ID M0QEB7_9ACTN Unreviewed; 493 AA.
AC M0QEB7;
DT 03-APR-2013, integrated into UniProtKB/TrEMBL.
DT 03-APR-2013, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE SubName: Full=Putative lyase {ECO:0000313|EMBL:GAC66789.1};
GN ORFNames=GS4_04_00450 {ECO:0000313|EMBL:GAC66789.1};
OS Gordonia soli NBRC 108243.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Gordoniaceae;
OC Gordonia.
OX NCBI_TaxID=1223545 {ECO:0000313|EMBL:GAC66789.1, ECO:0000313|Proteomes:UP000011666};
RN [1] {ECO:0000313|EMBL:GAC66789.1, ECO:0000313|Proteomes:UP000011666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 108243 {ECO:0000313|EMBL:GAC66789.1,
RC ECO:0000313|Proteomes:UP000011666};
RA Isaki-Nakamura S., Hosoyama A., Tsuchikane K., Ando Y., Baba S., Ohji S.,
RA Hamada M., Tamura T., Yamazoe A., Yamazaki S., Fujita N.;
RT "Whole genome shotgun sequence of Gordonia soli NBRC 108243.";
RL Submitted (JAN-2013) 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:GAC66789.1}.
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DR EMBL; BANX01000004; GAC66789.1; -; Genomic_DNA.
DR RefSeq; WP_007617327.1; NZ_BANX01000004.1.
DR AlphaFoldDB; M0QEB7; -.
DR STRING; 1223545.GS4_04_00450; -.
DR eggNOG; COG0076; Bacteria.
DR OrthoDB; 3401800at2; -.
DR Proteomes; UP000011666; 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:UP000011666}.
FT MOD_RES 241
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 493 AA; 51929 MW; C72F960B6573D68E CRC64;
MTDDRARDII DRLHALRRDD APTHGGRVLS YVYDAGIAGL DELARAAAAS VQSVNGLDPT
TFPSVARLER DVIDTARVLV HGDRLPTVGL ITSGGTESCL LAVKSARDRW RGAGGVGRPR
IVAPTSVHAA FHKAAGYFDV DLDLVPVDRE GRVDADEFIE RLDATMALVV VSAPNYPYGT
LDPVEQIAAA ADDLRIRCHV DACIGGWVLP FWDEASGGDT STPAWDFRLP GVTSISLDSH
KYGFAPKGTS VLLFRHRDDK RAAGFATTSW PGYPVVNPTM LGSRSATSLA AAWAVISYLG
TTGFVDLTRR THRATTALLA AVGGIDGLRV VGDPVGPLFS VATDPSVPVE RRVDPHIWSD
RVRTTGWVLQ PQPGATQFPS GPELPRTTHL TITPVTDAGL ADLVAALTSA ADAVRGTPPI
DATDLAAAFP RLAGTGPVSA DDAHEILTEL GLGGDDSGAL PDALAPVMAL LDVIPPGLAR
SLLAELIARL NES
//
