ID A0A3N2Q9C2_9PEZI Unreviewed; 566 AA.
AC A0A3N2Q9C2;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 24-JAN-2024, entry version 18.
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=SODALDRAFT_327445 {ECO:0000313|EMBL:ROT43258.1};
OS Sodiomyces alkalinus F11.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Plectosphaerellaceae; Sodiomyces.
OX NCBI_TaxID=1314773 {ECO:0000313|EMBL:ROT43258.1, ECO:0000313|Proteomes:UP000272025};
RN [1] {ECO:0000313|EMBL:ROT43258.1, ECO:0000313|Proteomes:UP000272025}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F11 {ECO:0000313|EMBL:ROT43258.1,
RC ECO:0000313|Proteomes:UP000272025};
RX PubMed=30368956; DOI=10.1111/mec.14912;
RA Grum-Grzhimaylo A.A., Falkoski D.L., van den Heuvel J.,
RA Valero-Jimenez C.A., Min B., Choi I.G., Lipzen A., Daum C.G., Aanen D.K.,
RA Tsang A., Henrissat B., Bilanenko E.N., de Vries R.P., van Kan J.A.L.,
RA Grigoriev I.V., Debets A.J.M.;
RT "The obligate alkalophilic soda-lake fungus Sodiomyces alkalinus has
RT shifted to a protein diet.";
RL Mol. Ecol. 27:4808-4819(2018).
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; ML119051; ROT43258.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N2Q9C2; -.
DR STRING; 1314773.A0A3N2Q9C2; -.
DR OrthoDB; 3024111at2759; -.
DR Proteomes; UP000272025; 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:UP000272025}.
FT MOD_RES 354
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 566 AA; 61974 MW; 49FBD12F9038D71E CRC64;
MPGTSRMPVS LRDSFNQVRR SRNTNPFLVL NLDLIRNIIF ILFVLRWTRR VWWKIKGRGI
IGTIVELYTE LRRVLYGYFL RAPGVRGKVQ KQVGETLAKL QSKMVPTNLT RYVTLPKEGL
SEDAIRAELD TLANMDHTRW EEGYVSGAVY HGEEDLLKLQ TEAFGKFTVA NPIHPDVFPG
VRKMEAEVVA MVLAMFNAPP GAAGACTSGG TDSILMACLS AREKAYREKG ITEPEMILPS
TAHTAFLKAG NYFKIKVHLV ACPAPNYQVD IKAVSRLINK NTILLVGSAP NFPHGIIDDI
SALSKLALRK KICLHVDCCL GSFMVPFLDK AGFDTEPFDF RLKGVTSISC DTHKYGFAPK
GNSTVLYRTA ELRRYQYYVS PDWSGGVYGS PGMAGSRPGA LIAGCWASLV RTGEAGYIDA
CVKIVGAAKK IADKIRTTPA LEAELEIVGR PLASVVAFTA RNLNIYDIAD GMGTKGWHLN
ALQNPPAIHI AVTLPVAKVW ERLMADLEAV VEEEKEKERV RVVEGKGAKG KAVGDSAALY
GVAGSLPNKS VVVDLANGFL DLLYKA
//
