ID A0A267G827_9PLAT Unreviewed; 545 AA.
AC A0A267G827;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Sphingosine-1-phosphate lyase {ECO:0008006|Google:ProtNLM};
GN ORFNames=BOX15_Mlig025281g2 {ECO:0000313|EMBL:PAA82195.1};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|EMBL:PAA82195.1, ECO:0000313|Proteomes:UP000215902};
RN [1] {ECO:0000313|EMBL:PAA82195.1, ECO:0000313|Proteomes:UP000215902}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DV1 {ECO:0000313|EMBL:PAA82195.1};
RC TISSUE=Whole organism {ECO:0000313|EMBL:PAA82195.1};
RA Berezikov E.;
RT "A platform for efficient transgenesis in Macrostomum lignano, a flatworm
RT model organism for stem cell research.";
RL Submitted (JUN-2017) 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:PAA82195.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; NIVC01000487; PAA82195.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A267G827; -.
DR STRING; 282301.A0A267G827; -.
DR Proteomes; UP000215902; Unassembled WGS sequence.
DR GO; GO:0016830; F:carbon-carbon lyase activity; IEA:InterPro.
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:SF9; SPHINGOSINE-1-PHOSPHATE LYASE; 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:UP000215902}.
FT MOD_RES 348
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 545 AA; 59328 MW; 3B93055333EF69D9 CRC64;
MSSLAVLAAL VELAVKAAAT MLFLLAAVRV WYDGPLAFLL DTLRRVPAVQ RAITASLRHQ
AGRVITDDLK ISAGSPPVAI PDKGEDPQQL LEQIETLRTH KTDQMFAYVY SEAAEVLGHA
LAKAQERAAL DFVSNDASEL DGGLSAEQRH LVAEYMRAFM HENALNPTLF VALRRFEVEL
VQMTAAMLNA GPAARGNVTS GGTESVLMAV KTYRDLARAR MPGSVGTPNI VAAVTVHPAF
NKAAHYFGLT MTLVPVDPVS QTVDPAALRA AVTSDTVLLV ASAPQYCHGI VDPVEEYGRV
AREFGLPLHV DACFGGFMLP WVEKLGYSVP AFDFRVPEVT SVSADLHKYG FAPKGASVIV
YRTGGLRKHQ LYAYSGWPGG LFGSPTMAGT RPGGYLATAW VTLRTMGQEG FLRIAGDLMD
LTKFWTEEIR ATGALKIVGS PQMTCFAITS NNPAVNVFVL ADLLEDKGWK MERESNPDCL
HVTVLPQHLA RRDDFVTDIR ACVDWILTEK IKPKGMAAVY GMVARVPAKE LIDEFLLEFF
NQIYS
//
