="AV -> VA (in Ref. 4; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="P -> S (in Ref. 4; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 81
FT /note="A -> D (in Ref. 3; AAO26743 and 4; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 105..117
FT /note="Missing (in Ref. 4; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 117
FT /note="K -> N (in Ref. 3; AAO26743)"
FT /evidence="ECO:0000305"
FT CONFLICT 158
FT /note="I -> T (in Ref. 3; AAO26743)"
FT /evidence="ECO:0000305"
FT CONFLICT 162
FT /note="H -> Q (in Ref. 3; AAO26743)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="R -> L (in Ref. 2; AAA22240)"
FT /evidence="ECO:0000305"
FT CONFLICT 171
FT /note="H -> Q (in Ref. 3; AAO26743)"
FT /evidence="ECO:0000305"
FT CONFLICT 218
FT /note="E -> V (in Ref. 3; AAO26743)"
FT /evidence="ECO:0000305"
FT CONFLICT 237..238
FT /note="VA -> AT (in Ref. 3; AAO26743)"
FT /evidence="ECO:0000305"
FT CONFLICT 339
FT /note="S -> G (in Ref. 2; AAA22240 and 3; AAO26743)"
FT /evidence="ECO:0000305"
FT CONFLICT 347
FT /note="L -> V (in Ref. 3; AAO26743)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="A -> S (in Ref. 2; AAA22240)"
FT /evidence="ECO:0000305"
FT CONFLICT 385
FT /note="S -> A (in Ref. 3; AAO26743)"
FT /evidence="ECO:0000305"
FT CONFLICT 390
FT /note="V -> I (in Ref. 3; AAO26743)"
FT /evidence="ECO:0000305"
FT CONFLICT 401
FT /note="D -> A (in Ref. 3; AAO26743)"
FT /evidence="ECO:0000305"
FT CONFLICT 421
FT /note="K -> I (in Ref. 3; AAO26743)"
FT /evidence="ECO:0000305"
FT CONFLICT 464
FT /note="A -> T (in Ref. 3; AAO26743)"
FT /evidence="ECO:0000305"
FT CONFLICT 487..488
FT /note="EP -> DS (in Ref. 3; AAO26743)"
FT /evidence="ECO:0000305"
FT CONFLICT 493
FT /note="S -> A (in Ref. 3; AAO26743)"
FT /evidence="ECO:0000305"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:1VJS"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:1VJS"
FT HELIX 50..56
FT /evidence="ECO:0007829|PDB:1VJS"
FT HELIX 58..63
FT /evidence="ECO:0007829|PDB:1VJS"
FT STRAND 68..70
FT /evidence="ECO:0007829|PDB:1VJS"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:1VJS"
FT HELIX 109..121
FT /evidence="ECO:0007829|PDB:1VJS"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:1VJS"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:1VJS"
FT STRAND 139..149
FT /evidence="ECO:0007829|PDB:1VJS"
FT STRAND 151..153
FT /evidence="ECO:0007829|PDB:1VJS"
FT STRAND 162..170
FT /evidence="ECO:0007829|PDB:1VJS"
FT TURN 173..177
FT /evidence="ECO:0007829|PDB:1VJS"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:1VJS"
FT STRAND 189..193
FT /evidence="ECO:0007829|PDB:1VJS"
FT TURN 196..199
