ID U7PN25_SPOS1 Unreviewed; 577 AA.
AC U7PN25;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, 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=HMPREF1624_07261 {ECO:0000313|EMBL:ERS96351.1};
OS Sporothrix schenckii (strain ATCC 58251 / de Perez 2211183) (Rose-picker's
OS disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Ophiostomatales; Ophiostomataceae; Sporothrix.
OX NCBI_TaxID=1391915 {ECO:0000313|EMBL:ERS96351.1, ECO:0000313|Proteomes:UP000018087};
RN [1] {ECO:0000313|Proteomes:UP000018087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 58251 / de Perez 2211183
RC {ECO:0000313|Proteomes:UP000018087};
RX PubMed=24855299; DOI=10.1128/genomea.00446-14;
RA Cuomo C.A., Rodriguez-Del Valle N., Perez-Sanchez L., Abouelleil A.,
RA Goldberg J., Young S., Zeng Q., Birren B.W.;
RT "Genome sequence of the pathogenic fungus Sporothrix schenckii (ATCC
RT 58251).";
RL Genome Announc. 2:E0044614-E0044614(2014).
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 ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; KI440850; ERS96351.1; -; Genomic_DNA.
DR AlphaFoldDB; U7PN25; -.
DR STRING; 1391915.U7PN25; -.
DR eggNOG; KOG1383; Eukaryota.
DR HOGENOM; CLU_028929_1_0_1; -.
DR OrthoDB; 3024111at2759; -.
DR Proteomes; UP000018087; 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:UP000018087}.
FT MOD_RES 353
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 577 AA; 62662 MW; 0894FAB463AEB63B CRC64;
MPGSSSMLIS LRDNISNVRR RPASPLLLLN LDLLRNLVFF FFVLRLTRRT VWKLRGRGFV
GSITELYNDI RRIVFGWFLR LPGVRTKVRQ QVDEALGKME GKLVPVGVIR HTSLPAQGLA
HDEVRRQLES LAELDHMRWE DGRVSGAVYH GEDDLLKLQT EAFGKFTVAN PIHPDVFPGV
RKMEAEVVAM VLALFNGPAG AAGVATSGGT ESILMACLSA RQKAYVERGV TEPEMIIPET
AHTAFHKASQ YYKIKLHLVA CPAPGYQVDV RRVARLINPN TVLLVGSAPN FPHGIIDDIA
ALGRLAVRKR LPLHVDCCLG SFMVPFLEKA GFETAPFDFR VRGVTSISVD THKYGFAPKG
NSVVLYRTAA LRAYQYFVSA DWAGGVYASP GAAGSRPGAL IAGCWASMMA VGESGYLDAC
GRIVGHARKF AEHITTSPVL SPEIEVMGRP LVSVVAFRAR RSAPSTSSSP FTPINIYALS
DAMSARGWHL NALQNPPAIH VAFTMPIVKS FDTLVSDLEA CVEAEREKVR VRAVEGGAKA
TDESGDAAAL YGVAGSLPNK SVVVDLATGF LDLLYKA
//
