ID   AMY_PSEHA               Reviewed;         669 AA.
AC   P29957;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   30-MAY-2000, sequence version 3.
DT   03-MAY-2023, entry version 126.
DE   RecName: Full=Alpha-amylase;
DE            EC=3.2.1.1 {ECO:0000269|PubMed:1544904};
DE   AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE   Flags: Precursor;
GN   Name=amy;
OS   Pseudoalteromonas haloplanktis (Alteromonas haloplanktis).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC   Pseudoalteromonadaceae; Pseudoalteromonas.
OX   NCBI_TaxID=228;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 25-64 AND 471-477,
RP   CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, AND BIOPHYSICOCHEMICAL
RP   PROPERTIES.
RC   STRAIN=A23;
RX   PubMed=1544904; DOI=10.1016/s0021-9258(18)42754-8;
RA   Feller G., Lonhienne T., Deroanne C., Libioulle C., van Beeumen J.,
RA   Gerday C.;
RT   "Purification, characterization, and nucleotide sequence of the
RT   thermolabile alpha-amylase from the antarctic psychrotroph Alteromonas
RT   haloplanctis A23.";
RL   J. Biol. Chem. 267:5217-5221(1992).
RN   [2]
RP   SEQUENCE REVISION.
RC   STRAIN=A23;
RX   PubMed=9575155; DOI=10.1074/jbc.273.20.12109;
RA   Feller G., D'Amico S., Benotmane A.M., Joly F., van Beeumen J., Gerday C.;
RT   "Characterization of the C-terminal propeptide involved in bacterial wall
RT   spanning of alpha-amylase from the psychrophile Alteromonas haloplanctis.";
RL   J. Biol. Chem. 273:12109-12115(1998).
RN   [3]
RP   X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS) OF 25-477 IN COMPLEX WITH CALCIUM
RP   AND CHLORIDE, AND DISULFIDE BONDS.
RC   STRAIN=A23;
RX   PubMed=9541387; DOI=10.1002/pro.5560070304;
RA   Aghajari N., Feller G., Gerday C., Haser R.;
RT   "Crystal structures of the psychrophilic alpha-amylase from Alteromonas
RT   haloplanctis in its native form and complexed with an inhibitor.";
RL   Protein Sci. 7:564-572(1998).
RN   [4]
RP   X-RAY CRYSTALLOGRAPHY (1.74 ANGSTROMS) OF 25-472 IN COMPLEX WITH
RP   OLIGOSACCHARIDE; CHLORIDE AND CALCIUM, ACTIVE SITE, COFACTOR, AND DISULFIDE
RP   BONDS.
RX   PubMed=11914073; DOI=10.1021/bi0160516;
RA   Aghajari N., Roth M., Haser R.;
RT   "Crystallographic evidence of a transglycosylation reaction: ternary
RT   complexes of a psychrophilic alpha-amylase.";
RL   Biochemistry 41:4273-4280(2002).
RN   [5]
RP   X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 25-472 IN COMPLEXES WITH CALCIUM,
RP   COFACTOR, ACTIVITY REGULATION, MUTAGENESIS OF LYS-324, AND DISULFIDE BONDS.
RX   PubMed=12021442; DOI=10.1110/ps.0202602;
RA   Aghajari N., Feller G., Gerday C., Haser R.;
RT   "Structural basis of alpha-amylase activation by chloride.";
RL   Protein Sci. 11:1435-1441(2002).
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:1544904};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000269|PubMed:12021442};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000269|PubMed:11914073,
CC       ECO:0000269|PubMed:12021442, ECO:0000269|PubMed:9541387};
CC   -!- COFACTOR:
CC       Name=chloride; Xref=ChEBI:CHEBI:17996;
CC         Evidence={ECO:0000269|PubMed:12021442};
CC       Note=Binds 1 Cl(-) ion per subunit. {ECO:0000269|PubMed:11914073,
CC       ECO:0000269|PubMed:12021442, ECO:0000269|PubMed:9541387};
CC   -!- ACTIVITY REGULATION: Requires chloride ions for optimal activity.
CC       {ECO:0000269|PubMed:12021442}.
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Temperature dependence:
CC         Thermolabile. {ECO:0000269|PubMed:1544904};
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:11914073}.
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:1544904}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR   EMBL; X58627; CAA41481.1; -; Genomic_DNA.
DR   PIR; S23257; S23257.
DR   PDB; 1AQH; X-ray; 2.00 A; A=25-477.
DR   PDB; 1AQM; X-ray; 1.85 A; A=25-477.
