ID A0A0M4G8K2_9BACI Unreviewed; 556 AA.
AC A0A0M4G8K2;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 33.
DE RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN ORFNames=AM500_22065 {ECO:0000313|EMBL:ALC92160.1};
OS Bacillus sp. FJAT-18017.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1705566 {ECO:0000313|EMBL:ALC92160.1, ECO:0000313|Proteomes:UP000060713};
RN [1] {ECO:0000313|EMBL:ALC92160.1, ECO:0000313|Proteomes:UP000060713}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=FJAT-18017 {ECO:0000313|EMBL:ALC92160.1,
RC ECO:0000313|Proteomes:UP000060713};
RA Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Lan J., Che J., Ge C.,
RA Shi H., Pan Z., Liu X.;
RT "Genome sequencing project for genomic taxonomy and phylogenomics of
RT Bacillus-like bacteria.";
RL Submitted (AUG-2015) 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|RuleBase:RU361134};
CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000256|ARBA:ARBA00004613}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
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DR EMBL; CP012602; ALC92160.1; -; Genomic_DNA.
DR RefSeq; WP_053601141.1; NZ_CP012602.1.
DR AlphaFoldDB; A0A0M4G8K2; -.
DR STRING; 1705566.AM500_22065; -.
DR PATRIC; fig|1705566.3.peg.4879; -.
DR Proteomes; UP000060713; Chromosome.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0043169; F:cation binding; IEA:InterPro.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR CDD; cd11333; AmyAc_SI_OligoGlu_DGase; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
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};
KW Hydrolase {ECO:0000256|RuleBase:RU361134};
KW Reference proteome {ECO:0000313|Proteomes:UP000060713};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}.
FT DOMAIN 13..415
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 556 AA; 65543 MW; 2F8318A2B58DA1B3 CRC64;
MDKKWWKESI CYQVYPRSFM DSNGDGIGDL KGVTAKLDYI KELGIDVIWL SPMYKSPNDD
NGYDISDYQD IMDEFGTMAD FNELLEEVHK RGMKLILDLV INHTSDEHPW FIESRSSKNN
PKRDWYIWRD GEDGREPNNW ESIFSGSAWK LDEQTGQYFM HIFSARQPDL NWENPEVRNA
LYDMVNWWLD KGIDGFRVDA ISHIKKKPGL PDMPNPKGLE YVPSFDYMMN VEGVDGFLKE
FVSKTTRNYD VMTVGEANGV RITDADKWVG ERDGYFNMIF QFEFLGLWDK NKKDSVDVKA
LKRVLTKWQK GLEGIGWNAL FIENHDQPRR VSTWGNDKKY WKESAKMLGA MYFFMKGTPF
IYQGQEIGMT NVQFPSIEDY NDVGMRNYYR IETEKGRSHE EIMEFIWKHG RDNARTPMQW
DSSHLAGFTA ADKTWFGINP NYTKINVASQ LDDKDSILHF YKELIRLRKE NKLFVYGKYH
LYYPNHPKLF VYTRTLGRQK AIILCNVHGT PSRFKMPAAI RYKKSELILN NYPVQGKKLP
KEFTMKPFET RVYFLY
//
