ID B6QPY0_TALMQ Unreviewed; 574 AA.
AC B6QPY0;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 24-JAN-2024, entry version 61.
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=PMAA_040430 {ECO:0000313|EMBL:EEA20186.1};
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA20186.1, ECO:0000313|Proteomes:UP000001294};
RN [1] {ECO:0000313|Proteomes:UP000001294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000313|Proteomes:UP000001294};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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; DS995904; EEA20186.1; -; Genomic_DNA.
DR RefSeq; XP_002151186.1; XM_002151150.1.
DR AlphaFoldDB; B6QPY0; -.
DR STRING; 441960.B6QPY0; -.
DR VEuPathDB; FungiDB:PMAA_040430; -.
DR HOGENOM; CLU_028929_1_0_1; -.
DR OrthoDB; 3024111at2759; -.
DR PhylomeDB; B6QPY0; -.
DR Proteomes; UP000001294; 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:UP000001294}.
FT MOD_RES 361
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 574 AA; 62634 MW; A8E3940E13949A7F CRC64;
MASSLIPASM QSRLMGVSSR NLSSATLTYL NLDLLKNLVF FFFVLRYTRK TFDSLRGYGI
IGSIKRVFAA IRLWVYYIFL RAPGVRGQVD KQVTTAITKL EEKLVRKGPG ITSYLTLPKE
GWTSEQIRTE ITQLTGMEHA KWEEGRVSGA VYHGGEDLSK LQTEAIGSFA VSNPLHPDVF
PGIRKMESEI VAMVLSLFHG PTDGAGVTTS GGTESILMAC LAARQKGRAE RGITEPEMVV
PETVHAAFFK AGNYFGIKVH QVPCPAPDYK VHIPSVRRLI NRNTVLIVGS APNFPHGIVD
DIPALSRLAV KYKIPLHVDC CLGSFVIAFL KKAGFPSPYE EEGGFDFRQP GVTSISVDTH
KYGFAPKGNS VLLYRNRSYR NHQYFIFPEW TGGVYASPSI AGSRSGALIA GCWVSLMSIG
ESGYVASCHQ IMGAAKQFET AIREDPILSA NLEVIGNPQV SVVAFASKNV GIDTYDIADA
MSAKGWHLNA LQDPAAIHVA FTRPTALAVE KLQSELTEVV SAELAKAEER QRQGKSYARQ
RGDTSALYGV AGSLPDKSIV SRLAEGFLDT LYKP
//
