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
//