ID   A0A151FAS6_9EURY        Unreviewed;       455 AA.
AC   A0A151FAS6;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   RecName: Full=Pyridoxal-dependent decarboxylase {ECO:0008006|Google:ProtNLM};
GN   ORFNames=AYK18_08380 {ECO:0000313|EMBL:KYK38023.1};
OS   Theionarchaea archaeon DG-70.
OC   Archaea; Euryarchaeota; Theionarchaea.
OX   NCBI_TaxID=1803813 {ECO:0000313|EMBL:KYK38023.1, ECO:0000313|Proteomes:UP000075311};
RN   [1] {ECO:0000313|Proteomes:UP000075311}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Baker B.J., Lazar C.S., Teske A.P., Dick G.J.;
RL   Submitted (FEB-2016) 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|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:KYK38023.1}.
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DR   EMBL; LSSB01000042; KYK38023.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151FAS6; -.
DR   Proteomes; UP000075311; Unassembled WGS sequence.
DR   GO; GO:0016830; F:carbon-carbon lyase activity; IEA:InterPro.
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; PTHR45677:SF8; CYSTEINE SULFINIC ACID DECARBOXYLASE; 1.
DR   PANTHER; PTHR45677; GLUTAMATE DECARBOXYLASE-RELATED; 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         274
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   455 AA;  50517 MW;  253549481608C870 CRC64;
     MATRIYSGAS PQQIAEELIP LVDFQDEGMP LPQLKKLVEE RLIPHLMLYN QPGFQSMFNT
     FLEKGAELGA HIALTYNQGV TNWQVSPGGV VLEELCCKAL CHLFGFSADA DATFMYSGTY
     ANQQALYLAL HQKAEQEGFN LGKKGLQGFQ DPEKLAVVAS HDAHYSLRHA VRMLGLGDRS
     LITVPVDKNR RMNVEALKKI LKKAQNVFCI VATTGTTSTG AVDPVLPISE LCKNAKIWLH
     VDGAYGLAYS LVPEWNPLFS GVERADSVCW DPHKQMGVPI PNSVLFVKRK ENFDRMAMYS
     SYFSRRKDTE PNPGLKSPPS TRPFSALPLV TSLRYQGMKK VVERLCAPLI AVKTVAETLR
     SFKDIEVCHT PDTGILCFRM VPEGVPEHTL NQLHHNIYRR ILAEGTRTIS LTTLDEKTVL
     RLVAVSPAVT SEALMETVSH AQELAHEYLN LPGLS
//