FT /evidence="ECO:0007829|PDB:1VJS"
FT STRAND 204..206
FT /evidence="ECO:0007829|PDB:1VJS"
FT TURN 207..209
FT /evidence="ECO:0007829|PDB:1BPL"
FT STRAND 213..215
FT /evidence="ECO:0007829|PDB:1OB0"
FT HELIX 223..226
FT /evidence="ECO:0007829|PDB:1VJS"
FT STRAND 228..230
FT /evidence="ECO:0007829|PDB:1VJS"
FT HELIX 235..252
FT /evidence="ECO:0007829|PDB:1VJS"
FT STRAND 256..259
FT /evidence="ECO:0007829|PDB:1VJS"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:1VJS"
FT HELIX 267..281
FT /evidence="ECO:0007829|PDB:1VJS"
FT STRAND 286..289
FT /evidence="ECO:0007829|PDB:1VJS"
FT HELIX 296..305
FT /evidence="ECO:0007829|PDB:1VJS"
FT TURN 306..308
FT /evidence="ECO:0007829|PDB:1VJS"
FT STRAND 310..313
FT /evidence="ECO:0007829|PDB:1VJS"
FT HELIX 315..326
FT /evidence="ECO:0007829|PDB:1VJS"
FT TURN 327..329
FT /evidence="ECO:0007829|PDB:1VJS"
FT HELIX 333..337
FT /evidence="ECO:0007829|PDB:1VJS"
FT STRAND 338..340
FT /evidence="ECO:0007829|PDB:1VJS"
FT HELIX 341..344
FT /evidence="ECO:0007829|PDB:1VJS"
FT HELIX 346..348
FT /evidence="ECO:0007829|PDB:1VJS"
FT STRAND 349..353
FT /evidence="ECO:0007829|PDB:1BPL"
FT TURN 356..358
FT /evidence="ECO:0007829|PDB:1VJS"
FT TURN 370..372
FT /evidence="ECO:0007829|PDB:1VJS"
FT HELIX 373..382
FT /evidence="ECO:0007829|PDB:1VJS"
FT STRAND 383..386
FT /evidence="ECO:0007829|PDB:1VJS"
FT STRAND 389..391
FT /evidence="ECO:0007829|PDB:1VJS"
FT HELIX 392..396
FT /evidence="ECO:0007829|PDB:1VJS"
FT STRAND 401..404
FT /evidence="ECO:0007829|PDB:1VJS"
FT HELIX 410..422
FT /evidence="ECO:0007829|PDB:1VJS"
FT STRAND 428..431
FT /evidence="ECO:0007829|PDB:1VJS"
FT STRAND 434..442
FT /evidence="ECO:0007829|PDB:1VJS"
FT STRAND 453..460
FT /evidence="ECO:0007829|PDB:1VJS"
FT STRAND 463..468
FT /evidence="ECO:0007829|PDB:1VJS"
FT HELIX 471..473
FT /evidence="ECO:0007829|PDB:1VJS"
FT STRAND 477..480
FT /evidence="ECO:0007829|PDB:1VJS"
FT STRAND 495..501
FT /evidence="ECO:0007829|PDB:1VJS"
FT STRAND 506..510
FT /evidence="ECO:0007829|PDB:1VJS"
SQ SEQUENCE 512 AA; 58549 MW; D8BB77759CD4C482 CRC64;
MKQQKRLYAR LLTLLFALIF LLPHSAAAAA NLNGTLMQYF EWYMPNDGQH WKRLQNDSAY
LAEHGITAVW IPPAYKGTSQ ADVGYGAYDL YDLGEFHQKG TVRTKYGTKG ELQSAIKSLH
SRDINVYGDV VINHKGGADA TEDVTAVEVD PADRNRVISG EHRIKAWTHF HFPGRGSTYS
DFKWHWYHFD GTDWDESRKL NRIYKFQGKA WDWEVSNENG NYDYLMYADI DYDHPDVAAE
IKRWGTWYAN ELQLDGFRLD AVKHIKFSFL RDWVNHVREK TGKEMFTVAE YWQNDLGALE
NYLNKTNFNH SVFDVPLHYQ FHAASTQGGG YDMRKLLNST VVSKHPLKAV TFVDNHDTQP
GQSLESTVQT WFKPLAYAFI LTRESGYPQV FYGDMYGTKG DSQREIPALK HKIEPILKAR
KQYAYGAQHD YFDHHDIVGW TREGDSSVAN SGLAALITDG PGGAKRMYVG RQNAGETWHD
ITGNRSEPVV INSEGWGEFH VNGGSVSIYV QR
