ID A0A0K2YNL8_9NOCA Unreviewed; 488 AA.
AC A0A0K2YNL8;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Pyridoxal dependent decarboxylase {ECO:0000313|EMBL:CRK54526.1};
GN ORFNames=RHCRD62_90205 {ECO:0000313|EMBL:CRK54526.1};
OS Rhodococcus sp. RD6.2.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Nocardiaceae;
OC Rhodococcus.
OX NCBI_TaxID=260936 {ECO:0000313|EMBL:CRK54526.1, ECO:0000313|Proteomes:UP000044872};
RN [1] {ECO:0000313|EMBL:CRK54526.1, ECO:0000313|Proteomes:UP000044872}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RD6.2 {ECO:0000313|EMBL:CRK54526.1,
RC ECO:0000313|Proteomes:UP000044872};
RA Wang D.B., Wang M.;
RL Submitted (MAY-2015) 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; CVQP01000012; CRK54526.1; -; Genomic_DNA.
DR RefSeq; WP_050067415.1; NZ_CVQP01000012.1.
DR AlphaFoldDB; A0A0K2YNL8; -.
DR STRING; 260936.RHCRD62_90205; -.
DR OrthoDB; 3401800at2; -.
DR Proteomes; UP000044872; 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:UP000044872}.
FT MOD_RES 240
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 488 AA; 51689 MW; 6FD47191178EC260 CRC64;
MQFEQSPQDV LARLDELREA DAPTSGGRLL SYVYDSGIAE LDDLAGAAAR KAQPLNGLDP
TTFPSVAALE RDLVALARSV LADGVDGVVG SVTSGGTESC MLAVKSARDT WRAVTGREDR
PTLVIGSTAH AAFIKAAHYL DLRLRVLPVD PDTCRLRPDD VAAALDDSVA LVVASTPSYP
HGALDPITEI AEVCAAQGVP VHVDGCIGAW VLPWWPGADT RPLWDLRVPG VASLSVDLHK
YGYAPKGVSV LLYRDRDRHR RQWFATSAWP GYAVVNPTML GSRTVMPIAA GWAVSKALGG
NGFDELTGRI ARSAAHLRAV IDDIDGLRIV GDPVGPLLAV ATDTSIPEDR RVDPHRWADA
ARELGWVLQP QPGRTQSDGT VLPRTTHLTL TPVTEAVADD LATAVTKAAD AVRGVPGAVA
PEDFIAAADH IRPEDLTSEN CAAVLTLAGL DPTAGLGGSM ADLLALIEAL PEPVAERLLI
EFLARFME
//
