ID A0A2J5HH61_9EURO Unreviewed; 491 AA.
AC A0A2J5HH61;
DT 28-MAR-2018, integrated into UniProtKB/TrEMBL.
DT 28-MAR-2018, sequence version 1.
DT 27-MAR-2024, entry version 19.
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 ORFNames=BDW42DRAFT_22821 {ECO:0000313|EMBL:PLN76326.1};
OS Aspergillus taichungensis.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus.
OX NCBI_TaxID=482145 {ECO:0000313|EMBL:PLN76326.1, ECO:0000313|Proteomes:UP000235023};
RN [1] {ECO:0000313|Proteomes:UP000235023}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 19404 {ECO:0000313|Proteomes:UP000235023};
RG DOE Joint Genome Institute;
RA Mondo S.J., Kjaerbolling I., Vesth T.C., Frisvad J.C., Nybo J.L.,
RA Theobald S., Kuo A., Bowyer P., Matsuda Y., Lyhne E.K., Kogle M.E.,
RA Clum A., Lipzen A., Salamov A., Ngan C.Y., Daum C., Chiniquy J., Barry K.,
RA LaButti K., Haridas S., Simmons B.A., Magnuson J.K., Mortensen U.H.,
RA Larsen T.O., Grigoriev I.V., Baker S.E., Andersen M.R., Nordberg H.P.,
RA Cantor M.N., Hua S.X.;
RL Submitted (DEC-2017) 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 -!- 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; KZ559621; PLN76326.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2J5HH61; -.
DR OrthoDB; 3249969at2759; -.
DR Proteomes; UP000235023; Unassembled WGS sequence.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016052; P:carbohydrate catabolic process; IEA:InterPro.
DR CDD; cd11319; AmyAc_euk_AmyA; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
DR InterPro; IPR013777; A-amylase-like.
DR InterPro; IPR015340; A_amylase_C_dom.
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; PTHR10357:SF215; ALPHA-AMYLASE 1; 1.
DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR Pfam; PF09260; A_amylase_dom_C; 1.
DR Pfam; PF00128; Alpha-amylase; 1.
DR PIRSF; PIRSF001024; Alph-amyl_fung; 1.
DR PRINTS; PR00110; ALPHAAMYLASE.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|PIRSR:PIRSR001024-3};
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW Disulfide bond {ECO:0000256|PIRSR:PIRSR001024-4};
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|PIRSR:PIRSR001024-3};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..15
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 16..491
FT /note="Alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5014410176"
FT DOMAIN 28..384
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
FT ACT_SITE 221
FT /note="Nucleophile"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-1"
FT ACT_SITE 245
FT /note="Proton donor"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-1"
FT BINDING 98
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT BINDING 136
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-3"
FT BINDING 137
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT BINDING 177
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-3"
FT BINDING 190
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-3"
FT BINDING 219
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT BINDING 221
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-3"
FT BINDING 225
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="1"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-3"
FT BINDING 245
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /ligand_label="2"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-3"
FT BINDING 249
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT BINDING 312
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT BINDING 359
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-5"
FT SITE 312
FT /note="Transition state stabilizer"
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-2"
FT DISULFID 45..53
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-4"
FT DISULFID 165..179
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-4"
FT DISULFID 255..298
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-4"
FT DISULFID 455..490
FT /evidence="ECO:0000256|PIRSR:PIRSR001024-4"
SQ SEQUENCE 491 AA; 54237 MW; F99651179A0ED1BC CRC64;
MRLSLWSLLV GTTLAATPAE WKSQSIYFLL TDRFARTDGS TEEPCDTDAR KYCGGTWQGI
IKKLDYIQNM GFTAIWITPV TSQIKDTTAY GDAYHGYWQQ DINSLEEHYG KPEDLTALSD
ALHERGMYLM VDVVANHMGY KGAGNSVDYS IFTPFNKQEY FHDYCPIKNY DDPTQSEQCW
LGDDKVALPD LNTESEEVKN IWYEWVGNLV KKYKIDGLRI DTVKHVQKEF WKGYNEAAGV
YCVGEVLDGD VDNICSYQEV LDGLLNYPIY YPLINAFKAP GGSMSELANM ITTVQEKCKD
ANLLGSFVDN HDNPRFASYT KDIALAKNIA AYSILADGIP IIYAGQEQHF SGGEDPANRE
ATWTSGYDTE NELYKVIASS NKVRNLAIKQ DKTYVDSKTK AIFSDDSSIA ISKGAEGSQI
VTVLTNKGES GGEQTVEVTG TGYESGTELT DVISCTPVKA GDNGSVSVPL KSGAPAVLYP
TKKLADSKIC A
//
