ID U5LGV8_9BACI Unreviewed; 551 AA.
AC U5LGV8;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 47.
DE RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN ORFNames=N288_24275 {ECO:0000313|EMBL:AGX06690.1};
OS Bacillus infantis NRRL B-14911.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX NCBI_TaxID=1367477 {ECO:0000313|EMBL:AGX06690.1, ECO:0000313|Proteomes:UP000017805};
RN [1] {ECO:0000313|EMBL:AGX06690.1, ECO:0000313|Proteomes:UP000017805}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL B-14911 {ECO:0000313|EMBL:AGX06690.1,
RC ECO:0000313|Proteomes:UP000017805};
RA Massilamany C., Smith T.P.L., Loy J.D., Barletta R., Reddy J.;
RT "Complete genome sequence of Bacillus infantis NRRL B-14911 that has
RT potential to induce cardiac disease by antigenic mimicry.";
RL Submitted (JUL-2013) 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; CP006643; AGX06690.1; -; Genomic_DNA.
DR RefSeq; WP_009794379.1; NC_022524.1.
DR AlphaFoldDB; U5LGV8; -.
DR STRING; 1367477.N288_24275; -.
DR GeneID; 85554463; -.
DR KEGG; bif:N288_24275; -.
DR PATRIC; fig|1367477.3.peg.4848; -.
DR HOGENOM; CLU_006462_1_2_9; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000017805; 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; IPR032091; Malt_amylase_C.
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 Pfam; PF16657; Malt_amylase_C; 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:UP000017805};
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 551 AA; 64139 MW; C6A47D13C66E8560 CRC64;
MKKIWWKEAV GYQIYPRSFQ DSNGDGIGDL QGIIERLDYV KDLGIDVIWI CPVYKSPNDD
NGYDISDYQD IMEDFGTMAD FDRLLEEVHQ RGMKLIIDLV LNHTSDEHPW FIESRSSETS
PKRDWYIWRD GKQGAEPNNW ESIFGGSAWE WDELTQQYFL HVFSRRQPDL NWENSEVREA
LYDVVNWWLE KGIDGFRIDA ISHIKKRPGM PDLPNPENKK YVSSFDMHMN QEGIHEFLQE
FKEKTYANYD SMSVGEANGV TVDEADLWVG SENGKMDMIF QFEHLGLWDA ETNPELDIVE
LKKVLTRWQK GLEKDGWNAL FIENHDKPRV VSTWGNDQEF WRESATSMAA MYFLMQGTPF
IYQGQEIGMT NVQFPSIDDY DDVAVKNLYK LKTEEGKSHQ EIMEIIWASS RDNSRTPMQW
DSTANAGFSS GSPWMKVNSN YTNINVEKQE KDEESILSFY KKMISLKKAN EVFTYGQYDL
LLEEDKQIYA YTRTLEDDQV IVITNLSAKE AVFTSGFALK PENLLLNNYP AAEAEGKSVT
LKPYEARVYR I
//
