ID   AMY_BUTFI               Reviewed;         976 AA.
AC   P30269;
DT   01-APR-1993, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1993, sequence version 1.
DT   03-AUG-2022, entry version 93.
DE   RecName: Full=Alpha-amylase;
DE            EC=3.2.1.1;
DE   AltName: Full=1,4-alpha-D-glucan glucanohydrolase;
DE   Flags: Precursor;
GN   Name=amyA;
OS   Butyrivibrio fibrisolvens.
OC   Bacteria; Firmicutes; Clostridia; Eubacteriales; Lachnospiraceae;
OC   Butyrivibrio.
OX   NCBI_TaxID=831;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=H17C;
RX   PubMed=2061294; DOI=10.1128/jb.173.13.4203-4211.1991;
RA   Rumbak E., Rawlings D.E., Lindsey G.G., Woods D.R.;
RT   "Cloning, nucleotide sequence, and enzymatic characterization of an alpha-
RT   amylase from the ruminal bacterium Butyrivibrio fibrisolvens H17c.";
RL   J. Bacteriol. 173:4203-4211(1991).
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;
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108; Evidence={ECO:0000250};
CC       Note=Binds 1 Ca(2+) ion per subunit. {ECO:0000250};
CC   -!- SUBUNIT: Monomer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family. {ECO:0000305}.
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DR   EMBL; M62507; AAA23005.1; -; Genomic_DNA.
DR   PIR; A42466; A42466.
DR   AlphaFoldDB; P30269; -.
DR   SMR; P30269; -.
DR   CAZy; CBM26; Carbohydrate-Binding Module Family 26.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 2.60.40.10; -; 3.
DR   Gene3D; 2.60.40.1180; -; 1.
DR   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR031965; CBM26.
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   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF16738; CBM26; 2.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; SSF51445; 1.
PE   3: Inferred from homology;
KW   Calcium; Carbohydrate metabolism; Glycosidase; Hydrolase; Metal-binding;
KW   Signal.
FT   SIGNAL          1..33
FT                   /evidence="ECO:0000255"
FT   CHAIN           34..976
FT                   /note="Alpha-amylase"
FT                   /id="PRO_0000001337"
FT   REGION          45..98
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        323
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        375
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         243
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         284
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         293
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         327
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   SITE            447
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   976 AA;  106695 MW;  61D690FDC19315AC CRC64;
     MKRGKLWGRL VSAAGLSLSI FLSSIGNVST AYAMESNDAL VLDETKENTE SATDASSNEA
     SDAEADNDTD EAITDASSKE LSAENDGASE SDSSFDEYDH TALPETDEIT VTAAGELSTA
     KAELYTLAPR EAREADNSLV TRDSIHDGAI LHAFCWSFNT IADNMADIAD AGYTAVQTSP
     INECLSTNPG MNLHGPDGMW YYHYQPTDWV IGNYQLGSRD EFKHMCDVAD EYGVAVIVDI
     LPNHTTPSTG SIAKALMEAA GGSDALYHAT GKIGGGYTDR LELTYYSMGG LPDVDTENTG
     FQQYFYEFLK DCVYLGADGF RIDTAKHISL PDDPVPSDYS DAGRNTFYPN MREALNEYSE
     EVGTKSYDEL FVYGEVLQGT NDRLAAYQQY IGGTTASNYG SSLRSALSSG NLSVNRLLDY
     QIYDDTAYGS TYTADTEKLV TWVESHDNYM NDSESCWKSI DDDMVIMGWS IIAARDAGTP
     LFFSRPNNSS AENPYGDNLI GAAGSPIYKA PEVKAVNLFR EKMGEADEYL SNPGGNIQTL
     MIERYNDTVQ GAVIVNAAQT RTTISTETHL SDGIYPDQVE GSNSVFLVKD GVLSGSVEGE
     GVVVLSEKMD GTGKVVSFYN NKNWNGVVAR VDNAEETLDT IDENDGWFQV TVLDDEFTIR
     FESADGKEVS PEFQITAESG TFATPDSSEL YYSKAEAEEG LGIHTYPVYF FNTENWGSVY
     TYGWLDGGAQ LFGGWPGTVA VNEGSGWYRA DVKTTGEITA FNLIFNNGNG IQTVNVEGIT
     PDSKDIYLAV DAEKSNGQLI VNRYEDKESA EKALGVSGSY TTAYFYNTEG WDKVCAYTWG
     ATALGDWPGK ELTQDEDGWY SVVLPAGPSE DLNIIFNNGN NGKQTNDMKI SDMKYRFILN
     NGISYQKYGS KKDAMEAIAG AGDVTYETVY FYNEKADDAN WKNVYLYVFG GTDGEYNNLV
     GTWPGKLMEK EEDSNG