ID   A0A0V0VZE2_9BILA        Unreviewed;       620 AA.
AC   A0A0V0VZE2;
DT   16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT   16-MAR-2016, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   RecName: Full=sphinganine-1-phosphate aldolase {ECO:0000256|ARBA:ARBA00038965};
DE            EC=4.1.2.27 {ECO:0000256|ARBA:ARBA00038965};
DE   AltName: Full=Sphingosine-1-phosphate aldolase {ECO:0000256|ARBA:ARBA00042568};
GN   ORFNames=T09_349 {ECO:0000313|EMBL:KRX68834.1};
OS   Trichinella sp. T9.
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Enoplea; Dorylaimia;
OC   Trichinellida; Trichinellidae; Trichinella.
OX   NCBI_TaxID=181606 {ECO:0000313|EMBL:KRX68834.1, ECO:0000313|Proteomes:UP000054681};
RN   [1] {ECO:0000313|EMBL:KRX68834.1, ECO:0000313|Proteomes:UP000054681}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ISS409 {ECO:0000313|EMBL:KRX68834.1};
RA   Korhonen P.K., Edoardo P., Giuseppe L.R., Gasser R.B.;
RT   "Evolution of Trichinella species and genotypes.";
RL   Submitted (JAN-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};
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:KRX68834.1}.
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DR   EMBL; JYDN01000001; KRX68834.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0V0VZE2; -.
DR   STRING; 181606.A0A0V0VZE2; -.
DR   Proteomes; UP000054681; 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: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:0000313|EMBL:KRX68834.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000054681}.
FT   MOD_RES         406
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   620 AA;  70398 MW;  53F72F8D16168384 CRC64;
     MKVAKLWMLD REKRSLNRQH RTQKMDWLLV HIDFLIDYMS TLTVEKLYND IRMFVFSCFL
     ASIHLIDWCR RLYNVTFGEL EPWQISAYTF CAFSVFLWLD KFFHCEEAFV VRLEKTLFRT
     ARRLPWVKRK ISVQLSKTRQ SVQMELQKND PDPEFIRHLP DRGFDQNDII AKAERYQKAG
     TFDFSKGKVS GAVYNANVEL LSLNAEIMKL FCWSNPLHPD IFPGIRKMEA EIVRMVCNMF
     NGGNNACGTV NCFISSHVTS GGTESLILAC LAYRNRAYGR GNKDPEIVVP ISAHGAFDKA
     AQMLRLRIRH VPLEAGTFKV DLDKMKQMIT KSTCMLVASA PNFPYGIIDP IEQVAALGEK
     FGIPVHVDCC LGGFLLPFME RADYPLDEEF DFRIRGVTSI SCDTHKYGFS TKGTSVLMYR
     NKLYQRYQYF CQPNWPGGIY ATATVAGSRN GANSASCWAT MLHFGIHGYV QCTRKIIRTA
     RYIERKLREV KGIYIFGHPR VSVVAFTSYV FDIYAFASQM GDRGWSLNLL QLPPAVHFCI
     TMNQTLEGVA HSFIEDATAV AEALLEDPSK SNDISGAAAL YGSSQTLPDR TLVNEIACAY
     LDACYATETK CDPDDLDGLI
//