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Database: UniProt
Entry: C3Y062_BRAFL
LinkDB: C3Y062_BRAFL
Original site: C3Y062_BRAFL 
ID   C3Y062_BRAFL            Unreviewed;       566 AA.
AC   C3Y062;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   24-JAN-2024, entry version 67.
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=BRAFLDRAFT_277711 {ECO:0000313|EMBL:EEN66428.1};
OS   Branchiostoma floridae (Florida lancelet) (Amphioxus).
OC   Eukaryota; Metazoa; Chordata; Cephalochordata; Leptocardii; Amphioxiformes;
OC   Branchiostomatidae; Branchiostoma.
OX   NCBI_TaxID=7739;
RN   [1] {ECO:0000313|EMBL:EEN66428.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=S238N-H82 {ECO:0000313|EMBL:EEN66428.1};
RC   TISSUE=Testes {ECO:0000313|EMBL:EEN66428.1};
RX   PubMed=18563158; DOI=10.1038/nature06967;
RG   US DOE Joint Genome Institute (JGI-PGF);
RA   Putnam N.H., Butts T., Ferrier D.E.K., Furlong R.F., Hellsten U.,
RA   Kawashima T., Robinson-Rechavi M., Shoguchi E., Terry A., Yu J.-K.,
RA   Benito-Gutierrez E.L., Dubchak I., Garcia-Fernandez J., Gibson-Brown J.J.,
RA   Grigoriev I.V., Horton A.C., de Jong P.J., Jurka J., Kapitonov V.V.,
RA   Kohara Y., Kuroki Y., Lindquist E., Lucas S., Osoegawa K., Pennacchio L.A.,
RA   Salamov A.A., Satou Y., Sauka-Spengler T., Schmutz J., Shin-I T.,
RA   Toyoda A., Bronner-Fraser M., Fujiyama A., Holland L.Z., Holland P.W.H.,
RA   Satoh N., Rokhsar D.S.;
RT   "The amphioxus genome and the evolution of the chordate karyotype.";
RL   Nature 453:1064-1071(2008).
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; GG666477; EEN66428.1; -; Genomic_DNA.
DR   RefSeq; XP_002610418.1; XM_002610372.1.
DR   AlphaFoldDB; C3Y062; -.
DR   STRING; 7739.C3Y062; -.
DR   eggNOG; KOG1383; Eukaryota.
DR   InParanoid; C3Y062; -.
DR   GO; GO:0005783; C:endoplasmic reticulum; IBA:GO_Central.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   GO; GO:0008117; F:sphinganine-1-phosphate aldolase activity; IBA:GO_Central.
DR   GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR   GO; GO:0030149; P:sphingolipid catabolic process; IBA:GO_Central.
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:0000256|RuleBase:RU000382};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        40..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   MOD_RES         353
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   566 AA;  62909 MW;  EE5CC8BC59D3DBE4 CRC64;
     MDVYLHVLLE SAFKVSDYVT SIEESFNTYI EQNGYPPHQL FLFTIACTLL MVWLYRFFFM
     HELSMWERFK LSLFKTVRRL PYFGPQIQRE VEKTLDKMAG SMFQLPPGMK YVYGLPENGL
     SEDQVMRAVK GYQQLGHVDW KKGNVSGTVY SGQPELTQLC TKVYGEFAWS NPLHPDVFPG
     VRKMEAEVVA MTLKMFNAGA NACGAMTSGG TESILMACLA YRNMAKERGV TLPEIIAPFS
     VHAAFDKAAH YFGMRIIHVR MDPKSWKVNI KAMRRSISSS TCMLVGSAPQ FPHGIIDPIA
     DIAKLGKRYG IPVHVDACLG GFLLPFMGKA GFELPPFDFR LDGVTSISAD THKYGFAPKG
     SSVVLYSDKK YRHSQYFVQP NWPGGVYATG TMAGSRAGAI VAACWATMMN IGEDGYVEST
     KKIVKAARYI AKELRKIDGI FVFGEPEVSV VAFGSEVFDI YRVSNTLTAK GWNLNSLQFP
     SSIHLCCTLC HTLPGVTDRF INDVKNAVAD ALADPQAKTT GQGAIYGMAQ SVPDRKIIAD
     IAWGYLDCVY DIKRKDKDGP VNGMHH
//
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