ID Q8I9P8_9BIVA Unreviewed; 699 AA.
AC Q8I9P8;
DT 01-MAR-2003, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2004, sequence version 2.
DT 24-JAN-2024, entry version 107.
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=Amy {ECO:0000313|EMBL:AAO17927.2};
OS Corbicula fluminea.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Mollusca; Bivalvia;
OC Autobranchia; Heteroconchia; Euheterodonta; Imparidentia; Neoheterodontei;
OC Venerida; Cyrenoidea; Cyrenidae; Corbicula.
OX NCBI_TaxID=45949 {ECO:0000313|EMBL:AAO17927.2};
RN [1] {ECO:0000313|EMBL:AAO17927.2}
RP NUCLEOTIDE SEQUENCE.
RA Da Lage J.-L., Van Wormhoudt A., Cariou M.-L.;
RT "Diversity and evolution of the alpha-amylase genes in Animals.";
RL Biologia 57:181-189(2002).
RN [2] {ECO:0000313|EMBL:AAO17927.2}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=14704857; DOI=10.1007/s00018-003-3334-y;
RA Da Lage J.L., Feller G., Janecek S.;
RT "Horizontal gene transfer from Eukarya to bacteria and domain shuffling:
RT the alpha-amylase model.";
RL Cell. Mol. Life Sci. 61:97-109(2004).
RN [3] {ECO:0000313|EMBL:AAO17927.2}
RP NUCLEOTIDE SEQUENCE.
RA Da Lage J.-L.;
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
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}.
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DR EMBL; AF468016; AAO17927.2; -; Genomic_DNA.
DR AlphaFoldDB; Q8I9P8; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
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 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.
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 Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..699
FT /note="Alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004308505"
FT DOMAIN 28..390
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT DOMAIN 398..478
FT /note="Alpha-amylase C-terminal"
FT /evidence="ECO:0000259|SMART:SM00632"
FT REGION 474..511
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 699 AA; 76544 MW; 25D57008165B04CB CRC64;
MSAWFLLAAS IVGVCWCAYT DPHCDGKQVI VHLFEWKWPD VALECERFLS KKGFCGVQVS
PANEHVMVNS PPRPWWERYQ PVSYKLHSRS GTEAEFTDMV QRCKAVGVRI FVDVVINHMA
GLGRTGTGTA GSSFDSSNYN FPGVPFVREH FNPYCKLNNY GDPNQVRNCY LVDLTDLDQG
NEYVRNKIAA FLNQMIDIGV AGFRVDAAKH MWPKDIDAIQ QKLKDLPEGG RPFFYHEVID
QSNEPIKTSQ YTSLGYVTEF RYCLKIREGI QDFGRLGQAV DYGWGMTDSE HAFVFVDNHD
NQRGHGGGGN IITHEKPKEY KMAVAFLLAN DYGFTRVMSS YYFGDNSDLG PPHNDDYSAK
DVPINADGTC GNGWVCEHRW RPIANMVAFK NAVAGTQKGN YYNMNNQIAF SRGNKGFFAM
ARDSHMDATL QTGLPAGEYC ELISDCARKI AVDGSGNAHI VINNNEEPII AFIVGGPSSG
SGSGTGGGSS SGGGTQPADT TPSGPLPTAP AGWSRTVVLM ERQTSVGQDL FIRGGLDHKT
HTGCTSDAAT SACSIPIRVR PLGTGSHYDR YNAWSAHDDH LDWYGAEANQ GRYNGAMAQG
TPALWTTNSA GQAGHSDLNT YGQHYWLVDV DMDCSKTDNG WFELKAVVNN EWEGNVPAGT
CTGSGAGAPT AQTGNHWARC GMMNVFHFNS ASCEIKSLP
//
