ID A0A1B8EP36_9PEZI Unreviewed; 566 AA.
AC A0A1B8EP36;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=VF21_08913 {ECO:0000313|EMBL:OBT73127.1}, VF21_08941
GN {ECO:0000313|EMBL:OBT73109.1};
OS Pseudogymnoascus sp. 05NY08.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1622149 {ECO:0000313|EMBL:OBT73109.1, ECO:0000313|Proteomes:UP000092096};
RN [1] {ECO:0000313|EMBL:OBT73109.1, ECO:0000313|Proteomes:UP000092096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=05NY08 {ECO:0000313|EMBL:OBT73109.1,
RC ECO:0000313|Proteomes:UP000092096};
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Comparative genomics of Pseudogymnoascus destructans, the fungus causing
RT white-nose syndrome of bats.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000092096}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=05NY08 {ECO:0000313|Proteomes:UP000092096};
RX PubMed=29295979; DOI=10.1038/s41467-017-02441-z;
RA Palmer J.M., Drees K.P., Foster J.T., Lindner D.L.;
RT "Extreme sensitivity to ultraviolet light in the fungal pathogen causing
RT white-nose syndrome of bats.";
RL Nat. Commun. 9:35-35(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; KV458870; OBT73109.1; -; Genomic_DNA.
DR EMBL; KV458870; OBT73127.1; -; Genomic_DNA.
DR STRING; 1622149.A0A1B8EP36; -.
DR OrthoDB; 3024111at2759; -.
DR Proteomes; UP000092096; 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:UP000092096}.
FT MOD_RES 355
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 566 AA; 60842 MW; 30194F0796DD9B71 CRC64;
MPGTSRMPIS LRNTIAARTG GSGTQLLSLN IDLLRNIIFF LFLWRWTKKA YLKLKGRGLA
GSTIDGYVSV RRTLYGLFLR APGVRTQVQK QVNEAITKLQ AKLIQSGPGI TRHLTLPKEG
WTDETVQKEL ETLANMDHTK WEDGYVSGAV YHGGDDLIKL QTEAFGKFTV ANPIHPDVFP
GVRKMEAEIV AMVLGIFNAP PGAAGATTSG GTESILMACL SARQKAYVER GVTEPEMILP
DTGHTAFHKA GHYFGIKVHL VACPAPTYQV SIPAVSRLIN SNTILLVGSA PNFPHGIIDD
ISALSKLAVA RRIPLHVDCC LGSFLVPFLG AAGFPAPLFD FRLRGVTSIS CDTHKYGFAP
KGNSTVLYRT AKLRTYQYFI AADWSGGVYA SPNMAGSRPG ALIAGCWASL MRVGESGYIA
SAHEIVGAAR SIADAVRTNP SLSTDLQIVG EPLVSVVAVR SSTLDIYDIA DGMSGKGWHL
NALQNPPAVH MAVTLPVAKV WQKFITDLEA VVEAEREKER ERGVNGRKKG EARGDSAALY
GVAGSLPNKS VVVELAGGFL DTLYKA
//