ID A0A0Q8V3R8_9MICO Unreviewed; 505 AA.
AC A0A0Q8V3R8;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:KRC50633.1};
GN ORFNames=ASE16_06390 {ECO:0000313|EMBL:KRC50633.1};
OS Leifsonia sp. Root227.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC Leifsonia.
OX NCBI_TaxID=1736496 {ECO:0000313|EMBL:KRC50633.1, ECO:0000313|Proteomes:UP000051819};
RN [1] {ECO:0000313|EMBL:KRC50633.1, ECO:0000313|Proteomes:UP000051819}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root227 {ECO:0000313|EMBL:KRC50633.1,
RC ECO:0000313|Proteomes:UP000051819};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRC50633.1, ECO:0000313|Proteomes:UP000051819}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root227 {ECO:0000313|EMBL:KRC50633.1,
RC ECO:0000313|Proteomes:UP000051819};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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}.
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:KRC50633.1}.
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DR EMBL; LMIO01000002; KRC50633.1; -; Genomic_DNA.
DR RefSeq; WP_055892473.1; NZ_LMIO01000002.1.
DR AlphaFoldDB; A0A0Q8V3R8; -.
DR STRING; 1736496.ASE16_06390; -.
DR OrthoDB; 3401800at2; -.
DR Proteomes; UP000051819; 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:UP000051819}.
FT MOD_RES 239
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 505 AA; 53002 MW; C9EFEEB38CDACB85 CRC64;
MVVFDSAAIL GRLAALRAAD APTHGGRVLS YVYDSGLAEV DELAAQAMRL VQPVNGLDPT
TFTSVAVMER EVLGFARELL HGADDVVGSV TSGGTESCLL AVKTARDVWR AAGGTGRARM
VAPVTVHAAF QKAAHYFDVE LELVSVHPET WVVDAAAIVD RLGPDVALVV VSAPGYPLAA
LDPVEEVATA CAAEGIACHV DACIGGWILP FWRAADGSPL PLWDFRVPGV TSISADLHKF
GYAPKGASVL LQRGRDRQRM QYFATTGWPG YPVVNPTMLG SKSAGALAAS WAIVQALGAR
GFAELAESCR RATRALADIV GDIDGLRIVG DPVGPLLAVA TDESVPAERR VDPHHWADRA
GHRGWHLQLQ PGLVQPDGTR LPHTTHLTIT PVTEERVDEL EAALRASADE VRGVPRVDPA
AILGALPPGL AEGLAGGQAA GQLDAESAWG VLQAIGLAGA SDDTSGARLP DDLAPFLALI
EALPRPLTER LLIELLARIV EPTES
//
