ID A0A0F7ZME2_9HYPO Unreviewed; 566 AA.
AC A0A0F7ZME2;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 31.
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=HIM_08660 {ECO:0000313|EMBL:KJZ71980.1};
OS Hirsutella minnesotensis 3608.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Hirsutella.
OX NCBI_TaxID=1043627 {ECO:0000313|EMBL:KJZ71980.1, ECO:0000313|Proteomes:UP000054481};
RN [1] {ECO:0000313|EMBL:KJZ71980.1, ECO:0000313|Proteomes:UP000054481}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=3608 {ECO:0000313|EMBL:KJZ71980.1,
RC ECO:0000313|Proteomes:UP000054481};
RX PubMed=25359922; DOI=10.1093/gbe/evu241;
RA Lai Y., Liu K., Zhang X., Zhang X., Li K., Wang N., Shu C., Wu Y., Wang C.,
RA Bushley K.E., Xiang M., Liu X.;
RT "Comparative genomics and transcriptomics analyses reveal divergent
RT lifestyle features of nematode endoparasitic fungus Hirsutella
RT minnesotensis.";
RL Genome Biol. Evol. 6:3077-3093(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}.
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DR EMBL; KQ030556; KJZ71980.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0F7ZME2; -.
DR OrthoDB; 3024111at2759; -.
DR Proteomes; UP000054481; 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:UP000054481}.
FT MOD_RES 354
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 566 AA; 61695 MW; 4CC0D8ECBAFD1EE7 CRC64;
MPGSSRMPVS LRGGFESVKR RRPALSLSMI NLDLLRNVVF FYFVLRWTRR AFWKLKGYGI
IGALLELYRD IQRTLYGYFL RAPGVRGKVQ KQVQDSLAKM SAKMVPESQT RYLTLPKEGL
PADTIRAELE ALATMDHTRW EDGFVSGAVY HGEEDLIQLQ TEAFGKFTVA NPIHPDVFPG
VRKMEAEVVS MVLNMFHAPP GAAGVSTAGG TESILMACLA ARQKAYAERG VTEPEMIIPN
TAHTAFRKAG EYFNIKIHMV ACPAPDYQAD IRAMSRLINS NTVLLVGSAP NFPHGIIDDI
AAMSKLALRK KLCLHVDCCL GSFMIPCLEK AGFETQPFDF RLKGVTSISC DTHKYGFAPK
GNSTVLYRTA ALRTYQYYVC PDWSGGVYAS PGMAGSRPGA LIAGCWASLM TVGEAGYVDA
CGKIVGTAKK IADAIRDGPA LSGELEILGK PLVSVVAFTA RNLNIYDIAD GMSHKGWHLN
ALQSPPAIHV AVTLPIVKVW ERLVSDLEAV VEEEREKERV RLVEGKGAKG NAVGDSAALY
GVAGSLPNKS VVVDLARGFL DLLYKA
//
