ID   A0A0K9H1B7_9BACI        Unreviewed;       464 AA.
AC   A0A0K9H1B7;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   SubName: Full=Amino acid decarboxylase {ECO:0000313|EMBL:KMY52640.1};
GN   ORFNames=AC623_00495 {ECO:0000313|EMBL:KMY52640.1};
OS   Bacillus sp. FJAT-27231.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Bacillus.
OX   NCBI_TaxID=1679168 {ECO:0000313|EMBL:KMY52640.1, ECO:0000313|Proteomes:UP000037077};
RN   [1] {ECO:0000313|Proteomes:UP000037077}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FJAT-27231 {ECO:0000313|Proteomes:UP000037077};
RA   Liu B., Wang J., Zhu Y., Liu G., Chen Q., Chen Z., Che J., Ge C., Shi H.,
RA   Pan Z., Liu X.;
RT   "Genome sequencing project for genomic taxonomy and phylogenomics of
RT   Bacillus-like bacteria.";
RL   Submitted (JUL-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR602129-50, ECO:0000256|RuleBase:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {ECO:0000256|ARBA:ARBA00009533, ECO:0000256|RuleBase:RU000382}.
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:KMY52640.1}.
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DR   EMBL; LFZU01000001; KMY52640.1; -; Genomic_DNA.
DR   RefSeq; WP_049659432.1; NZ_LFZU01000001.1.
DR   AlphaFoldDB; A0A0K9H1B7; -.
DR   STRING; 1679168.AC623_00495; -.
DR   PATRIC; fig|1679168.3.peg.88; -.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000037077; Unassembled WGS sequence.
DR   GO; GO:0004058; F:aromatic-L-amino-acid decarboxylase activity; IEA:UniProt.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0006520; P:amino acid metabolic process; IEA:InterPro.
DR   Gene3D; 3.90.1150.10; Aspartate Aminotransferase, domain 1; 1.
DR   Gene3D; 3.40.640.10; Type I PLP-dependent aspartate aminotransferase-like (Major domain); 1.
DR   InterPro; IPR010977; Aromatic_deC.
DR   InterPro; IPR002129; PyrdxlP-dep_de-COase.
DR   InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR   InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR   InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR   PANTHER; PTHR11999:SF70; AROMATIC-L-AMINO-ACID DECARBOXYLASE; 1.
DR   PANTHER; PTHR11999; GROUP II PYRIDOXAL-5-PHOSPHATE DECARBOXYLASE; 1.
DR   Pfam; PF00282; Pyridoxal_deC; 1.
DR   PRINTS; PR00800; YHDCRBOXLASE.
DR   SUPFAM; SSF53383; PLP-dependent transferases; 1.
PE   3: Inferred from homology;
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU000382};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037077}.
FT   MOD_RES         293
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   464 AA;  51776 MW;  79CD5F1F38853EE2 CRC64;
     MNIMNQDQKD FERILTEVVQ HATNFYHGLE ERCVAVQSYD MPKNQLSTSG IGASAALEYF
     THHYATGLSA SVGSRYLGFV TGGSTPAAII GDWLVSIYDQ NAASSQDSIA GLVELETIDL
     LKELLHLSHD YSGTFVSGAT MANFVGLAQA RQWIAHHYGK DISMEGLYDI PSIKILSGAP
     HSSVFKAASM LGIGRKSIHS IPCQENREAI DIEKLKEFLE QQKSEPCIVV ANVGTVNTVD
     YDDLAAIGKL KKHYRFWLHI DAAFGGFAAC SPLYRELVEG MDAADSITID AHKWLNVPYD
     SAMQFTRHKQ LQAEVFQNNA AYLGDAIEHP EFFNLTPENS RRFRALPAWF TLKAYGKSGY
     QNLIEQNVEL AKRLGEKINN SREFKLLSPV RLNVVCFSLN KQSITAEMNN QFLTALNQQG
     KVFMTPTIYN GVPAIRAAFS NWRTEEKDID IIWEALRSTV QSIK
//