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Database: UniProt
Entry: A0A0J6FQ48_9BACI
LinkDB: A0A0J6FQ48_9BACI
Original site: A0A0J6FQ48_9BACI 
ID   A0A0J6FQ48_9BACI        Unreviewed;       554 AA.
AC   A0A0J6FQ48;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-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=AB986_10870 {ECO:0000313|EMBL:KMM36472.1};
OS   Alkalihalobacillus macyae.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Alkalihalobacillus.
OX   NCBI_TaxID=157733 {ECO:0000313|EMBL:KMM36472.1, ECO:0000313|Proteomes:UP000035996};
RN   [1] {ECO:0000313|EMBL:KMM36472.1, ECO:0000313|Proteomes:UP000035996}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 16346 {ECO:0000313|EMBL:KMM36472.1,
RC   ECO:0000313|Proteomes:UP000035996};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Zheng C., Che J., Ge C., Shi H.,
RA   Pan Z., Liu X.;
RL   Submitted (JUN-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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KMM36472.1}.
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DR   EMBL; LELK01000004; KMM36472.1; -; Genomic_DNA.
DR   RefSeq; WP_048311184.1; NZ_LELK01000004.1.
DR   AlphaFoldDB; A0A0J6FQ48; -.
DR   STRING; 157733.AB986_10870; -.
DR   PATRIC; fig|157733.3.peg.186; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000035996; Unassembled WGS sequence.
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:UP000035996}.
FT   DOMAIN          13..415
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   554 AA;  65101 MW;  3FB3405F7A02F3CC CRC64;
     MKKIWWKEAV GYQIYPRSFQ DSNGDGVGDL QGIIQRLDYI KDLGVDVIWI CPMYKSPNDD
     NGYDISDYQD IMEDFGTMKD FDALLKEVHK RDMKLIIDLV LNHTSDEHEW FIESRSSKED
     PKRDWYIWRD GKDGREPNNW ESIFGGSAWE YDKKTDQYYL HVFSTKQPDV NWENPDVRVA
     LYDTVNWWLD KGIDGFRIDA ISHIKKRPGL PDMPNPYKKD YVSSFDMHMN QNGIQEFLQE
     FKDETYAKYD VMTVGEANGV SIDEADQWVD EKDGKMDMIF QFEHLGLWDA EENPDLDIVS
     LKKVLTRWQK GLENKGWNAL FVENHDKPRV VSTWGNDKEY WRESATSMGA MYFLMQGTPF
     IYQGQEIGMT NVQFPSIEDY DDVADKNRYR IQRAAGVPHD QIMKVIWASS RDNSRTPMQW
     NNDSNAGFTT GNPWMKVNPN YVDINVKKQE QDEESILSFY KKMIDLKKNN LVFTYGSYDL
     LLEEDKQIYA YTRTTKDDRV LVVTNLSTEP AVFKSEFIID EDQLLLNNYE VNHVSNESIV
     LKPYEARVYR LNRA
//
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