ID   A0A1V8M5I3_9GAMM        Unreviewed;       486 AA.
AC   A0A1V8M5I3;
DT   07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT   07-JUN-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
DE   SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:OQK16756.1};
GN   ORFNames=AU255_02280 {ECO:0000313|EMBL:OQK16756.1};
OS   Methyloprofundus sedimenti.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC   Methylococcaceae; Methyloprofundus.
OX   NCBI_TaxID=1420851 {ECO:0000313|EMBL:OQK16756.1, ECO:0000313|Proteomes:UP000191980};
RN   [1] {ECO:0000313|EMBL:OQK16756.1, ECO:0000313|Proteomes:UP000191980}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=WF1 {ECO:0000313|EMBL:OQK16756.1,
RC   ECO:0000313|Proteomes:UP000191980};
RA   Shamseldin A., Moawad H., Abd El-Rahim W.M., Sadowsky M.J.;
RL   Submitted (DEC-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:OQK16756.1}.
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DR   EMBL; LPUF01000001; OQK16756.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1V8M5I3; -.
DR   STRING; 1420851.AU255_02280; -.
DR   OrthoDB; 9803665at2; -.
DR   Proteomes; UP000191980; Unassembled WGS sequence.
DR   GO; GO:0016831; F:carboxy-lyase 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; 3.90.1150.170; -; 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   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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000191980}.
FT   MOD_RES         294
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   486 AA;  52711 MW;  430830403B92C376 CRC64;
     MYQEHAECGK LPELLQRLGE DLTNYLRFEH PDAMCNEESW KTALGGPLPD QGIGCEQLLD
     IIGQHLIPNG SQVPKPGCTS FITTGATSIG VLATLSGVVA APQRVGLTAF NYLEELSLQW
     MAEMFALPST MKGIYSSGGS VANLVALGAA RQWAFERLGL NPAENGVQKP CRIYASSACH
     RTIHRAAAVL GMGRSAVITI ATDNNGRLCP NALRRQLQAD ANTGFVPVAV VANAGTTNTG
     AIDPLREIAE IAAAYQIWFH VDGAYGLPGI LDPRIRPLYE GLSLADSVIV DPHKWLGAPV
     GIGATYVRDR SILNRAFSQG AADYLEGACH DDNIQNSMLS MGVPYHDFGV ELSAPSRGAV
     VWALIREIGK TGMRERICRH NDMARLVADL ARKHPALEVV QEPTLSICCF RYVSDKVQNL
     NDLNKQIHRH LVQDGRCIPS TTILNGILVI RPCFVGARTT EQHARELVDA VVETGNNLLR
     DMHPTT
//