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Database: UniProt
Entry: M7ZBV6_TRIUA
LinkDB: M7ZBV6_TRIUA
Original site: M7ZBV6_TRIUA 
ID   M7ZBV6_TRIUA            Unreviewed;       489 AA.
AC   M7ZBV6;
DT   29-MAY-2013, integrated into UniProtKB/TrEMBL.
DT   29-MAY-2013, sequence version 1.
DT   27-MAR-2024, entry version 57.
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=TRIUR3_09166 {ECO:0000313|EMBL:EMS57131.1};
OS   Triticum urartu (Red wild einkorn) (Crithodium urartu).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Pooideae; Triticodae; Triticeae; Triticinae; Triticum.
OX   NCBI_TaxID=4572 {ECO:0000313|EMBL:EMS57131.1};
RN   [1] {ECO:0000313|EMBL:EMS57131.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=23535596; DOI=10.1038/nature11997;
RA   Ling H.Q., Zhao S., Liu D., Wang J., Sun H., Zhang C., Fan H., Li D.,
RA   Dong L., Tao Y., Gao C., Wu H., Li Y., Cui Y., Guo X., Zheng S., Wang B.,
RA   Yu K., Liang Q., Yang W., Lou X., Chen J., Feng M., Jian J., Zhang X.,
RA   Luo G., Jiang Y., Liu J., Wang Z., Sha Y., Zhang B., Wu H., Tang D.,
RA   Shen Q., Xue P., Zou S., Wang X., Liu X., Wang F., Yang Y., An X., Dong Z.,
RA   Zhang K., Zhang X., Luo M.C., Dvorak J., Tong Y., Wang J., Yang H., Li Z.,
RA   Wang D., Zhang A., Wang J.;
RT   "Draft genome of the wheat A-genome progenitor Triticum urartu.";
RL   Nature 496:87-90(2013).
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; KD149549; EMS57131.1; -; Genomic_DNA.
DR   AlphaFoldDB; M7ZBV6; -.
DR   STRING; 4572.M7ZBV6; -.
DR   eggNOG; KOG1383; Eukaryota.
DR   OMA; DPHKMGL; -.
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   GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
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   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW   ECO:0000256|RuleBase:RU000382}.
FT   MOD_RES         283
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ   SEQUENCE   489 AA;  52428 MW;  AF924955C3FD8E31 CRC64;
     MAAVKLVPGV SGYIAAEKSK VVEKLQSGSA SSKKDLRTEL PAVGIPDGVI GDLQALKDKD
     VRWQGKCSGT VYIAGSESEG HFSLINKAYS MFSHTNPLHQ DVFKSVAQLE AEVVAMTAAL
     LGSKEKASGG QICGNMTSGG TESILLAVKT SRDYMQSKKG ITKPEMIIAE SAHSAYDKAA
     QYFNIKVRRV PVNKEFLADV KGFKRCINGN TIMMVGSAPG FPHGLIDPIE ELGELASQYG
     ICLHVDLCLG GFVLPFARKL GYPIPPFDFS VKGVTSISTD VHKYGLAPKG TSTVLYRNHE
     IRKHQFVAVT EWTGGLYISP TMAGSRPGGL VAGAWAAMMS LGLNGYLEST GKIMEVSKKI
     QKGIDDISGL FVIGKPDMTV VAFGSDAVDI FEVNDIMSSK GWHLNALQRP NSANPDSATW
     FFSLHICVTL QHTAIYEEFL KDLEDSVDTV KANPGPISGG MAPIYGAAGK MPDRGTVKEL
     LVEFMDSSC
//
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