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Database: UniProt/TrEMBL
Entry: A0A1Y0CKF7_9BACI
LinkDB: A0A1Y0CKF7_9BACI
Original site: A0A1Y0CKF7_9BACI 
ID   A0A1Y0CKF7_9BACI        Unreviewed;       516 AA.
AC   A0A1Y0CKF7;
DT   30-AUG-2017, integrated into UniProtKB/TrEMBL.
DT   30-AUG-2017, sequence version 1.
DT   24-JAN-2024, entry version 20.
DE   RecName: Full=Alpha-amylase {ECO:0000256|RuleBase:RU361134};
DE            EC=3.2.1.1 {ECO:0000256|RuleBase:RU361134};
GN   ORFNames=B4U37_06880 {ECO:0000313|EMBL:ART75769.1};
OS   Sutcliffiella horikoshii.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Sutcliffiella.
OX   NCBI_TaxID=79883 {ECO:0000313|EMBL:ART75769.1, ECO:0000313|Proteomes:UP000195573};
RN   [1] {ECO:0000313|EMBL:ART75769.1, ECO:0000313|Proteomes:UP000195573}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=20a {ECO:0000313|EMBL:ART75769.1,
RC   ECO:0000313|Proteomes:UP000195573};
RA   Zarza E., Alcaraz L.D., Aguilar-Salinas B., Islas A., Olmedo-Alvarez G.;
RT   "Complete Genome Sequence of the Bacillus horikoshii 20a strain from Cuatro
RT   Cienegas, Coahuila, Mexico.";
RL   Submitted (APR-2017) 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   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 13 family.
CC       {ECO:0000256|ARBA:ARBA00008061, ECO:0000256|RuleBase:RU003615}.
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DR   EMBL; CP020880; ART75769.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1Y0CKF7; -.
DR   KEGG; bhk:B4U37_06880; -.
DR   Proteomes; UP000195573; Chromosome.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0043169; F:cation binding; IEA:InterPro.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR   CDD; cd11339; AmyAc_bac_CMD_like_2; 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   PANTHER; PTHR10357:SF215; ALPHA-AMYLASE 1; 1.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 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   Lyase {ECO:0000313|EMBL:ART75769.1}; Membrane {ECO:0000256|SAM:Phobius};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..28
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           29..516
FT                   /note="Alpha-amylase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5012982432"
FT   TRANSMEM        486..508
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          42..390
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   516 AA;  60147 MW;  33BC1445169D1D8B CRC64;
     MKRVMGLILV PFLLFSAWFV PSVQPVNAEK EEHAWQDEII YFIMIDRFNN GDTSNDFEVN
     RDDPKSYHGG DFRGITEKLD YLKDMGFTAL WLTPIVQNEE KGYHGYWTED FYNTEEHFGS
     IEEFKELVKE AHKRDMKIIV DLVVNHTGYQ HAWLNETDKQ NWFHPNEPIR NWDDQEQVEN
     GWIYGLPDLN QDNPETRKYL IDMAKWWIEE TDIDGYRLDT VKHVPKDFWK EFSEEMKSVK
     EDFFLIGEVW HDDPNYVAGY QETGIDSFVD FPTYNEITRV FSGPDESLTR LDSLFQSKQK
     LYENPYVLGT FLDNHDVERF TRAAIKKKQH PPTRLKLALA YMYTTPGIPI MYYGTEIALD
     GGEDPDNRRD MNFRADKELI DYITKLAELR KTMPSLTHGS YEMVYDDNAM TVIKREYEEE
     TTFVAINNSS ETQVAPIDAE LVGEDLELRG TLGDELVRNS DGKYTIGLDR ETAEIYTVKE
     DSGINVGFVS AMALIYGGFI AFIAAAVMRR KKKNKQ
//
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