ID A0A1V6XKF8_PENNA Unreviewed; 572 AA.
AC A0A1V6XKF8;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
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=PENNAL_c0071G01437 {ECO:0000313|EMBL:OQE75652.1},
GN PNAL_LOCUS9185 {ECO:0000313|EMBL:CAG8271474.1};
OS Penicillium nalgiovense.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Penicillium.
OX NCBI_TaxID=60175 {ECO:0000313|EMBL:OQE75652.1, ECO:0000313|Proteomes:UP000191691};
RN [1] {ECO:0000313|EMBL:OQE75652.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 13039 {ECO:0000313|EMBL:OQE75652.1};
RA Nielsen J.C., Nielsen J.;
RT "Uncovering the secondary metabolism of Penicillium species provides
RT insights into the evolution of 6-MSA pathways.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000191691}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=IBT 13039 {ECO:0000313|Proteomes:UP000191691};
RX PubMed=28368369; DOI=10.1038/nmicrobiol.2017.44;
RA Nielsen J.C., Grijseels S., Prigent S., Ji B., Dainat J., Nielsen K.F.,
RA Frisvad J.C., Workman M., Nielsen J.;
RT "Global analysis of biosynthetic gene clusters reveals vast potential of
RT secondary metabolite production in Penicillium species.";
RL Nat. Microbiol. 2:17044-17044(2017).
RN [3] {ECO:0000313|EMBL:CAG8271474.1}
RP NUCLEOTIDE SEQUENCE.
RA Branca A.L. A.;
RL Submitted (JUL-2021) 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:OQE75652.1}.
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DR EMBL; CAJVNV010000614; CAG8271474.1; -; Genomic_DNA.
DR EMBL; MOOB01000071; OQE75652.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V6XKF8; -.
DR STRING; 60175.A0A1V6XKF8; -.
DR OMA; DPHKMGL; -.
DR OrthoDB; 3024111at2759; -.
DR Proteomes; UP000191691; Unassembled WGS sequence.
DR Proteomes; UP001153461; 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:UP000191691}.
FT MOD_RES 359
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 572 AA; 62314 MW; A9C5AB37462E9918 CRC64;
MSSSMLPVAL QNKLVGYGRV SSAHLSASNL DLIRNIVFIL FILRYTRKTF YSIRGYGILG
SIRNIYISLR LFCYSIFLRV PGVSGQVDKQ VSTAITNLES KLVNSGPDVT RYLTLPKEGW
SPEQVRVELD KLAGLEHTRW EDGRVSGAVY HGGAELLKLQ AEAFGQFGVA NPIHPDVFPG
VRKMEAEVVA MVLALFNAPS DGAGVTTSGG TESILMACLA ARQKAFLERG VTEPEMIIPD
TAHAAFIKAC NYFKIKLHRV PCPEPEFKVD VHAVRRLINP NTVLLVGSAP NFPHGIVDDI
PALSHLATKY KIPLHVDCCL GSFVIAHLKK AGFPSPYEEE GGFDFRQPGV TSISVDTHKY
GFAPKGNSVL IYRNKSYRNN QYFIYPDWSG GVYASPSVAG SRPGALIAGC WASLMSVGEA
GYINSCTDII NAARKFETAV RTDSTISLHM EVIGNPIVSV VAFRSKNGAI DIYDIADDLS
TKGWHLNALQ SPPAIHCAFT IPTAKAVDQL IADLTEVIGK ELEKAEQRKR EGKSYILKRG
DTSALYGVAG SIPDKSVVSR LAEGFLDTLY KA
//
