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
//