ID A5I276_CLOBH Unreviewed; 554 AA.
AC A5I276; A7G3X6;
DT 26-JUN-2007, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2007, sequence version 1.
DT 27-MAR-2024, entry version 109.
DE RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN Name=malL {ECO:0000313|EMBL:CAL83141.1};
GN OrderedLocusNames=CBO1604 {ECO:0000313|EMBL:CAL83141.1};
OS Clostridium botulinum (strain Hall / ATCC 3502 / NCTC 13319 / Type A).
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=441771 {ECO:0000313|EMBL:CAL83141.1, ECO:0000313|Proteomes:UP000001986};
RN [1] {ECO:0000313|EMBL:CAL83141.1, ECO:0000313|Proteomes:UP000001986}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Hall / ATCC 3502 / NCTC 13319 / Type A [Sanger]
RC {ECO:0000313|Proteomes:UP000001986};
RX PubMed=17519437; DOI=10.1101/gr.6282807;
RA Sebaihia M., Peck M.W., Minton N.P., Thomson N.R., Holden M.T.G.,
RA Mitchell W.J., Carter A.T., Bentley S.D., Mason D.R., Crossman L.,
RA Paul C.J., Ivens A., Wells-Bennik M.H.J., Davis I.J., Cerdeno-Tarraga A.M.,
RA Churcher C., Quail M.A., Chillingworth T., Feltwell T., Fraser A.,
RA Goodhead I., Hance Z., Jagels K., Larke N., Maddison M., Moule S.,
RA Mungall K., Norbertczak H., Rabbinowitsch E., Sanders M., Simmonds M.,
RA White B., Whithead S., Parkhill J.;
RT "Genome sequence of a proteolytic (Group I) Clostridium botulinum strain
RT Hall A and comparative analysis of the clostridial genomes.";
RL Genome Res. 17:1082-1092(2007).
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|RuleBase:RU361134};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
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DR EMBL; AM412317; CAL83141.1; -; Genomic_DNA.
DR RefSeq; WP_011949139.1; NC_009698.1.
DR RefSeq; YP_001254108.1; NC_009495.1.
DR RefSeq; YP_001387491.1; NC_009698.1.
DR AlphaFoldDB; A5I276; -.
DR CAZy; GH13; Glycoside Hydrolase Family 13.
DR GeneID; 5185859; -.
DR KEGG; cbh:CLC_1632; -.
DR KEGG; cbo:CBO1604; -.
DR PATRIC; fig|413999.7.peg.1579; -.
DR HOGENOM; CLU_006462_1_1_9; -.
DR Proteomes; UP000001986; Chromosome.
DR GO; GO:0004556; F:alpha-amylase activity; IBA:GO_Central.
DR GO; GO:0043169; F:cation binding; IEA:InterPro.
DR GO; GO:0009313; P:oligosaccharide catabolic process; IBA:GO_Central.
DR CDD; cd11333; AmyAc_SI_OligoGlu_DGase; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
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 InterPro; IPR045857; O16G_dom_2.
DR PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR PANTHER; PTHR10357:SF178; OLIGO-1,6-GLUCOSIDASE 3-RELATED; 1.
DR Pfam; PF00128; Alpha-amylase; 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 Carbohydrate metabolism {ECO:0000256|RuleBase:RU361134};
KW Glycosidase {ECO:0000256|RuleBase:RU361134, ECO:0000313|EMBL:CAL83141.1};
KW Hydrolase {ECO:0000256|RuleBase:RU361134, ECO:0000313|EMBL:CAL83141.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001986}.
FT DOMAIN 13..415
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 554 AA; 65686 MW; D47800D832B788BB CRC64;
MNKTWWKEAV AYQIYPRSFK DSNDDGIGDI EGIISKLDYL KDLGIDIIWI CPMYKSPNDD
NGYDISDYKA IMDEFGTMED FDKLLQKAHE KGMKLIIDLV INHTSDEHKW FIESRSSKDN
PKRDFYIWRD GKDGKEPNNW ESIFKGSAWE YDYNTEQYFL HLFSKKQPDL NWENENVRNE
LYKMINWWLD KGIDGFRVDA ISHIKKEKGL KDIHNPKNLD YVPSFEKHMN VEGIQKYLKE
LKENTFDKYD IITVGEANGV NISQAPQWVG EKDGKFNMIF QFEHLDLWDV DHKEQSTIKK
LKEVLSKWQE GLEGVGWNAL FIENHDIQRV VSTLGDDKNF WEESSKALAL MYFMQKGTPF
IYQGQEIGMT NVKFEGIEDY NDIKTINIYK EKIRKGIPKD QALKYVWETS RDNSRTPMQW
DTTENAGFSK EKPWMKVNPN YVDINAREQE NNLNSILNFY KKIIRVKKEN EALIYGKYNL
ILAHHEQIYA YTRTLRNEKF IVIANLTNKE AKYTYKREKL NYKGLIISNY SIEKHEDITE
ILLKPFEARL YKIV
//
