ID A0A094H5Z5_9PEZI Unreviewed; 566 AA.
AC A0A094H5Z5;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 24-JAN-2024, entry version 27.
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=V499_01337 {ECO:0000313|EMBL:KFY79692.1};
OS Pseudogymnoascus sp. VKM F-103.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420912 {ECO:0000313|EMBL:KFY79692.1, ECO:0000313|Proteomes:UP000029295};
RN [1] {ECO:0000313|EMBL:KFY79692.1, ECO:0000313|Proteomes:UP000029295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-103 {ECO:0000313|EMBL:KFY79692.1,
RC ECO:0000313|Proteomes:UP000029295};
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:KFY79692.1}.
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DR EMBL; JPKB01000172; KFY79692.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094H5Z5; -.
DR HOGENOM; CLU_028929_1_0_1; -.
DR Proteomes; UP000029295; 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}.
FT MOD_RES 355
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 566 AA; 60842 MW; 1DD5BDE9BAB5A249 CRC64;
MPGTSRMPIS LRNTIAARAG GSGTQLLSLN IDLLRNIIFF LFLWRWTKKA YLKLKGRGFA
GSTIDGYVSV RRTLYGLFLR APGVRTQVQK QVNEAITKLQ AKLIQSGPGI TRHLTLPKEG
WTDETVQKEL ETLANMDHTK WEDGYVSGAV YHGGDDLIKL QTEAFGKFTV ANPIHPDVFP
GVRKMEAEIV AMVLGIFNAP PGAAGATTSG GTESILMACL SARQKAYVER GVTEPEMILP
DTGHTAFHKA GHYFGIKVHL VACPAPSYQV SIPAVSRLIN GNTILLVGSA PNFPHGIIDD
ISALSKLAVA RRIPLHVDCC LGSFLVPFLG AAGFPAPLFD FRLRGVTSIS CDTHKYGFAP
KGNSTILYRS AKLRTYQYFI SPDWSGGVYA SPNMAGSRPG ALIAGCWASL MRVGEAGYIA
SAHEIVGAAR SIAEAVRTNP SLSTDLQIVG EPLVSVVAVR SSTLDIYDIA DGMSGKGWHL
NALQNPPAVH MAVTLPVAKV WQKFITDLEA VVEAEREKER ERGVNGRKKG EARGDSAALY
GVAGSLPNKS VVVELAGGFL DTLYKA
//
