ID A3P8Y1_BURP0 Unreviewed; 498 AA.
AC A3P8Y1;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 24-JAN-2024, entry version 80.
DE SubName: Full=Sphingosine-1-phosphate lyase {ECO:0000313|EMBL:ABN94008.1};
GN OrderedLocusNames=BURPS1106A_A2761 {ECO:0000313|EMBL:ABN94008.1};
OS Burkholderia pseudomallei (strain 1106a).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Burkholderiaceae; Burkholderia; pseudomallei group.
OX NCBI_TaxID=357348 {ECO:0000313|EMBL:ABN94008.1, ECO:0000313|Proteomes:UP000006738};
RN [1] {ECO:0000313|Proteomes:UP000006738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=1106a {ECO:0000313|Proteomes:UP000006738};
RA DeShazer D., Woods D.E., Nierman W.C.;
RL Submitted (FEB-2007) 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; CP000573; ABN94008.1; -; Genomic_DNA.
DR AlphaFoldDB; A3P8Y1; -.
DR KEGG; bpl:BURPS1106A_A2761; -.
DR HOGENOM; CLU_028929_1_0_4; -.
DR OMA; ECRDKNM; -.
DR Proteomes; UP000006738; Chromosome II.
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; 6.10.140.2150; -; 1.
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}.
FT MOD_RES 296
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 498 AA; 54655 MW; 857A9836278D2EDE CRC64;
MQPHPGNIRT HIGVPTDVGT AKENVMDLEE GIRRLYPYAE EFGVMRGFPE QGTPRDELLA
QLRSMAERED RNWESGHSSG AMYSGDRDHH AWLNEAYSVF SHVNALRRDM CPSMNRMESE
IVGMTVAMLH GDAVAAHHPG QRACGMITLG GTESILGATL AYREKARAER GIERPRMIWP
ASAHPVFRKA AHLFGFDVTV APIDPVTMQV DADFVRDAVD ANTVMLVGSA CNYPYGTIDP
IGALSAIAVE KDVWLHVDGC LGGWMLPWGE ALGYPDIPAF DFRLPGVTSI SADTHKFGYG
PKGGSVLAWR DASFRRHQYF LMTDWVGGVY GSPGLTGSRS GGLIAATWAA LRSLGREGYL
ARAKAIFETA FDMQAAVRAI PELRVLGKPT FCFAFTSDAF DIYHVNDFMR QRGWRLNGLR
RPDALQMCVT GPQTQPGVAE QFRCDLGAAA DYARAHAQER PKTSGVYASD AAGVDLSDDA
RTRAFFTQVI DLFTDCPL
//