ID   F1S574_PIG              Unreviewed;       511 AA.
AC   F1S574; I3LAV8;
DT   03-MAY-2011, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 3.
DT   27-MAR-2024, entry version 101.
DE   RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595, ECO:0000256|RuleBase:RU361134};
GN   Name=AMY2 {ECO:0000313|Ensembl:ENSSSCP00000007308.3};
GN   Synonyms=LOC100521789 {ECO:0000313|Ensembl:ENSSSCP00000021176.2};
OS   Sus scrofa (Pig).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Laurasiatheria; Artiodactyla; Suina; Suidae; Sus.
OX   NCBI_TaxID=9823 {ECO:0000313|Ensembl:ENSSSCP00000007308.3, ECO:0000313|Proteomes:UP000008227};
RN   [1] {ECO:0000313|Ensembl:ENSSSCP00000007308.3, ECO:0000313|Proteomes:UP000008227}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Duroc {ECO:0000313|Ensembl:ENSSSCP00000007308.3,
RC   ECO:0000313|Proteomes:UP000008227};
RG   Porcine genome sequencing project;
RL   Submitted (NOV-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:HDA93438.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=30723633; DOI=.7717/peerj.6374;
RA   Gilbert D.G.;
RT   "Genes of the pig, Sus scrofa, reconstructed with EvidentialGene.";
RL   PeerJ 7:E6374-E6374(2019).
RN   [3] {ECO:0000313|Ensembl:ENSSSCP00000007308.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
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:0000256|ARBA:ARBA00000548,
CC         ECO:0000256|RuleBase:RU361134};
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- COFACTOR:
CC       Name=chloride; Xref=ChEBI:CHEBI:17996;
CC         Evidence={ECO:0000256|ARBA:ARBA00001923};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; DQIR01137962; HDA93438.1; -; Transcribed_RNA.
DR   EMBL; DQIR01289550; HDC45028.1; -; Transcribed_RNA.
DR   Ensembl; ENSSSCT00000007507.5; ENSSSCP00000007308.3; ENSSSCG00000036331.3.
DR   Ensembl; ENSSSCT00000025528.4; ENSSSCP00000021176.2; ENSSSCG00000028277.4.
DR   GeneTree; ENSGT00940000154802; -.
DR   HOGENOM; CLU_013336_2_1_1; -.
DR   OMA; FRYAYDL; -.
DR   OrthoDB; 3249969at2759; -.
DR   TreeFam; TF312850; -.
DR   Reactome; R-SSC-189085; Digestion of dietary carbohydrate.
DR   Proteomes; UP000008227; Chromosome 4.
DR   Bgee; ENSSSCG00000028277; Expressed in semimembranosus muscle and 30 other cell types or tissues.
DR   GO; GO:0005615; C:extracellular space; IBA:GO_Central.
DR   GO; GO:0004556; F:alpha-amylase activity; IBA:GO_Central.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IBA:GO_Central.
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.
DR   Genevisible; I3LAV8; SS.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW   Chloride {ECO:0000256|ARBA:ARBA00023214};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361134};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU361134};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Pyrrolidone carboxylic acid {ECO:0000256|ARBA:ARBA00023283};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008227};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..15
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           16..511
FT                   /note="Alpha-amylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5015090507"
FT   DOMAIN          26..413
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   DOMAIN          422..510
FT                   /note="Alpha-amylase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM00632"
SQ   SEQUENCE   511 AA;  57130 MW;  E1218CB52086C37E CRC64;
     MKLFLLLSAF GFCWAQYAPQ TQSGRTSIVH LFEWRWVDIA LECERYLGPK GFGGVQVSPP
     NENIVVTNPS RPWWERYQPV SYKLCTRSGN ENEFRDMVTR CNNVGVRIYV DAVINHMCGS
     GAAAGTGTTC GSYCNPGNRE FPAVPYSAWD FNDGKCKTAS GGIESYNDPY QVRDCQLVGL
     LDLALEKDYV RSMIADYLNK LIDIGVAGFR IDASKHMWPG DIKAVLDKLH NLNTNWFPAG
     SRPFIFQEVI DLGGEAIQSS EYFGNGRVTE FKYGAKLGTV VRKWSGEKMS YLKNWGEGWG
     FMPSDRALVF VDNHDNQRGH GAGGASILTF WDARLYKVAV GFMLAHPYGF TRVMSSYRWA
     RNFVNGQDVN DWIGPPNNNG VIKEVTINAD TTCGNDWVCE HRWRQIRNMV WFRNVVDGQP
     FANWWDNGSN QVAFGRGNRG FIVFNNDDWQ LSSTLQTGLP GGTYCDVISG DKVGNSCTGI
     KVYVSSDGTA QFSISNSAED PFIAIHAESK L
//