ID S3C147_OPHP1 Unreviewed; 585 AA.
AC S3C147;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 27-MAR-2024, entry version 34.
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=F503_02595 {ECO:0000313|EMBL:EPE06467.1};
OS Ophiostoma piceae (strain UAMH 11346) (Sap stain fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Ophiostoma.
OX NCBI_TaxID=1262450 {ECO:0000313|EMBL:EPE06467.1, ECO:0000313|Proteomes:UP000016923};
RN [1] {ECO:0000313|EMBL:EPE06467.1, ECO:0000313|Proteomes:UP000016923}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=UAMH 11346 {ECO:0000313|EMBL:EPE06467.1,
RC ECO:0000313|Proteomes:UP000016923};
RX PubMed=23725015; DOI=10.1186/1471-2164-14-373;
RA Haridas S., Wang Y., Lim L., Massoumi Alamouti S., Jackman S., Docking R.,
RA Robertson G., Birol I., Bohlmann J., Breuil C.;
RT "The genome and transcriptome of the pine saprophyte Ophiostoma piceae, and
RT a comparison with the bark beetle-associated pine pathogen Grosmannia
RT clavigera.";
RL BMC Genomics 14:373-373(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; KE148153; EPE06467.1; -; Genomic_DNA.
DR AlphaFoldDB; S3C147; -.
DR STRING; 1262450.S3C147; -.
DR VEuPathDB; FungiDB:F503_02595; -.
DR eggNOG; KOG1383; Eukaryota.
DR HOGENOM; CLU_028929_1_0_1; -.
DR OMA; DPHKMGL; -.
DR OrthoDB; 3024111at2759; -.
DR Proteomes; UP000016923; 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:0000256|RuleBase:RU000382};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50,
KW ECO:0000256|RuleBase:RU000382};
KW Reference proteome {ECO:0000313|Proteomes:UP000016923}.
FT MOD_RES 357
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 585 AA; 63084 MW; 80F3FAA8F104947C CRC64;
MPGSSSMLIS LRENISSVRR NGAGASPLLS LAFNIDLLRN IVFFFFVLRA ARRTVWKLKG
RGVFGTAAEL YIDTRRILFG WFLRMPGVRS KVREQVEEAL GKMEEKLVPS GMTRYTKLPT
TGWAYDDVRK QLEALSGLEH TRWEDGRVSG AVYHGEDDLM ALQTEAYGKF TVANPIHPDV
FPGVRKMEAE IVAMVLGLFN GPQGSAGVTT SGGTESILMA CLSARQKGYI ERGITEPEMI
IPETAHTAFH KASQYYKIKL HLVKCPAPGY QVDVRSVARL INPNTVLLVG SAPNFPHGII
DDIAGLGRLA SRNKIPLHVD CCLGSFMVPM LEKAGFETTP FDFRVRGVTS ISVDTHKYGF
APKGNSVVLY RTTTLRGYQY FVSADWAGGV YASPGAAGSR PGALIAGCWA SMMAVGESGY
LEACGKIVGT AHKFAEHITT SPLLKSDIEV MGRPLVSVVA FKAKKSKSSG SAVNIYSLAD
AMSAKGWHLN ALQNPPAIHV AFTMPIVKAY DSLVADLEAC IEEEREKARV RAVEAASSGS
KGLGMMAKGD SDGDAAALYG VAGSLPNKSV VVDLATGFLD LLYKA
//
