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Database: UniProt
Entry: A0A0N9N8E0_9ACTN
LinkDB: A0A0N9N8E0_9ACTN
Original site: A0A0N9N8E0_9ACTN 
ID   A0A0N9N8E0_9ACTN        Unreviewed;       499 AA.
AC   A0A0N9N8E0;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 36.
DE   SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:ALG84395.1};
GN   ORFNames=ACH46_07650 {ECO:0000313|EMBL:ALG84395.1};
OS   Gordonia phthalatica.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=1136941 {ECO:0000313|EMBL:ALG84395.1, ECO:0000313|Proteomes:UP000063789};
RN   [1] {ECO:0000313|Proteomes:UP000063789}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QH-11 {ECO:0000313|Proteomes:UP000063789};
RA   Jin D., Kong X., Bai Z.;
RT   "Complete genome sequence and metabolic analysis of phthalate degradation
RT   pathway in Gordonia sp. QH-11.";
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ALG84395.1, ECO:0000313|Proteomes:UP000063789}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=QH-11 {ECO:0000313|EMBL:ALG84395.1,
RC   ECO:0000313|Proteomes:UP000063789};
RX   PubMed=29068282; DOI=10.1099/ijsem.0.002430;
RA   Jin D., Kong X., Jia M., Yu X., Wang X., Zhuang X., Deng Y., Bai Z.;
RT   "Gordonia phthalatica sp. nov., a di-n-butyl phthalate-degrading bacterium
RT   isolated from activated sludge.";
RL   Int. J. Syst. Evol. Microbiol. 67:5128-5133(2017).
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; CP011853; ALG84395.1; -; Genomic_DNA.
DR   RefSeq; WP_062392381.1; NZ_CP011853.1.
DR   AlphaFoldDB; A0A0N9N8E0; -.
DR   STRING; 1136941.ACH46_07650; -.
DR   KEGG; goq:ACH46_07650; -.
DR   PATRIC; fig|1136941.3.peg.1562; -.
DR   Proteomes; UP000063789; Chromosome.
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         239
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   499 AA;  51397 MW;  7EEF1B7041C0FA44 CRC64;
     MSPVSDQRPG QDPDTVLAEL RRLRAADAPT HGGHVLSYVY DSGRQRLDEL AAAAADLVRP
     VNGLDPTVFG SVAAMERDLV GFAREAFGSA DAVGTVTSGG TESCLLAVLA AWRASGVARS
     RANIVAPATV HAAFLKAGDI FGIEVRRVPV DAMTTEVSAA AMADRIDDGT VLLVASAPNY
     PTGAVDPIAE IGAVALERGV PLHVDACLGG FALAWWPDDL LAWDLSTPGV TSLSADFHKY
     GYSPKGASIL LHADRDRHRA GFFATADWPG YPIVNPTLLG SRSAAGTASA WAIARYLGAD
     GFAGLVADIA AARDALVDTV DGIDGLRIIG RPRGPVFAVA ADPDAPTPID PHRWADEAAA
     RGFTLQAQPR YTQPDGVDLA ASTHVTVTPV TRRVQPELVA ALVDAADAAR GQRATPAPTA
     LRDLADAFGS GAVSVADALA LDSATTESVL VGAGIDPHTD PSAASDALDI GAVIAAIDVL
     PRPVTAKMLA EFLAAFTNP
//
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