AMY_BACAM
ID AMY_BACAM Reviewed; 514 AA.
AC P00692;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1988, sequence version 1.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=Alpha-amylase;
DE EC=3.2.1.1 {ECO:0000250|UniProtKB:P29957};
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE Flags: Precursor;
OS Bacillus amyloliquefaciens (Bacillus velezensis).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus amyloliquefaciens group.
OX NCBI_TaxID=1390;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=IH;
RX PubMed=6185474; DOI=10.1016/s0021-9258(18)33151-x;
RA Takkinen K., Pettersson R.F., Kalkkinen N., Palva I., Soederlund H.,
RA Kaeaeriaeinen L.;
RT "Amino acid sequence of alpha-amylase from Bacillus amyloliquefaciens
RT deduced from the nucleotide sequence of the cloned gene.";
RL J. Biol. Chem. 258:1007-1013(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-96.
RX PubMed=6170539; DOI=10.1016/0378-1119(81)90103-7;
RA Palva I., Pettersson R.F., Kalkkinen N., Lehtovaara P., Sarvas M.,
RA Soederlund H., Takkinen K., Kaeaeriaeinen L.;
RT "Nucleotide sequence of the promoter and NH2-terminal signal peptide region
RT of the alpha-amylase gene from Bacillus amyloliquefaciens.";
RL Gene 15:43-51(1981).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-39, AND SUBCELLULAR LOCATION.
RX PubMed=2830166; DOI=10.1016/0378-1119(87)90324-6;
RA Ruohonen L., Hackman P., Lehtovaara P., Knowles J.K.C., Karaenen S.;
RT "Efficient secretion of Bacillus amyloliquefaciens alpha-amylase by its own
RT signal peptide from Saccharomyces cerevisiae host cells.";
RL Gene 59:161-170(1987).
RN [4]
RP PROTEIN SEQUENCE OF 32-222.
RX PubMed=6156671; DOI=10.1042/bj1850387;
RA Chung H.S., Friedberg F.;
RT "Sequence of the N-terminal half of Bacillus amyloliquefaciens alpha-
RT amylase.";
RL Biochem. J. 185:387-395(1980).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (1.70 ANGSTROMS) OF 32-331 IN COMPLEX WITH
RP CARBOHYDRATE; SODIUM AND CALCIUM, AND COFACTOR.
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 [6] {ECO:0007744|PDB:3BH4}
RP X-RAY CRYSTALLOGRAPHY (1.40 ANGSTROMS) OF 32-514 IN COMPLEX WITH CALCIUM,
RP AND COFACTOR.
RX PubMed=20124706; DOI=10.1107/s1744309109051938;
RA Alikhajeh J., Khajeh K., Ranjbar B., Naderi-Manesh H., Lin Y.H., Liu E.,
RA Guan H.H., Hsieh Y.C., Chuankhayan P., Huang Y.C., Jeyaraman J., Liu M.Y.,
RA Chen C.J.;
RT "Structure of Bacillus amyloliquefaciens alpha-amylase at high resolution:
RT implications for thermal stability.";
RL Acta Crystallogr. F 66:121-129(2010).
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:0000250|UniProtKB:P29957};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000269|PubMed:10924103, ECO:0000269|PubMed:20124706};
CC Note=Binds 3 Ca(2+) ions per subunit. {ECO:0000269|PubMed:10924103,
CC ECO:0000269|PubMed:20124706};
CC -!- COFACTOR:
CC Name=Na(+); Xref=ChEBI:CHEBI:29101;
CC Evidence={ECO:0000269|PubMed:10924103};
CC Note=Binds 1 sodium ion per subunit. {ECO:0000269|PubMed:10924103};
CC -!- SUBUNIT: Monomer.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2830166}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR EMBL; J01542; AAA22191.1; -; mRNA.
DR EMBL; V00092; CAA23430.1; -; Genomic_DNA.
DR EMBL; M18424; AAA22192.1; -; Genomic_DNA.
DR PIR; A92389; ALBSN.
DR RefSeq; WP_013352208.1; NZ_CP054415.1.
DR PDB; 1E3X; X-ray; 1.90 A; A=32-514.
DR PDB; 1E3Z; X-ray; 1.93 A; A=32-514.
DR PDB; 1E40; X-ray; 2.20 A; A=32-514.
DR PDB; 1E43; X-ray; 1.70 A; A=32-514.
DR PDB; 3BH4; X-ray; 1.40 A; A/B=32-514.
DR PDBsum; 1E3X; -.
DR PDBsum; 1E3Z; -.