DR   PDB; 1B0I; X-ray; 2.40 A; A=25-477.
DR   PDB; 1G94; X-ray; 1.74 A; A=25-472.
DR   PDB; 1G9H; X-ray; 1.80 A; A=25-472.
DR   PDB; 1JD7; X-ray; 2.25 A; A=25-477.
DR   PDB; 1JD9; X-ray; 2.50 A; A=25-477.
DR   PDB; 1KXH; X-ray; 2.30 A; A=25-472.
DR   PDB; 1L0P; X-ray; 2.10 A; A=25-472.
DR   PDBsum; 1AQH; -.
DR   PDBsum; 1AQM; -.
DR   PDBsum; 1B0I; -.
DR   PDBsum; 1G94; -.
DR   PDBsum; 1G9H; -.
DR   PDBsum; 1JD7; -.
DR   PDBsum; 1JD9; -.
DR   PDBsum; 1KXH; -.
DR   PDBsum; 1L0P; -.
DR   AlphaFoldDB; P29957; -.
DR   SMR; P29957; -.
DR   DrugBank; DB04164; 1,4-Deoxy-4-((5-Hydroxymethyl-2,3,4-Trihydroxycyclohex-5-Enyl)Amino)Fructose.
DR   DrugBank; DB02379; Beta-D-Glucose.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   BRENDA; 3.2.1.1; 5081.
DR   SABIO-RK; P29957; -.
DR   EvolutionaryTrace; P29957; -.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd11317; AmyAc_bac_euk_AmyA; 1.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR   InterPro; IPR006048; A-amylase/branching_C.
DR   InterPro; IPR031319; A-amylase_C.
DR   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR43447; ALPHA-AMYLASE; 1.
DR   PANTHER; PTHR43447:SF49; ALPHA-AMYLASE; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF02806; Alpha-amylase_C; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SMART; SM00632; Aamy_C; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Calcium; Carbohydrate metabolism; Chloride;
KW   Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW   Metal-binding; Secreted; Signal.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000269|PubMed:1544904"
FT   CHAIN           25..477
FT                   /note="Alpha-amylase"
FT                   /id="PRO_0000001328"
FT   PROPEP          478..669
FT                   /note="Removed in mature form"
FT                   /id="PRO_0000001329"
FT   ACT_SITE        198
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000269|PubMed:11914073"
FT   ACT_SITE        224
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000269|PubMed:11914073"
FT   BINDING         71..75
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|PubMed:11914073"
FT   BINDING         112
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000269|PubMed:11914073,
FT                   ECO:0000269|PubMed:12021442, ECO:0000269|PubMed:9541387,
FT                   ECO:0007744|PDB:1AQH"
FT   BINDING         113
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|PubMed:11914073"
FT   BINDING         159
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000269|PubMed:11914073,
FT                   ECO:0000269|PubMed:12021442, ECO:0000269|PubMed:9541387,
FT                   ECO:0007744|PDB:1AQH"
FT   BINDING         168
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000269|PubMed:11914073,
FT                   ECO:0000269|PubMed:12021442, ECO:0000269|PubMed:9541387,
FT                   ECO:0007744|PDB:1AQH"
FT   BINDING         196
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000269|PubMed:11914073,
FT                   ECO:0000269|PubMed:9541387, ECO:0007744|PDB:1AQH"
FT   BINDING         196
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         201..202
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|PubMed:11914073"
FT   BINDING         202
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000269|PubMed:11914073,
FT                   ECO:0000269|PubMed:12021442, ECO:0000269|PubMed:9541387,
FT                   ECO:0007744|PDB:1AQH"
FT   BINDING         231
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|PubMed:11914073"
FT   BINDING         286
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000269|PubMed:9541387,
FT                   ECO:0007744|PDB:1AQH"
FT   BINDING         288
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|PubMed:11914073"
FT   BINDING         293
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000305|PubMed:11914073"
FT   BINDING         324
FT                   /ligand="chloride"
FT                   /ligand_id="ChEBI:CHEBI:17996"
FT                   /evidence="ECO:0000269|PubMed:11914073,
FT                   ECO:0000269|PubMed:9541387, ECO:0007744|PDB:1AQH"
FT   SITE            288
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   DISULFID        44..98
FT                   /evidence="ECO:0000269|PubMed:11914073,
FT                   ECO:0000269|PubMed:12021442, ECO:0000269|PubMed:9541387,
FT                   ECO:0007744|PDB:1AQH"
FT   DISULFID        144..161
FT                   /evidence="ECO:0000269|PubMed:11914073,
FT                   ECO:0000269|PubMed:12021442, ECO:0000269|PubMed:9541387,
FT                   ECO:0007744|PDB:1AQH"
FT   DISULFID        352..359
FT                   /evidence="ECO:0000269|PubMed:11914073,
FT                   ECO:0000269|PubMed:12021442, ECO:0000269|PubMed:9541387,
FT                   ECO:0007744|PDB:1AQH"
FT   DISULFID        426..440
FT                   /evidence="ECO:0000269|PubMed:11914073,
FT                   ECO:0000269|PubMed:12021442, ECO:0000269|PubMed:9541387,
FT                   ECO:0007744|PDB:1AQH"
FT   MUTAGEN         324
FT                   /note="K->Q: Abolishes chloride binding and reduces
FT                   catalytic rate."
