ID   A0A2U9CHI2_SCOMX        Unreviewed;       618 AA.
AC   A0A2U9CHI2;
DT   12-SEP-2018, integrated into UniProtKB/TrEMBL.
DT   12-SEP-2018, sequence version 1.
DT   24-JAN-2024, entry version 16.
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=SMAX5B_008726 {ECO:0000313|EMBL:AWP14332.1};
OS   Scophthalmus maximus (Turbot) (Psetta maxima).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Actinopterygii; Neopterygii; Teleostei; Neoteleostei; Acanthomorphata;
OC   Carangaria; Pleuronectiformes; Pleuronectoidei; Scophthalmidae;
OC   Scophthalmus.
OX   NCBI_TaxID=52904 {ECO:0000313|EMBL:AWP14332.1, ECO:0000313|Proteomes:UP000246464};
RN   [1] {ECO:0000313|EMBL:AWP14332.1, ECO:0000313|Proteomes:UP000246464}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Martinez P.;
RT   "Integrating genomic resources of turbot (Scophthalmus maximus) in depth
RT   evaluation of genetic and physical mapping variation across individuals.";
RL   Submitted (DEC-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};
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; CP026257; AWP14332.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A2U9CHI2; -.
DR   STRING; 52904.ENSSMAP00000021328; -.
DR   Proteomes; UP000246464; Chromosome 15.
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   CDD; cd06450; DOPA_deC_like; 1.
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:AWP14332.1};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000246464}.
FT   MOD_RES         402
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   618 AA;  68617 MW;  3AB3FD1ED6B931CC CRC64;
     MCWVTDRGLE LKGADSPFAL MRRISSNLYE DMFDKRSGSV SVRRMLSSVG VVTMASDSAL
     EVYKEMVLLY LDEGRRQVNS RCADLEPWQI IGATVITTLG AVWVKGFLFQ QESLTSRIKK
     QCFRIIRRIP YIGVAIQSQL NKALDDMSAS LCTLKNGMSY TRQLPPKGLS QNQVLDKIRE
     YETLNEVQWE KGCVSGAVYW GDESLTKFLV KVYGDFAWSN PLHPDIFPGV RKMEAEVVRM
     ACTLFHGGPN SCGTVTSGGT ESILMACKAY RDMAYERGVK YPEILAPLSV HAAFNKAAHY
     FGMKLVHVPL DKKTMKVDVK AMKRAINKNT AMLVCSAPQF PHGIIDPVEE LGELAVRYNL
     PLHVDACLGG FLIVFMDKLG YQLAPFDFRV KGVTSISADT HKYGYAPKGS SVILYSDNKY
     RHYQYFVAPD WQGGIYASPS IAGSRPGGII AACWATMMHM GENGYLDATR KIISTARRIT
     REVNKIEGVF VFGEPEVSVV AIGSDVFDIF RLSNALTSKG WNLNTLQFPS SIHICCTVLH
     TQPGVADQFI RDVQEQAAII MKNPSEKTTG MGAIYGMAQS IPDRSMVTEI SRGFLDCLYS
     TEVRKSDTSH MNGNGKAH
//