ID A0A1J7JCC4_9PEZI Unreviewed; 568 AA.
AC A0A1J7JCC4;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
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=CONLIGDRAFT_428160 {ECO:0000313|EMBL:OIW27400.1};
OS Coniochaeta ligniaria NRRL 30616.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Sordariomycetidae; Coniochaetales; Coniochaetaceae; Coniochaeta.
OX NCBI_TaxID=1408157 {ECO:0000313|EMBL:OIW27400.1, ECO:0000313|Proteomes:UP000182658};
RN [1] {ECO:0000313|EMBL:OIW27400.1, ECO:0000313|Proteomes:UP000182658}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NRRL 30616 {ECO:0000313|EMBL:OIW27400.1,
RC ECO:0000313|Proteomes:UP000182658};
RG DOE Joint Genome Institute;
RA Jimenez D.J., Hector R.E., Riley R., Sun H., Grigoriev I.V.,
RA Van Elsas J.D., Nichols N.N.;
RT "Draft genome sequence of Coniochaeta ligniaria NRRL30616, a
RT lignocellulolytic fungus for bioabatement of inhibitors in plant biomass
RT hydrolysates.";
RL Submitted (OCT-2016) 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}.
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DR EMBL; KV875099; OIW27400.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1J7JCC4; -.
DR STRING; 1408157.A0A1J7JCC4; -.
DR InParanoid; A0A1J7JCC4; -.
DR OrthoDB; 3024111at2759; -.
DR Proteomes; UP000182658; 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:0016740; F:transferase activity; IEA:UniProtKB-KW.
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:UP000182658};
KW Transferase {ECO:0000313|EMBL:OIW27400.1}.
FT MOD_RES 360
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 568 AA; 62517 MW; E6F02A9EE5B844B1 CRC64;
MPGTSRMPVS LRESFNNVRN KARARRPVWS NPLQVLSIDL IRQIVFFLFV LRWTRRALWK
LKGRGLLGTI VELYTDAYRA LYGYFLRLPG VRTTVRKQVD EAIAKMSVKL VPTNATRYLT
LPKEGWSEEA VRKELDTLAN MDHTRWEDGY VSGAVYHGEA DLMRLQTEAY GKFTVANPIH
PDVFPGVRKM EAEIVSMVLN LFNAPPGAAG TCTIGGTESI LMACLSARQK GYAERGITEP
EMILPETAHT AFRKAGEYFK IKIHLVPCPA PAYQVDVRRV SRLINPNTVL LVGSAPNFPH
GIIDDISALS KLALRRRVPL HVDCCLGSFL VPFLEQAGFE TQPFDFRLKG VTSISCDTHK
YGFAPKGNST VLYRTEQLRS YQYFVDPSWS GGVYASPGAA GSRPGALLAA CWASLVSVGQ
SGYLDACARI VGCAKQLAER IGANPELEII GRPLVSVVAF RARDLNVYDI ADAMGARGWH
LNALQNPPAM HVAVTLPIVK VWERLARDLD EVVEAEREKE RVRVVQGKGA RGAATGDAAA
LYGVAGSLPN KSVVVDLAKG FLDLCYKA
//
