AMY_ACASI
ID AMY_ACASI Reviewed; 517 AA.
AC B0KZK1;
DT 03-JUL-2019, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 1.
DT 03-AUG-2022, entry version 70.
DE RecName: Full=Alpha-amylase {ECO:0000255, ECO:0000255|RuleBase:RU361134, ECO:0000303|PubMed:22292590};
DE EC=3.2.1.1 {ECO:0000255, ECO:0000255|RuleBase:RU361134, ECO:0000269|PubMed:22292590};
DE AltName: Full=1,4-alpha-D-glucan glucanohydrolase {ECO:0000305};
DE AltName: Allergen=Aca s 4 {ECO:0000303|PubMed:22292590};
DE Flags: Precursor;
OS Acarus siro (Flour mite) (Tyroglyphus farinae).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Chelicerata; Arachnida; Acari;
OC Acariformes; Sarcoptiformes; Astigmata; Acaroidea; Acaridae; Acarinae;
OC Acarus.
OX NCBI_TaxID=66546 {ECO:0000312|EMBL:ABL09312.1};
RN [1] {ECO:0000312|EMBL:ABL09312.1}
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Tan C.L., Chew F.T.;
RT "Isolation and characterization of group 4 allergen from Acarus siro.";
RL Submitted (AUG-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP PROTEIN SEQUENCE OF 22-34; 35-44; 60-90; 170-178; 221-263; 273-280;
RP 322-337; 356-364; 444-458 AND 502-515, IDENTIFICATION BY MASS SPECTROMETRY,
RP 3D-STRUCTURE MODELING, CATALYTIC ACTIVITY, ACTIVITY REGULATION,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND ALLERGEN.
RX PubMed=22292590; DOI=10.1186/1471-2091-13-3;
RA Pytelkova J., Lepsik M., Sanda M., Talacko P., Maresova L., Mares M.;
RT "Enzymatic activity and immunoreactivity of Aca s 4, an alpha-amylase
RT allergen from the storage mite Acarus siro.";
RL BMC Biochem. 13:3-3(2012).
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:0000255|RuleBase:RU361134,
CC ECO:0000269|PubMed:22292590};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000250|UniProtKB:P56634};
CC Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250|UniProtKB:P56634};
CC -!- COFACTOR:
CC Name=chloride; Xref=ChEBI:CHEBI:17996;
CC Evidence={ECO:0000250|UniProtKB:P56634};
CC Note=Binds 1 Cl(-) ion per subunit. {ECO:0000250|UniProtKB:P56634};
CC -!- ACTIVITY REGULATION: Activated by chloride ions. Inhibited by acarbose.
CC Not inhibited by wheat alpha-amylase inhibitors 1 (WI-1, the tetrameric
CC form) or 3 (WI-3, the monomeric form) and bean alpha-amylase inhibitor
CC 1 (alphaAI-1). {ECO:0000269|PubMed:22292590}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6.5. Active in slightly acidic to neutral pH range.
CC {ECO:0000269|PubMed:22292590};
CC -!- SUBUNIT: Monomer. {ECO:0000250|UniProtKB:P56634}.
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305|PubMed:22292590}.
CC -!- ALLERGEN: Causes an allergic reaction in human. Binds to IgE of
CC patients allergic to house dust mite. {ECO:0000269|PubMed:22292590}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000255|RuleBase:RU003615, ECO:0000305}.
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DR EMBL; DQ979807; ABL09312.1; -; mRNA.
DR AlphaFoldDB; B0KZK1; -.
DR SMR; B0KZK1; -.
DR BindingDB; B0KZK1; -.
DR Allergome; 9894; Aca s 4.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004556; F:alpha-amylase activity; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; ISS:UniProtKB.
DR GO; GO:0031404; F:chloride ion binding; ISS:UniProtKB.
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 Allergen; Calcium; Carbohydrate metabolism; Chloride;
KW Direct protein sequencing; Disulfide bond; Glycosidase; Hydrolase;
KW Metal-binding; Secreted; Signal.
FT SIGNAL 1..21
FT /evidence="ECO:0000255, ECO:0000269|PubMed:22292590"
FT CHAIN 22..517
FT /note="Alpha-amylase"
FT /evidence="ECO:0000255, ECO:0000305|PubMed:22292590"
FT /id="PRO_5002751170"
FT ACT_SITE 217
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT ACT_SITE 253
FT /note="Proton donor"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 122
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 178
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 187
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 215
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 221
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT BINDING 355
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT SITE 318
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000250|UniProtKB:P04746"
FT DISULFID 52..108
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT DISULFID 397..403
FT /evidence="ECO:0000250|UniProtKB:P56634"
FT DISULFID 470..482
FT /evidence="ECO:0000250|UniProtKB:P56634"
SQ SEQUENCE 517 AA; 58092 MW; 88D3C9AC850BCD85 CRC64;
MAHLLLAVVA ITLALSQSVF GGSPYSNPHF TGSRSVITHL MQWKFDDIAA ECERFLGPKG
YGGIQLSPVN EHAVLGNRPW YELYQPVGYK IQSRSGNEEQ FKGMVQRCNK VGVRIYVDIV
MNHMSGAQEG HGNCWFKLQW HHDVSRCSLL VPNDFHGRES CHTDNMDIKN YDNPEEARNC
RLSGLRDLKQ SSEYVRQKQA DFLNHLIDLG VAGSRSDASK HMWPGDLEAI YGKLHNLNTA
YFPANSRPFI YHEVIYYGGD GIKSSDYTKL GRAIEFHFYR DIANVVRRHN QLKTVKNFGQ
PWGMVPSDDA LVMVDSHDLQ RFHTGQVGVN INYFESRLLK VATAFMLAWP YGVPRVMSSY
HWDQKIEDGK DKNDWIGPPS DGSGNILSVT PQPDDTCNKE WICEHRWRQI YNMVHFRNVA
GNEAVSHWWD NGDYQIAFGR GSKAFIAINL QDGQGLNRKL ATGLPQGTYC DLVTGNLAGG
KCTGGTVTVD GSGNADINIA KTAEDPFVAI HVEAKLH
