ID   AMY_CLOAB               Reviewed;         760 AA.
AC   P23671; Q9S429;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   29-AUG-2001, sequence version 2.
DT   27-MAR-2024, entry version 141.
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; Synonyms=amyP; OrderedLocusNames=CA_P0168;
OS   Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / LMG 5710
OS   / VKM B-1787).
OG   Plasmid pSOL1.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=272562;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RA   Schaffer S., Duerre P.;
RT   "Nucleotide sequence analysis and ECF sigma factor-dependent expression of
RT   an alpha-amylase gene from Clostridium acetobutylicum DSM 792.";
RL   Submitted (MAR-1999) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RA   Sabathe F., Cornillot E., Croux C., Soucaille P.;
RT   "Molecular characterization of amyP, a pSOL1 located gene coding the major
RT   alpha-amylase of Clostridium acetobutylicum ATCC824, and its use as a
RT   reporter system for strain degeneration.";
RL   Submitted (JUN-1999) to the EMBL/GenBank/DDBJ databases.
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=11466286; DOI=10.1128/jb.183.16.4823-4838.2001;
RA   Noelling J., Breton G., Omelchenko M.V., Makarova K.S., Zeng Q., Gibson R.,
RA   Lee H.M., Dubois J., Qiu D., Hitti J., Wolf Y.I., Tatusov R.L., Sabathe F.,
RA   Doucette-Stamm L.A., Soucaille P., Daly M.J., Bennett G.N., Koonin E.V.,
RA   Smith D.R.;
RT   "Genome sequence and comparative analysis of the solvent-producing
RT   bacterium Clostridium acetobutylicum.";
RL   J. Bacteriol. 183:4823-4838(2001).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 292-760.
RC   STRAIN=ATCC 824 / DSM 792 / JCM 1419 / LMG 5710 / VKM B-1787;
RX   PubMed=2254264; DOI=10.1128/jb.172.12.6907-6918.1990;
RA   Gerischer U., Duerre P.;
RT   "Cloning, sequencing, and molecular analysis of the acetoacetate
RT   decarboxylase gene region from Clostridium acetobutylicum.";
RL   J. Bacteriol. 172:6907-6918(1990).
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; M55392; AAA63759.2; -; Genomic_DNA.
DR   EMBL; AF164199; AAD47072.1; -; Genomic_DNA.
DR   EMBL; AE001438; AAK76913.1; -; Genomic_DNA.
DR   PIR; B37837; B37837.
DR   RefSeq; NP_149331.1; NC_001988.2.
DR   RefSeq; WP_010890852.1; NC_001988.2.
DR   AlphaFoldDB; P23671; -.
DR   SMR; P23671; -.
DR   CAZy; CBM25; Carbohydrate-Binding Module Family 25.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   GeneID; 45000393; -.
DR   KEGG; cac:CA_P0168; -.
DR   PATRIC; fig|272562.8.peg.169; -.
DR   HOGENOM; CLU_013336_4_1_9; -.
DR   OrthoDB; 9761789at2; -.
DR   Proteomes; UP000000814; Plasmid pSOL1.
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:2001070; F:starch binding; IEA:InterPro.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd11315; AmyAc_bac1_AmyA; 1.
DR   CDD; cd02688; E_set; 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; 3.
DR   InterPro; IPR031319; A-amylase_C.
DR   InterPro; IPR006046; Alpha_amylase.
DR   InterPro; IPR005085; CBM25.
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   PANTHER; PTHR43447; ALPHA-AMYLASE; 1.
DR   PANTHER; PTHR43447:SF49; ALPHA-AMYLASE; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF16760; CBM53; 3.
DR   PRINTS; PR00110; ALPHAAMYLASE.
DR   SMART; SM00642; Aamy; 1.
DR   SMART; SM00632; Aamy_C; 1.
DR   SMART; SM01066; CBM_25; 3.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   3: Inferred from homology;
KW   Calcium; Carbohydrate metabolism; Glycosidase; Hydrolase; Metal-binding;
KW   Plasmid; Reference proteome; Signal.
FT   SIGNAL          1..34
FT                   /evidence="ECO:0000255"
FT   CHAIN           35..760
FT                   /note="Alpha-amylase"
FT                   /id="PRO_0000001338"
FT   ACT_SITE        222
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000250"
FT   ACT_SITE        262
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250"
FT   BINDING         143
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         184
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         192
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   BINDING         226
FT                   /ligand="Ca(2+)"
FT                   /ligand_id="ChEBI:CHEBI:29108"
FT                   /evidence="ECO:0000250"
FT   SITE            321
FT                   /note="Transition state stabilizer"
FT                   /evidence="ECO:0000250"
FT   CONFLICT        213
FT                   /note="D -> H (in Ref. 1; AAA63759)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        222
FT                   /note="D -> H (in Ref. 1; AAA63759)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        571
FT                   /note="A -> G (in Ref. 1; AAA63759)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   760 AA;  83045 MW;  10E146F40252F6D0 CRC64;
     MSKRSKLLKR RMLSLSVICV LIGYGPVFNP VRSQAKVMTY SSENRELPEN TKDGVMLHAF
     DWSFNNIKKE LPSIAAAGYK AVQVSPVQGT KSNSTNSSDW WLLYQPTNQA IGNAQLGSYD
     DFKSLCSEAK NYGISIVVDV VMNHMANNGN DDEVASEVDP SFKDPSLYHH NGQCTDWNNR
     QDVTQEGIGM PDLNTQSSAV QSKAITFLNQ CVDAGATGFR FDAAKHIETD LGLDANKSWS
     GNYWENVLGS LHNKSNLYIY GEVLQDGKVD NISAYESFMN VEASAYDGSL RGAIKSGDLT
     NAQGMGGLDS NKCVDMLETH DEYEHNESKD LTDWQRKAGW AIAASRAGSV PLFFDRPTGN
     IGSEGDALWK DSDVVAVNEF HNAMAGQNEY LRLQNNNKAM IIERGSKGAV IVNEGDSFNL
     NTPTNLEDGN YDNHGSATDS LTVSQGRMTG TVPANSIIVI YNKNSNPGSD RVTLSEQAAK
     AGDSVTITYD AGTTALKDAS NVNLYWGYDG FSAATSKAMT SLGDNKWQTT ITVPKEVTKN
     VNFSFTDGTS WDNNNGANWN IPLASNYLPH AGYKVDYDSS NLVSGNNFTI YYNGNLANSS
     NVSLHWGVNG WSNMQNLAMV KDSNGFWEAT IAIPASSNTL NFCFTNGSSW DNNNNNNWTL
     NTWSSVPKVQ VTPAPEACKQ ISVYYNGSLA SSASNITLHW GCNGFTSPQD INMVKQADGR
     WLANITLPSG CYNVNMAFKD QSGTWDNNNS NNYNFSSTNN
//