ID S7ZFA5_PENO1 Unreviewed; 572 AA.
AC S7ZFA5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, 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=PDE_03915 {ECO:0000313|EMBL:EPS28969.1};
OS Penicillium oxalicum (strain 114-2 / CGMCC 5302) (Penicillium decumbens).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=933388 {ECO:0000313|EMBL:EPS28969.1, ECO:0000313|Proteomes:UP000019376};
RN [1] {ECO:0000313|EMBL:EPS28969.1, ECO:0000313|Proteomes:UP000019376}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=114-2 / CGMCC 5302 {ECO:0000313|Proteomes:UP000019376};
RX PubMed=23383313; DOI=10.1371/journal.pone.0055185;
RA Liu G., Zhang L., Wei X., Zou G., Qin Y., Ma L., Li J., Zheng H., Wang S.,
RA Wang C., Xun L., Zhao G.-P., Zhou Z., Qu Y.;
RT "Genomic and secretomic analyses reveal unique features of the
RT lignocellulolytic enzyme system of Penicillium decumbens.";
RL PLoS ONE 8:E55185-E55185(2013).
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; KB644411; EPS28969.1; -; Genomic_DNA.
DR AlphaFoldDB; S7ZFA5; -.
DR STRING; 933388.S7ZFA5; -.
DR eggNOG; KOG1383; Eukaryota.
DR HOGENOM; CLU_028929_1_0_1; -.
DR OrthoDB; 3024111at2759; -.
DR PhylomeDB; S7ZFA5; -.
DR Proteomes; UP000019376; 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:UP000019376}.
FT MOD_RES 359
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 572 AA; 62648 MW; 773A903DFA9BA894 CRC64;
MGSSALPVAL QDKLVGYGRA SRARLSAVNL DLFRNIVFIL FLFRYTRKAF YSLRGYGLFG
SIRNIYIAVR LFCYSIFLRA PGVRGQVDKQ VSTAIEKLES KLVQSGPDVD RHLTLPLEGW
TADRVREELN KLAGLEHTRW EDGRVSGAVY HGGEDLLKLQ AGAFEQFGVA NPIHPDVFPG
VRKMEAEVVA MVLSMFNGPS DGAGVTTSGG TESIIMACLG ARQKAFLERG VTEPEMIIPD
TAHAAFIKAC NYFKIKLHRV PCPEPEFKVD VNAVRRLINP NTVLLVGSAP NFPHGMVDDI
PALSRLATKY KIPLHVDCCL GSFIIAHLKK AGFPSPYEEE GGFDFRQPGV TSISVDTHKY
GFAPKGNSVL LYRNKAYRSH QYFIYPDWSG GVYASPSIAG SRPGALIAGC WASMMKVGQD
GYINSCTEII NAARKFESAV RGHPLISLHM EIVGDPMVSV VAFRSKNGAI DTYDIADDLS
AKGWHLNALQ SPPALHCAFT LPTAKAVEQL IADTAECVQR ELDKAEERRR QGKAYILKRG
DASALYGVAG SIPDKSVVSR LAEGFLDTLY KV
//
