ID   A4SRA2_AERS4            Unreviewed;       754 AA.
AC   A4SRA2;
DT   15-MAY-2007, integrated into UniProtKB/TrEMBL.
DT   15-MAY-2007, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00017303, ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   Name=amyA {ECO:0000313|EMBL:ABO91424.1};
GN   OrderedLocusNames=ASA_3455 {ECO:0000313|EMBL:ABO91424.1};
OS   Aeromonas salmonicida (strain A449).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=382245 {ECO:0000313|EMBL:ABO91424.1, ECO:0000313|Proteomes:UP000000225};
RN   [1] {ECO:0000313|Proteomes:UP000000225}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=A449 {ECO:0000313|Proteomes:UP000000225};
RX   PubMed=18801193; DOI=10.1186/1471-2164-9-427;
RA   Reith M.E., Singh R.K., Curtis B., Boyd J.M., Bouevitch A., Kimball J.,
RA   Munholland J., Murphy C., Sarty D., Williams J., Nash J.H., Johnson S.C.,
RA   Brown L.L.;
RT   "The genome of Aeromonas salmonicida subsp. salmonicida A449: insights into
RT   the evolution of a fish pathogen.";
RL   BMC Genomics 9:427-427(2008).
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
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DR   EMBL; CP000644; ABO91424.1; -; Genomic_DNA.
DR   RefSeq; WP_005318926.1; NC_009348.1.
DR   AlphaFoldDB; A4SRA2; -.
DR   STRING; 29491.GCA_000820065_04341; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; asa:ASA_3455; -.
DR   PATRIC; fig|382245.13.peg.3445; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_369072_0_0_6; -.
DR   Proteomes; UP000000225; Chromosome.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
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   Gene3D; 2.60.40.10; Immunoglobulins; 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   InterPro; IPR013783; Ig-like_fold.
DR   InterPro; IPR022409; PKD/Chitinase_dom.
DR   InterPro; IPR000601; PKD_dom.
DR   InterPro; IPR035986; PKD_dom_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   Pfam; PF18911; PKD_4; 1.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SMART; SM00632; Aamy_C; 1.
DR   SMART; SM00089; PKD; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
DR   SUPFAM; SSF49299; PKD domain; 1.
DR   PROSITE; PS50093; PKD; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
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   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..754
FT                   /note="Alpha-amylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002672584"
FT   DOMAIN          576..653
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
SQ   SEQUENCE   754 AA;  81391 MW;  53C2E21F9A0FA89E CRC64;
     MHNTLFQTAM LTAVLSSFSH TATAEGVMVH LFQWKFNDIA NECENVLGPK GFGSVQITPP
     AEHKQGSQVW WTVYQPVSFK NFNSHGGNEA ELKSMIARCN AAGVKIYADA VFNQLASGTG
     TATGGGSYNS GQYQYPQFGY NDFHHSGDIT NYGDSNNVWN GALYGMPDLK TESPYVQDQI
     ATYMKTLLGW GVAGFRVDAA KHMAPADVKA ILVKAGSPKA YLEVIGAGGE SAEIQPNRYT
     HIDTVTEFKY GTDLAANFNG KIKNLKTLGE SWGLLPSDKS FIFVVNHDRE RGHGGGGMLT
     FMNGARYELA NVFMMAWPYG WKQVMSGYRF ENMGTYETDK GAPGSTPCSD TQWNCEQRRP
     QIMNMAMFHN QTKDLPVNNW WDNGNNQIAF SRGNKGFVAI NNESGNLVAS VQTGLPAGEY
     CNILSGNDYC SGAYIKVDGS GKAGLNLAGM KAAAILASCT KAAPCGGVIP GNRFSSLNLR
     GTHNAWGNTA MQVDDNRIWS AIINFTGAGD TSGAQRFKFD VFGNWTENYG DNEGDGIADK
     GRTRDIYFNG AGQYRIALKE SDLSYTVTAL SNNQAPVAVI SPKKPSVKLG ESLVFDASGS
     TDDAGVASYS WSTGGIGKTE TVQFDTLGSR TVTVTVTDTE GLTASVSATV HVTDGSGAYT
     SELPTLHFRG TPNGWGVLAM TLVADNQWEA RVTFDGQTNQ RFKFDVKGDW SQNYGDTNKD
     GVAELTGADI TTPVVGAYVV RFNDQTLTYS LNAQ
//