ID A0A0D6Z898_9BACI Unreviewed; 552 AA.
AC A0A0D6Z898;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN ORFNames=UB32_10700 {ECO:0000313|EMBL:KIY22019.1};
OS Mesobacillus subterraneus.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Mesobacillus.
OX NCBI_TaxID=285983 {ECO:0000313|EMBL:KIY22019.1, ECO:0000313|Proteomes:UP000032512};
RN [1] {ECO:0000313|EMBL:KIY22019.1, ECO:0000313|Proteomes:UP000032512}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MITOT1 {ECO:0000313|EMBL:KIY22019.1,
RC ECO:0000313|Proteomes:UP000032512};
RA Peet K.C., Thompson J.R.;
RT "Draft genome sequences of the supercritical CO2 tolerant bacteria Bacillus
RT subterraneus MITOT1 and Bacillus cereus MIT0214.";
RL Submitted (JAN-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:KIY22019.1}.
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DR EMBL; JXIQ01000085; KIY22019.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0D6Z898; -.
DR PATRIC; fig|285983.3.peg.703; -.
DR OrthoDB; 9805159at2; -.
DR Proteomes; UP000032512; 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; 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; 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:UP000032512}.
FT DOMAIN 13..414
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 552 AA; 64093 MW; 513BC66A5289AC1A CRC64;
MKHTWWKEAV AYQIYPRSFM DSNGDGIGDL QGIISKLDYL QDLGIDVIWI CPMYKSPNDD
NGYDISDYQD IMDEFGSMAD FDQLLAETHR RGMKLIIDLV INHTSDEHQW FIESRASKHS
PKRDWYIWRD GKDGAEPNNW ESIFGGSAWE YDELTNQYFL HIFSRKQPDL NWENKQVRTA
LYEMINWWLD KGIDGFRVDA ISHIKKEEGL KDMPNPEGLP YVSSFEKHMN VDGIQTFLEE
LKQETFAKYD IMTVGEANGV SIEEADLWVG EEQGKFNMVF QFEHLDLWDS EKKALDLAKL
KNTFTRWQKG LEGKGWNALF IENHDKARIV STWGDDQSYW RESATALAAM YFLMQGTPFI
YQGQEIGMTN VQFPSIDDYD DVATKNLYTI RRENGVSHEE IMNFIWATSR DNSRTPMQWS
NAVNAGFTTG SPWLGINPNY QAVHVEAQLM DQDSILHFYK KMIQMKKANQ VFTYGTYDLV
LEGHEQIYAY TRTLDDKQAI VISNLSGEPA SFAFDGFPLE TSRLLLHNYQ VEDHGPAAAF
TFKPYETRVY TK
//
