ID A0A094IEV0_9PEZI Unreviewed; 560 AA.
AC A0A094IEV0;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-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=V501_00974 {ECO:0000313|EMBL:KFZ18856.1};
OS Pseudogymnoascus sp. VKM F-4519 (FW-2642).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420914 {ECO:0000313|EMBL:KFZ18856.1, ECO:0000313|Proteomes:UP000029315};
RN [1] {ECO:0000313|EMBL:KFZ18856.1, ECO:0000313|Proteomes:UP000029315}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4519 (FW-2642) {ECO:0000313|Proteomes:UP000029315};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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, ECO:0000256|RuleBase:RU000382};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family. Sphingosine-
CC 1-phosphate lyase subfamily. {ECO:0000256|ARBA:ARBA00038302}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFZ18856.1}.
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DR EMBL; JPKD01000321; KFZ18856.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094IEV0; -.
DR STRING; 1420914.A0A094IEV0; -.
DR HOGENOM; CLU_028929_1_0_1; -.
DR Proteomes; UP000029315; 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:UP000029315}.
FT MOD_RES 349
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 560 AA; 60196 MW; 2B10FC34889846C4 CRC64;
MPISLRNTIA ARAGGSGTQL LSLNIDLLRN IIFFLFLWRW TKKAYLKLKG RGFAGSTIDG
YVSVRRTLYG LFLRAPGVRT QVQKQVNEAI TKLQAKLIQS GPGITRHLTL PKEGWTDETV
QKELETLANM DHTKWEDGYV SGAVYHGGDD LIKLQTEAFG KFTVANPIHP DVFPGVRKME
AEIVAMVLGI FNAPPGAAGA TTSGGTESIL MACLSARQKA YVERGVTEPE MILPDTGHTA
FHKAGHYFGI KVHLVACPAP SYQVSIPAVS RLINGNTILL VGSAPNFPHG IIDDISALSK
LAVARRIPLH VDCCLGSFLV PFLGAAGFPA PLFDFRLRGV TSISCDTHKY GFAPKGNSTI
LYRSAKLRTY QYFIAPDWSG GVYASPNMAG SRPGALIAGC WASLMRVGEA GYIASAHEIV
GAARSIAEAV RTNPSLSTDL QIVGEPLVSV VAVRSSTLDI YDIADGMSGK GWHLNALQNP
PAVHMAVTLP VAKVWQKFIT DLEAVVEAER EKERERGVNG RKKGEARGDS AALYGVAGSL
PNKSVVVELA GGFLDTLYKA
//
