ID A0A0Q8UWC7_9ACTN Unreviewed; 475 AA.
AC A0A0Q8UWC7;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE SubName: Full=Pyridoxal-dependent decarboxylase {ECO:0000313|EMBL:KRC46592.1};
GN ORFNames=ASE19_22595 {ECO:0000313|EMBL:KRC46592.1};
OS Nocardioides sp. Root79.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736600 {ECO:0000313|EMBL:KRC46592.1, ECO:0000313|Proteomes:UP000051414};
RN [1] {ECO:0000313|EMBL:KRC46592.1, ECO:0000313|Proteomes:UP000051414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root79 {ECO:0000313|EMBL:KRC46592.1,
RC ECO:0000313|Proteomes:UP000051414};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KRC46592.1, ECO:0000313|Proteomes:UP000051414}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root79 {ECO:0000313|EMBL:KRC46592.1,
RC ECO:0000313|Proteomes:UP000051414};
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:KRC46592.1}.
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DR EMBL; LMIP01000015; KRC46592.1; -; Genomic_DNA.
DR RefSeq; WP_056896361.1; NZ_LMIP01000015.1.
DR AlphaFoldDB; A0A0Q8UWC7; -.
DR OrthoDB; 3401800at2; -.
DR Proteomes; UP000051414; 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:UP000051414}.
FT MOD_RES 231
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 475 AA; 49097 MW; C1677A736224EF0C CRC64;
MSPDEVRARL AALQAEDLPV HGGRTLAYVY DAGLAEVDAL AREAVAAFAG SNGLDPTAFP
SLLAMENDLV TFARALVDGP STTVGTLTSG GTESCLLAVQ GARDARPDIT APSMVVPETV
HAAFHKAAHY FGVRAVVVPV GPDHRADADA MAAAIDETTV LVVASAPSYA HGVVDPVTAI
AAAAAARGVR CHVDACIGGW VLPWATRLGR PVLPWTFAVE GVTSISMDLH KYAYAPKGSS
LLLHRTPELR RPQYFAHAGW PGYTMLNATL QSTRSGGPVA GAWATVQAIG DPGYLDLTRR
ALAATDRIVA GLAEVDGLAL LAVPDSTLVA AVADGPLDVF TVCDEMAERG WFVQPQLSYD
GRAPSLHLAV SAATDPEAFL AALEASVSAA LDAGPVPVDE AVVALLQTLD PTTLGDAEFD
LLLAAGGLAG DEGELGLPER MAPVNALLDA APPRLREAVL VAFLDRLARP IAADA
//
