ID   A0KGI8_AERHH            Unreviewed;       858 AA.
AC   A0KGI8;
DT   12-DEC-2006, integrated into UniProtKB/TrEMBL.
DT   12-DEC-2006, sequence version 1.
DT   27-MAR-2024, entry version 108.
DE   RecName: Full=Alpha-amylase {ECO:0000256|ARBA:ARBA00017303, ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   OrderedLocusNames=AHA_0837 {ECO:0000313|EMBL:ABK39061.1};
OS   Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC
OS   13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC   Aeromonadaceae; Aeromonas.
OX   NCBI_TaxID=380703 {ECO:0000313|EMBL:ABK39061.1, ECO:0000313|Proteomes:UP000000756};
RN   [1] {ECO:0000313|EMBL:ABK39061.1, ECO:0000313|Proteomes:UP000000756}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 /
RC   KCTC 2358 / NCIMB 9240 / NCTC 8049
RC   {ECO:0000313|Proteomes:UP000000756};
RX   PubMed=16980456; DOI=10.1128/JB.00621-06;
RA   Seshadri R., Joseph S.W., Chopra A.K., Sha J., Shaw J., Graf J., Haft D.,
RA   Wu M., Ren Q., Rosovitz M.J., Madupu R., Tallon L., Kim M., Jin S.,
RA   Vuong H., Stine O.C., Ali A., Horneman A.J., Heidelberg J.F.;
RT   "Genome sequence of Aeromonas hydrophila ATCC 7966T: jack of all trades.";
RL   J. Bacteriol. 188:8272-8282(2006).
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}.
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; CP000462; ABK39061.1; -; Genomic_DNA.
DR   RefSeq; WP_011704783.1; NC_008570.1.
DR   RefSeq; YP_855379.1; NC_008570.1.
DR   AlphaFoldDB; A0KGI8; -.
DR   STRING; 380703.AHA_0837; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   EnsemblBacteria; ABK39061; ABK39061; AHA_0837.
DR   KEGG; aha:AHA_0837; -.
DR   PATRIC; fig|380703.7.peg.836; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_369072_0_0_6; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000000756; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:InterPro.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0007156; P:homophilic cell adhesion via plasma membrane adhesion molecules; IEA:InterPro.
DR   CDD; cd11317; AmyAc_bac_euk_AmyA; 1.
DR   Gene3D; 2.60.40.3620; -; 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; IPR002126; Cadherin-like_dom.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
DR   InterPro; IPR013780; Glyco_hydro_b.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   InterPro; IPR007110; Ig-like_dom.
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; PS50268; CADHERIN_2; 1.
DR   PROSITE; PS50835; IG_LIKE; 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   Reference proteome {ECO:0000313|Proteomes:UP000000756};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..858
FT                   /note="Alpha-amylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002625709"
FT   DOMAIN          551..667
FT                   /note="Cadherin"
FT                   /evidence="ECO:0000259|PROSITE:PS50268"
FT   DOMAIN          577..661
FT                   /note="Ig-like"
FT                   /evidence="ECO:0000259|PROSITE:PS50835"
FT   DOMAIN          577..660
FT                   /note="PKD"
FT                   /evidence="ECO:0000259|PROSITE:PS50093"
SQ   SEQUENCE   858 AA;  91578 MW;  E526803D9E6AF656 CRC64;
     MHSTLLRTAL LTAALGSFSH TATAEGVMVH LFQWKFNDIA NECETVLGPK GFGGVQITPP
     AEHKQGSQVW WTVYQPVSFK NFNSFGGSEA ELRSMIARCN AAGVKVYADA VFNQLASGSG
     TATGGGSYNA GQYQYPQFGY NDFHHSGDIT NYGDSNNVWN GALYGMPDLN TGSPYVQDQI
     ATYMKTLLGW GVAGFRIDAA KHMAPTDVKA ILDKAGSPKA YLEVIGAGGE SPDIQPGRYT
     YIDTVTDFKY GTDLAANFNG QIKNLKTLGE SWGLLPSAKA FVFVVNHDRE RGHGGGGMLT
     FMSGARYDLA NTFMIAWPYG WKQVMSGYRF ENMSTYETDK GAPGSTPCTD SQWNCEQRRP
     TIMNMALFHN RTEGQPVSNW WDNGNNQIAF GRGDKGFVAI NNESGSLVAS LQTALPAGEY
     CNLLGGNDYC SGGYVTVDGS GKASLNVPGM KAAAIIAGCT KASPCGGSAL PGTKFSSMNL
     RGTHNAWGNT PMTVDANRVW SATLTLTGNG DATGAQRFKF DVFGNWAENY GDNEGDGIAD
     KGSSKDILVS GAGSYRITLN ESDLRYTVTP LTSNQAPVAA LSPKTLSVKA GESVVFDASA
     SHDDGGVVSY SWSSGGTAAT ETVRFDTPGT YTVTVTVTDA EGLTASASAT VTVTDDNGTY
     TSVLPTLNFR GTPNAWGSLA MTLVADNQWE ALVTFNGQAN QRFKFDVKGD WSKNYGDTNK
     DGVAELAGSD ILTSVTGQYR VRFNDQTLQY SLTPVSVGYA KNFASLNIRG TTNNWGSTPM
     SLVGDHLWQA SVTFTGSGDG NGGQRFKFDV KGDWTQNYGD TNRDGVAEQA GADITTALVG
     VYVVRFNDQT LAYSLNAQ
//