ID   E3N551_CAERE            Unreviewed;       548 AA.
AC   E3N551;
DT   11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT   11-JAN-2011, sequence version 1.
DT   24-JAN-2024, entry version 48.
DE   SubName: Full=CRE-TAG-38 protein {ECO:0000313|EMBL:EFO87030.1};
GN   Name=Cre-tag-38 {ECO:0000313|EMBL:EFO87030.1};
GN   ORFNames=CRE_19389 {ECO:0000313|EMBL:EFO87030.1};
OS   Caenorhabditis remanei (Caenorhabditis vulgaris).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC   Caenorhabditis.
OX   NCBI_TaxID=31234 {ECO:0000313|Proteomes:UP000008281};
RN   [1] {ECO:0000313|Proteomes:UP000008281}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PB4641 {ECO:0000313|Proteomes:UP000008281};
RG   Caenorhabditis remanei Sequencing Consortium;
RA   Wilson R.K.;
RT   "PCAP assembly of the Caenorhabditis remanei genome.";
RL   Submitted (JUL-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; DS268530; EFO87030.1; -; Genomic_DNA.
DR   RefSeq; XP_003096491.1; XM_003096443.1.
DR   AlphaFoldDB; E3N551; -.
DR   STRING; 31234.E3N551; -.
DR   EnsemblMetazoa; CRE19389.1; CRE19389.1; WBGene00068627.
DR   GeneID; 9823770; -.
DR   KEGG; crq:GCK72_017178; -.
DR   CTD; 9823770; -.
DR   eggNOG; KOG1383; Eukaryota.
DR   HOGENOM; CLU_028929_1_0_1; -.
DR   InParanoid; E3N551; -.
DR   OMA; AFWQLRG; -.
DR   OrthoDB; 3024111at2759; -.
DR   Proteomes; UP000008281; 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:SF15; SPHINGOSINE 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:UP000008281}.
FT   MOD_RES         338
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   548 AA;  61864 MW;  2FC0746CBD88C214 CRC64;
     MEVLTQNLYV AKDLLVTELQ KYNPIALVAT TFAVTYVLTN LRHMQLDDMG IRKRISTWFF
     TTVKRVPFIR RMIDKQLDEV KVELEKSLQI PDHTTEYFRT IPVKSVGREE VLRLATIYDH
     LEGPAFLEGR VSGAVFNRED DKDEREMYEE VFGRFAWSNP LWPKLFPGVR IMEAEVVRMC
     CNMMNGDEET CGTMSTGGSI SILLACLAHR NRLLKRGEKY TEMIVPSSVH AAFFKAAETF
     RIKVRKIPVD PVTFKVDLTK MRAAINSRTC MLVGSAPNFP FGTVDDIEAI GQLGLEYNIP
     VHVDACLGGF LLPFLEDDAI RYDFRVPGVS SISADSHKYG LAPKGSSVVL YKNKELLHNQ
     YFCDADWQGG IYASATMEGS RAGHNIALCW AAMLYHAQDG YKANAKKIVE TTRKIRDGLA
     GIKGIKLQGP SDVCIVSWTT DDNVELYRFH NYMKERHWQL NGLQFPSGVH IMVTMNHTHP
     GLAEEFIADC KAAVEFVRTK PVSESDKKSE AAIYGLAQSI PDRSLVHEFA HSYLDAVYAL
     PEQSKKSF
//