AMY_CLOAB
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 03-AUG-2022, entry version 136.
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; Firmicutes; 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 EnsemblBacteria; AAK76913; AAK76913; CA_P0168.
DR GeneID; 45000393; -.
DR KEGG; cac:CA_P0168; -.
DR PATRIC; fig|272562.8.peg.169; -.
DR HOGENOM; CLU_013336_4_1_9; -.
DR OMA; FHNAMVG; -.
DR OrthoDB; 99080at2; -.
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 Gene3D; 2.60.40.10; -; 3.
DR Gene3D; 2.60.40.1180; -; 1.
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 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; SSF51445; 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
