ID   B6EGT4_ALISL            Unreviewed;       554 AA.
AC   B6EGT4;
DT   25-NOV-2008, integrated into UniProtKB/TrEMBL.
DT   25-NOV-2008, sequence version 1.
DT   27-MAR-2024, entry version 74.
DE   SubName: Full=Alpha-amylase {ECO:0000313|EMBL:CAQ80650.1};
DE            EC=3.2.1.1 {ECO:0000313|EMBL:CAQ80650.1};
GN   Name=malS {ECO:0000313|EMBL:CAQ80650.1};
GN   OrderedLocusNames=VSAL_I2966 {ECO:0000313|EMBL:CAQ80650.1};
OS   Aliivibrio salmonicida (strain LFI1238) (Vibrio salmonicida (strain
OS   LFI1238)).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Aliivibrio.
OX   NCBI_TaxID=316275 {ECO:0000313|EMBL:CAQ80650.1, ECO:0000313|Proteomes:UP000001730};
RN   [1] {ECO:0000313|EMBL:CAQ80650.1, ECO:0000313|Proteomes:UP000001730}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LFI1238 {ECO:0000313|EMBL:CAQ80650.1,
RC   ECO:0000313|Proteomes:UP000001730};
RX   PubMed=19099551; DOI=10.1186/1471-2164-9-616;
RA   Hjerde E., Lorentzen M.S., Holden M.T., Seeger K., Paulsen S., Bason N.,
RA   Churcher C., Harris D., Norbertczak H., Quail M.A., Sanders S.,
RA   Thurston S., Parkhill J., Willassen N.P., Thomson N.R.;
RT   "The genome sequence of the fish pathogen Aliivibrio salmonicida strain
RT   LFI1238 shows extensive evidence of gene decay.";
RL   BMC Genomics 9:616-616(2008).
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
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DR   EMBL; FM178379; CAQ80650.1; -; Genomic_DNA.
DR   RefSeq; WP_012551368.1; NC_011312.1.
DR   AlphaFoldDB; B6EGT4; -.
DR   CAZy; GH13; Glycoside Hydrolase Family 13.
DR   KEGG; vsa:VSAL_I2966; -.
DR   eggNOG; COG0366; Bacteria.
DR   HOGENOM; CLU_022115_1_0_6; -.
DR   Proteomes; UP000001730; Chromosome 1.
DR   GO; GO:0004556; F:alpha-amylase activity; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR006047; Glyco_hydro_13_cat_dom.
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   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS51257; PROKAR_LIPOPROTEIN; 1.
PE   4: Predicted;
KW   Glycosidase {ECO:0000313|EMBL:CAQ80650.1};
KW   Hydrolase {ECO:0000313|EMBL:CAQ80650.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           19..554
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5002844349"
FT   DOMAIN          124..514
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
FT   REGION          22..46
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   554 AA;  61960 MW;  09FE362C3109264D CRC64;
     MKLSVCATFI SLSLLVGCQS TSLTSTDSSD SISTADSSNQ IESTTSSNNN TAICPVLGIQ
     PVTVSVSDLW ANGDVITDAY TGNIAQVVNG EITLTPSRHS GGVLLLESEE EKARFSWDGA
     TFYHIATDRF FNGNSWNDHS YGRQSTKEGF QGGDIVGLTK KLDYLAELGV DVVWISTPLE
     QVHGWLPNKS GNSPEYPYAG GATLDWTQLD TNMGSEQEMR TFVDLAHQLG MRVMWSVDTA
     PPTPTLSDLQ QFSIQPNNPD ALPSYWSEWQ PQEGQNLTHY LDAFKNKNGE IPDWWSEAWM
     EENNENAITL PAFFANKPST KVKSSEKTKN EYLAGWMSAW VSEFGIDGFV VSNSTPELTQ
     KIEQEGKDAF TLWNKDNAYK ALENASFRVI DLQQQNYFSD QMLSLKSNDE PHCLTKLNAE
     YVTQSQAEKP SMTRLTWFDG KSLSDSSVGS VNADNYADYR DAATALLLSP NAVSIWYGDE
     TAKMGGIYSK MNWNEIKDQR WSLQSHWKKL IEFRNNHSSI ANGEHQVIKR EPYYAFIRKN
     ESDSVMVVYT GEKK
//