ID   A0A124ILI7_9FIRM        Unreviewed;       470 AA.
AC   A0A124ILI7;
DT   13-APR-2016, integrated into UniProtKB/TrEMBL.
DT   13-APR-2016, sequence version 1.
DT   27-MAR-2024, entry version 25.
DE   SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:KUO66006.1};
GN   ORFNames=APF84_00215 {ECO:0000313|EMBL:KUO66006.1};
OS   Gracilibacter sp. BRH_c7a.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Gracilibacteraceae;
OC   Gracilibacter.
OX   NCBI_TaxID=1734398 {ECO:0000313|EMBL:KUO66006.1, ECO:0000313|Proteomes:UP000053404};
RN   [1] {ECO:0000313|EMBL:KUO66006.1, ECO:0000313|Proteomes:UP000053404}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BRH_c7a {ECO:0000313|EMBL:KUO66006.1};
RA   Bagnoud A., Chourey K., Hettich R.L., De Bruijn I., Andersson A.F.,
RA   Leupin O.X., Schwyn B., Bernier-Latmani R.;
RT   "Microbial metabolic network in the subsurface.";
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR602129-50,
CC         ECO:0000256|RuleBase:RU000382};
CC   -!- SIMILARITY: Belongs to the group II decarboxylase family.
CC       {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:KUO66006.1}.
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DR   EMBL; LOEZ01000018; KUO66006.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A124ILI7; -.
DR   STRING; 1734398.APF84_00215; -.
DR   Proteomes; UP000053404; 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:0019752; P:carboxylic 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; 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   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}.
FT   MOD_RES         301
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   470 AA;  51468 MW;  3FBF376B82978750 CRC64;
     MKTDNKIVSD NLREEALDFA LFEQAKNYAL DYMENILNQP VYPDKAALDG LNAFKEPLQA
     EYGDPYEILA KLHNNGSPVT VAQTGGRYFG FVNGGIIPVA LAAKWLSDTW DQNAALYVIS
     PIASVLEEVC EKWLIDLLQL PANTAAGFVG GSSTATLCGL TAGRNHLLNK LGYDVSKKGL
     FGAPEIRVVL GEGAHSTVYK ALSILGLGSE RIIKVPEDNQ GRINPDLVPE LDERTLLILQ
     AGNVNSGAFD DFNTLCQKAK KAGAWVHVDG AFGLWAAASD NLNHLTSGVG LADSWSVDAH
     KTLNAPYDNG IILCSNREAL TSALHMTGSY IVYSEQRDGM LYTPDMSRRA RIIELWATLK
     SLGKRGASEL IEDLHDKSRY FAAALEKNGF LIKNEVCFNQ ILVSLGNSKT TEMVLQHIQN
     SQECWCGGAK WKNESVIRIS VCSYRTTYED IDRSVNAFVK AKKEVTSYSS
//