ID A0A160M8K5_9BACI Unreviewed; 512 AA.
AC A0A160M8K5;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=alpha-amylase {ECO:0000256|ARBA:ARBA00012595};
DE EC=3.2.1.1 {ECO:0000256|ARBA:ARBA00012595};
GN ORFNames=A361_07295 {ECO:0000313|EMBL:AND38927.1};
OS Cytobacillus oceanisediminis 2691.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Cytobacillus.
OX NCBI_TaxID=1196031 {ECO:0000313|EMBL:AND38927.1, ECO:0000313|Proteomes:UP000077856};
RN [1] {ECO:0000313|EMBL:AND38927.1, ECO:0000313|Proteomes:UP000077856}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2691 {ECO:0000313|EMBL:AND38927.1,
RC ECO:0000313|Proteomes:UP000077856};
RA Jeong H., Kim H.J., Lee D.-W.;
RT "Complete genome sequence of Bacillus oceanisediminis strain 2691.";
RL Submitted (APR-2016) 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|ARBA:ARBA00000548};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000256|ARBA:ARBA00001913};
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DR EMBL; CP015506; AND38927.1; -; Genomic_DNA.
DR RefSeq; WP_019381460.1; NZ_CP015506.1.
DR AlphaFoldDB; A0A160M8K5; -.
DR STRING; 1196031.A361_07295; -.
DR KEGG; bon:A361_07295; -.
DR eggNOG; COG0366; Bacteria.
DR Proteomes; UP000077856; Chromosome.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0004556; F:alpha-amylase activity; IEA:InterPro.
DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
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; IPR013777; A-amylase-like.
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 PIRSF; PIRSF001024; Alph-amyl_fung; 1.
DR SMART; SM00642; Aamy; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE 4: Predicted;
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lyase {ECO:0000313|EMBL:AND38927.1}; 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..23
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 24..512
FT /note="alpha-amylase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5007818087"
FT TRANSMEM 482..503
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 38..386
FT /note="Glycosyl hydrolase family 13 catalytic"
FT /evidence="ECO:0000259|SMART:SM00642"
SQ SEQUENCE 512 AA; 59968 MW; F5F1C8F23652DF40 CRC64;
MNKGIITFIL IPFLLFYALP AGAAEKEERK WQDETFYFLM VDRFSNGDPN NDFKVDVQDP
KAYHGGDFKG ITERLDYIKD MGFTAIWLTP VFDNEEKGYH GYWIKDFYNT EEHFGTMDEL
KQLVQEAHKR DMKVILDFVV NHVGTNHEWV NDPGKKDWFH EKQDIINWTN QSEIENGWIY
GLPDLKQENP EVQNYLIDAA KWWIEETDID GYRLDTVKHV PKSFWTEFAK NVKSVKEDFY
LLGEVWSDDP KYIAEYEKTG IDGFVDYPLN DHLRTAFAEP DKSLSWLFAN WDRNKAFYEN
PYLMGSFMDN HDTVRFTRDA ITKNHHPGPR WKLALTYMYT TPGIPIVYYG SEIAMDGGED
PDNRRQMDFR TDKELIDYIA KLGEVRQMLP SLTRGDMELL EEKDGFAVYK RNYEDETTVI
VINNSTKSQK AVLDSTQLEE GKELRGMIAD DLIRDKDGKY EMIIDREEAE VYVLAEKSGL
NIPLIAALAA VYSAFMIFIY LLWKRSKQKK SE
//