DR PDBsum; 1E40; -.
DR PDBsum; 1E43; -.
DR PDBsum; 3BH4; -.
DR AlphaFoldDB; P00692; -.
DR SMR; P00692; -.
DR STRING; 692420.BAMF_1635; -.
DR DrugBank; DB03773; alpha-D-quinovopyranose.
DR DrugBank; DB02379; Beta-D-Glucose.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR OMA; SVAKYYK; -.
DR BRENDA; 3.2.1.1; 630.
DR EvolutionaryTrace; P00692; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
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..31
FT /evidence="ECO:0000269|PubMed:6156671"
FT CHAIN 32..514
FT /note="Alpha-amylase"
FT /id="PRO_0000001330"
FT ACT_SITE 262
FT /note="Nucleophile"
FT ACT_SITE 292
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:10924103,
FT ECO:0000269|PubMed:20124706, ECO:0007744|PDB:1E40"
FT BINDING 190
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10924103,
FT ECO:0000269|PubMed:20124706, ECO:0007744|PDB:1E40"
FT BINDING 190
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:10924103,
FT ECO:0007744|PDB:1E40"
FT BINDING 212
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10924103,
FT ECO:0000269|PubMed:20124706, ECO:0007744|PDB:1E40"
FT BINDING 214
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10924103,
FT ECO:0000269|PubMed:20124706, ECO:0007744|PDB:1E40"
FT BINDING 214
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:10924103,
FT ECO:0007744|PDB:1E40"
FT BINDING 225
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10924103,
FT ECO:0000269|PubMed:20124706, ECO:0007744|PDB:1E40"
FT BINDING 225
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:10924103,
FT ECO:0007744|PDB:1E40"
FT BINDING 231
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10924103,
FT ECO:0000269|PubMed:20124706, ECO:0007744|PDB:1E40"
FT BINDING 231
FT /ligand="Na(+)"
FT /ligand_id="ChEBI:CHEBI:29101"
FT /evidence="ECO:0000269|PubMed:10924103,
FT ECO:0007744|PDB:1E40"
FT BINDING 233
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10924103,
FT ECO:0000269|PubMed:20124706, ECO:0007744|PDB:1E40"
FT BINDING 235
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000269|PubMed:10924103,
FT ECO:0000269|PubMed:20124706, ECO:0007744|PDB:1E40"
FT BINDING 266
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000269|PubMed:10924103,
FT ECO:0000269|PubMed:20124706, ECO:0007744|PDB:1E40"
FT BINDING 331
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:20124706,
FT ECO:0007744|PDB:3BH4"
FT BINDING 438
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:20124706,
FT ECO:0007744|PDB:3BH4"
FT BINDING 461
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="3"
FT /evidence="ECO:0000269|PubMed:20124706,
FT ECO:0007744|PDB:3BH4"
FT SITE 359
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250"
FT CONFLICT 54
FT /note="L -> I (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 64
FT /note="I -> L (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 79
FT /note="S -> D (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT CONFLICT 84
FT /note="G -> S (in Ref. 4; AA sequence)"
FT /evidence="ECO:0000305"
FT STRAND 36..38
FT /evidence="ECO:0007829|PDB:3BH4"
FT STRAND 46..48
FT /evidence="ECO:0007829|PDB:3BH4"
FT HELIX 50..64
FT /evidence="ECO:0007829|PDB:3BH4"
FT STRAND 68..71
FT /evidence="ECO:0007829|PDB:3BH4"
