AMY_PSEHA
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-AUG-2022, entry version 123.
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; Proteobacteria; 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 Gene3D; 2.60.40.1180; -; 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 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; SSF51445; 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
