ID   A0A1T4Z2H1_9ACTN        Unreviewed;       469 AA.
AC   A0A1T4Z2H1;
DT   10-MAY-2017, integrated into UniProtKB/TrEMBL.
DT   10-MAY-2017, sequence version 1.
DT   24-JAN-2024, entry version 21.
DE   SubName: Full=Glutamate or tyrosine decarboxylase {ECO:0000313|EMBL:SKB08063.1};
GN   ORFNames=SAMN06295964_1967 {ECO:0000313|EMBL:SKB08063.1};
OS   Aeromicrobium choanae.
OC   Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC   Nocardioidaceae; Aeromicrobium.
OX   NCBI_TaxID=1736691 {ECO:0000313|EMBL:SKB08063.1, ECO:0000313|Proteomes:UP000191040};
RN   [1] {ECO:0000313|EMBL:SKB08063.1, ECO:0000313|Proteomes:UP000191040}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=9H-4 {ECO:0000313|EMBL:SKB08063.1,
RC   ECO:0000313|Proteomes:UP000191040};
RA   Peterson S.W.;
RL   Submitted (FEB-2017) 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. Sphingosine-
CC       1-phosphate lyase subfamily. {ECO:0000256|ARBA:ARBA00038302}.
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DR   EMBL; LT796768; SKB08063.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1T4Z2H1; -.
DR   STRING; 1736691.SAMN06295964_1967; -.
DR   OrthoDB; 3401800at2; -.
DR   Proteomes; UP000191040; Chromosome i.
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; 3.90.1150.10; 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; PTHR42735; -; 1.
DR   PANTHER; PTHR42735:SF6; SPHINGOSINE-1-PHOSPHATE LYASE 1; 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         229
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   469 AA;  49573 MW;  B4EB58CA84591254 CRC64;
     MSPDQILAEL AARRQGDLPT HGGRTLAYVY DSGLEEADEV ARQAIAMYAA TNGLDPTAFP
     SLLSMESDLV GFARSALHGG DEVVGTVTSG GTESILLAVQ TARDAAGVER PAMVVPTTIH
     AAFAKAAHYF GVELVTVPVG PGHRADVAAM TETIDRLGDR VVLVAASTPS YAHGVIDPVE
     DLAAVTRERG LRFHVDACIG GWILPWTPDA PAWDFAVPGV TSISVDLHKY AYTPKGVSLL
     LHADAALRRP QFFAHADWPG YTMLNSTTQS TKSGGPLAAA WAVVQLIGDE GYRDLVRRTL
     DGTRRLAEGI EAIDHLHLVE RPDTSLVVVG TDDAVDPFTI SDLMLDRGWF VQPQMRFGDE
     PANLHLTISA ATAASVPEFL EALRESVAAA AAAGPIRIDP LLAEAAAGLD PDTLDDEAFD
     GLLALAGLAG EGGQVAVPER LGPVNALVDV APPRVREALM IAFLDRLTR
//