FT STRAND 75..79
FT /evidence="ECO:0007829|PDB:3BH4"
FT STRAND 84..89
FT /evidence="ECO:0007829|PDB:3BH4"
FT STRAND 101..103
FT /evidence="ECO:0007829|PDB:1E43"
FT HELIX 109..121
FT /evidence="ECO:0007829|PDB:3BH4"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:3BH4"
FT STRAND 133..135
FT /evidence="ECO:0007829|PDB:3BH4"
FT STRAND 139..150
FT /evidence="ECO:0007829|PDB:3BH4"
FT STRAND 153..157
FT /evidence="ECO:0007829|PDB:3BH4"
FT STRAND 162..170
FT /evidence="ECO:0007829|PDB:3BH4"
FT TURN 173..177
FT /evidence="ECO:0007829|PDB:3BH4"
FT HELIX 186..188
FT /evidence="ECO:0007829|PDB:3BH4"
FT STRAND 189..195
FT /evidence="ECO:0007829|PDB:3BH4"
FT TURN 196..199
FT /evidence="ECO:0007829|PDB:3BH4"
FT STRAND 200..206
FT /evidence="ECO:0007829|PDB:3BH4"
FT STRAND 208..210
FT /evidence="ECO:0007829|PDB:1E43"
FT STRAND 215..217
FT /evidence="ECO:0007829|PDB:3BH4"
FT STRAND 228..232
FT /evidence="ECO:0007829|PDB:3BH4"
FT HELIX 237..254
FT /evidence="ECO:0007829|PDB:3BH4"
FT STRAND 258..261
FT /evidence="ECO:0007829|PDB:3BH4"
FT HELIX 264..266
FT /evidence="ECO:0007829|PDB:3BH4"
FT HELIX 269..283
FT /evidence="ECO:0007829|PDB:3BH4"
FT STRAND 288..291
FT /evidence="ECO:0007829|PDB:3BH4"
FT HELIX 298..307
FT /evidence="ECO:0007829|PDB:3BH4"
FT TURN 308..310
FT /evidence="ECO:0007829|PDB:3BH4"
FT STRAND 312..315
FT /evidence="ECO:0007829|PDB:3BH4"
FT HELIX 317..328
FT /evidence="ECO:0007829|PDB:3BH4"
FT TURN 329..331
FT /evidence="ECO:0007829|PDB:3BH4"
FT HELIX 335..337
FT /evidence="ECO:0007829|PDB:3BH4"
FT TURN 338..341
FT /evidence="ECO:0007829|PDB:3BH4"
FT HELIX 343..346
FT /evidence="ECO:0007829|PDB:3BH4"
FT HELIX 348..350
FT /evidence="ECO:0007829|PDB:3BH4"
FT STRAND 351..355
FT /evidence="ECO:0007829|PDB:3BH4"
FT TURN 358..360
FT /evidence="ECO:0007829|PDB:3BH4"
FT TURN 372..374
FT /evidence="ECO:0007829|PDB:3BH4"
FT HELIX 375..383
FT /evidence="ECO:0007829|PDB:3BH4"
FT STRAND 384..393
FT /evidence="ECO:0007829|PDB:3BH4"
FT HELIX 394..398
FT /evidence="ECO:0007829|PDB:3BH4"
FT STRAND 403..405
FT /evidence="ECO:0007829|PDB:1E3X"
FT HELIX 412..424
FT /evidence="ECO:0007829|PDB:3BH4"
FT STRAND 430..433
FT /evidence="ECO:0007829|PDB:3BH4"
FT STRAND 436..444
FT /evidence="ECO:0007829|PDB:3BH4"
FT STRAND 455..462
FT /evidence="ECO:0007829|PDB:3BH4"
FT STRAND 465..470
FT /evidence="ECO:0007829|PDB:3BH4"
FT HELIX 473..475
FT /evidence="ECO:0007829|PDB:3BH4"
FT STRAND 479..482
FT /evidence="ECO:0007829|PDB:3BH4"
FT STRAND 490..492
FT /evidence="ECO:0007829|PDB:3BH4"
FT STRAND 497..503
FT /evidence="ECO:0007829|PDB:3BH4"
FT STRAND 508..513
FT /evidence="ECO:0007829|PDB:3BH4"
SQ SEQUENCE 514 AA; 58403 MW; 3DE66B3FB5CCDE7E CRC64;
MIQKRKRTVS FRLVLMCTLL FVSLPITKTS AVNGTLMQYF EWYTPNDGQH WKRLQNDAEH
LSDIGITAVW IPPAYKGLSQ SDNGYGPYDL YDLGEFQQKG TVRTKYGTKS ELQDAIGSLH
SRNVQVYGDV VLNHKAGADA TEDVTAVEVN PANRNQETSE EYQIKAWTDF RFPGRGNTYS
DFKWHWYHFD GADWDESRKI SRIFKFRGEG KAWDWEVSSE NGNYDYLMYA DVDYDHPDVV
AETKKWGIWY ANELSLDGFR IDAAKHIKFS FLRDWVQAVR QATGKEMFTV AEYWQNNAGK
LENYLNKTSF NQSVFDVPLH FNLQAASSQG GGYDMRRLLD GTVVSRHPEK AVTFVENHDT
QPGQSLESTV QTWFKPLAYA FILTRESGYP QVFYGDMYGT KGTSPKEIPS LKDNIEPILK
ARKEYAYGPQ HDYIDHPDVI GWTREGDSSA AKSGLAALIT DGPGGSKRMY AGLKNAGETW
YDITGNRSDT VKIGSDGWGE FHVNDGSVSI YVQK
