ID   G7GW99_9ACTN            Unreviewed;       485 AA.
AC   G7GW99;
DT   25-JAN-2012, integrated into UniProtKB/TrEMBL.
DT   25-JAN-2012, sequence version 1.
DT   24-JAN-2024, entry version 38.
DE   SubName: Full=Putative lyase {ECO:0000313|EMBL:GAB07874.1};
GN   ORFNames=GOAMR_75_00340 {ECO:0000313|EMBL:GAB07874.1};
OS   Gordonia amarae NBRC 15530.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC   Gordonia.
OX   NCBI_TaxID=1075090 {ECO:0000313|EMBL:GAB07874.1, ECO:0000313|Proteomes:UP000006023};
RN   [1] {ECO:0000313|EMBL:GAB07874.1, ECO:0000313|Proteomes:UP000006023}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NBRC 15530 {ECO:0000313|EMBL:GAB07874.1,
RC   ECO:0000313|Proteomes:UP000006023};
RA   Takarada H., Hosoyama A., Tsuchikane K., Katsumata H., Yamazaki S.,
RA   Fujita N.;
RT   "Whole genome shotgun sequence of Gordonia amarae NBRC 15530.";
RL   Submitted (NOV-2011) 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}.
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:GAB07874.1}.
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DR   EMBL; BAED01000075; GAB07874.1; -; Genomic_DNA.
DR   AlphaFoldDB; G7GW99; -.
DR   STRING; 1075090.GOAMR_75_00340; -.
DR   eggNOG; COG0076; Bacteria.
DR   Proteomes; UP000006023; 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; 3.90.1150.10; 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};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006023}.
FT   MOD_RES         235
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   485 AA;  50693 MW;  6789AF4D67C8915B CRC64;
     MTDQRAEQIL ARLTELRADD APTRGGRILS YVYDPGLAVV DELARRAAQQ VQHVNGLDPT
     TFGSVARMEA DVIGFAAGIV HGDDAVGVVT SGGTESCLLA VKSARDRWRA RHREATGMPS
     IVAPTTVHAA FHKAARYFDL RLDLVPVGED GTVGADDLLA RCSGDTALVV VSAPCYPFGV
     IDPVADVAPR AAALGIACHV DACIGGWVLP FWGEGLPRWD FRVPGVTSMS LDAHKYGYSP
     KGVSVLLFAD RDAKRAASFA TTDWPGYPVV NPTMLGSRSA TALAAAWAIL EYLGADGLTG
     LTARTRQATE TLAGVVAGIE GLRVAGAPSG PLFAVRTDPE AAAGRGVDPH QWSDRVRELG
     WTLQPQPGLR QHGGPALPPT THLTVTPVTA GIVDALAAAM TRAADDVRGR PPIDLSALPD
     ALPALRSDAP LDSAAATEIL AALGLAGDGP ALPDHLAPVM ALLEVVPAPR AQELLTELLA
     RLNER
//