FT                   /evidence="ECO:0000269|PubMed:12021442"
FT   STRAND          29..32
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   HELIX           37..46
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   HELIX           48..51
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   STRAND          55..58
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   STRAND          67..69
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   HELIX           70..74
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   STRAND          75..77
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   STRAND          79..81
FT                   /evidence="ECO:0007829|PDB:1JD7"
FT   HELIX           88..100
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   STRAND          104..110
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   STRAND          112..114
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   STRAND          119..121
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   STRAND          126..128
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   HELIX           137..139
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   HELIX           150..153
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   HELIX           155..160
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   STRAND          161..163
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   STRAND          167..169
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   HELIX           174..190
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   STRAND          194..198
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   HELIX           200..202
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   HELIX           205..213
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   STRAND          215..217
FT                   /evidence="ECO:0007829|PDB:1AQH"
FT   STRAND          220..223
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   HELIX           235..241
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   STRAND          242..245
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   HELIX           247..259
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   HELIX           262..267
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   HELIX           270..272
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   HELIX           277..279
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   STRAND          280..282
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   HELIX           289..291
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   TURN            292..294
FT                   /evidence="ECO:0007829|PDB:1KXH"
FT   HELIX           302..305
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   HELIX           306..317
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   STRAND          320..327
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   STRAND          344..346
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   STRAND          352..357
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   HELIX           360..362
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   HELIX           364..375
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   TURN            376..378
FT                   /evidence="ECO:0007829|PDB:1B0I"
FT   STRAND          383..387
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   STRAND          389..396
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   HELIX           398..400
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   STRAND          401..406
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   STRAND          408..410
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   STRAND          415..417
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   STRAND          422..426
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   TURN            428..430
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   STRAND          440..442
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   STRAND          444..447
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   STRAND          451..454
FT                   /evidence="ECO:0007829|PDB:1G94"
FT   STRAND          461..466
FT                   /evidence="ECO:0007829|PDB:1G94"
SQ   SEQUENCE   669 AA;  73268 MW;  E3DD316D92B91EB7 CRC64;
     MKLNKIITTA GLSLGLLLPS IATATPTTFV HLFEWNWQDV AQECEQYLGP KGYAAVQVSP
     PNEHITGSQW WTRYQPVSYE LQSRGGNRAQ FIDMVNRCSA AGVDIYVDTL INHMAAGSGT
     GTAGNSFGNK SFPIYSPQDF HESCTINNSD YGNDRYRVQN CELVGLADLD TASNYVQNTI
     AAYINDLQAI GVKGFRFDAS KHVAASDIQS LMAKVNGSPV VFQEVIDQGG EAVGASEYLS
     TGLVTEFKYS TELGNTFRNG SLAWLSNFGE GWGFMPSSSA VVFVDNHDNQ RGHGGAGNVI
     TFEDGRLYDL ANVFMLAYPY GYPKVMSSYD FHGDTDAGGP NVPVHNNGNL ECFASNWKCE
     HRWSYIAGGV DFRNNTADNW AVTNWWDNTN NQISFGRGSS GHMAINKEDS TLTATVQTDM
     ASGQYCNVLK GELSADAKSC SGEVITVNSD GTINLNIGAW DAMAIHKNAK LNTSSASSTE
     SDWQRTVIFI NAQTQSGQDM FIRGGIDHAY ANANLGRNCQ TSNFECAMPI RHNNLKNVTT
     SPWKANDNYL DWYGIENGQS SEAEGSATDW TTNVWPAGWG AEKTVNTDGF GVTPLNIWGE
     HYWMLDVDMD CSKAVNGWFE LKAFIKNGQG WETAIAQDNA PYTSTNHMAQ CGKINKFEFN
     NSGVVIRSF
//