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Database: UniProt
Entry: A0A0K9F6M8_9BACI
LinkDB: A0A0K9F6M8_9BACI
Original site: A0A0K9F6M8_9BACI 
ID   A0A0K9F6M8_9BACI        Unreviewed;       488 AA.
AC   A0A0K9F6M8;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   24-JAN-2024, entry version 26.
DE   SubName: Full=Alpha-amlyase {ECO:0000313|EMBL:KMY29828.1};
GN   ORFNames=ACZ11_19145 {ECO:0000313|EMBL:KMY29828.1};
OS   Lysinibacillus xylanilyticus.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX   NCBI_TaxID=582475 {ECO:0000313|EMBL:KMY29828.1, ECO:0000313|Proteomes:UP000037326};
RN   [1] {ECO:0000313|Proteomes:UP000037326}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 23493 {ECO:0000313|Proteomes:UP000037326};
RG   Consortium for Microbial Forensics and Genomics (microFORGE);
RA   Knight B.M., Roberts D.P., Lin D., Hari K., Fletcher J., Melcher U.,
RA   Blagden T., Winegar R.A.;
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC         Evidence={ECO:0000256|ARBA:ARBA00001913};
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:KMY29828.1}.
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DR   EMBL; LFXJ01000010; KMY29828.1; -; Genomic_DNA.
DR   RefSeq; WP_049668729.1; NZ_LFXJ01000010.1.
DR   AlphaFoldDB; A0A0K9F6M8; -.
DR   PATRIC; fig|582475.4.peg.2892; -.
DR   OrthoDB; 9805159at2; -.
DR   Proteomes; UP000037326; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   Gene3D; 2.60.40.1180; Golgi alpha-mannosidase II; 1.
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   PANTHER; PTHR10357:SF215; ALPHA-AMYLASE 1; 1.
DR   PANTHER; PTHR10357; ALPHA-AMYLASE FAMILY MEMBER; 1.
DR   Pfam; PF00128; Alpha-amylase; 1.
DR   Pfam; PF16657; Malt_amylase_C; 1.
DR   SMART; SM00642; Aamy; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   SUPFAM; SSF51011; Glycosyl hydrolase domain; 1.
PE   4: Predicted;
KW   Lyase {ECO:0000313|EMBL:KMY29828.1}; 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..488
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5038784508"
FT   TRANSMEM        454..475
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          44..357
FT                   /note="Glycosyl hydrolase family 13 catalytic"
FT                   /evidence="ECO:0000259|SMART:SM00642"
SQ   SEQUENCE   488 AA;  54720 MW;  22B01DE47BF12511 CRC64;
     MKFKKWISAT AASLLLATSL VSATPVAHAD EASARTIAEE SIYDLLVDRF FNGSGTNDFD
     TNTQDPTKFA GGDFAGLQDK LKFIGEMGFT IASIGPIFAT EKYDGSMPTS YSTIERHFGT
     AEEFHSVIET YKAKNVSIMV DFPLNNVSPN HEWAKDPAKK DWIASTNNGQ VQWDLTNKDV
     QEALIKSATD FVSTYDVGGM RLTNIAGVDK GFINEMIKAL KDSKKSLYVI SNEESDANFD
     ASISPATADI YRNIFKNVDM DSSKLMEPLT GEKPTQIMVD SLETRRFTFD SAAENMFPPT
     RLKMAMGALF MMPGVPVVQY GTEIAMNGET KPDTHQIFNF KTDDELIEYI KNVQSLRNKS
     ETLRDGDFEV ITNENGLLVF TRTSDKEKWV IMVNNTSKTQ RVDLTPAQLG EGKMLNGILH
     EEKVRINEKD VYPVILDREM VEIYQVRDDE GLNVPYMVAL GLVWVIFIGF VVVIIRRGKV
     RRKEQDVQ
//
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