ID A0A182E4T6_ONCOC Unreviewed; 570 AA.
AC A0A182E4T6;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 27-MAR-2024, entry version 30.
DE SubName: Full=Sphingosine-1-phosphate lyase 1 {ECO:0000313|WBParaSite:nOo.2.0.1.t03010-RA};
GN ORFNames=NOO_LOCUS3010 {ECO:0000313|EMBL:VDK67655.1};
OS Onchocerca ochengi (Filarial nematode worm).
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Spirurina; Spiruromorpha; Filarioidea; Onchocercidae; Onchocerca.
OX NCBI_TaxID=42157 {ECO:0000313|Proteomes:UP000077448, ECO:0000313|WBParaSite:nOo.2.0.1.t03010-RA};
RN [1] {ECO:0000313|Proteomes:UP000077448}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=22919073; DOI=10.1101/gr.138420.112;
RA Darby A.C., Armstrong S.D., Bah G.S., Kaur G., Hughes M.A., Kay S.M.,
RA Koldkaer P., Rainbow L., Radford A.D., Blaxter M.L., Tanya V.N.,
RA Trees A.J., Cordaux R., Wastling J.M., Makepeace B.L.;
RT "Analysis of gene expression from the Wolbachia genome of a filarial
RT nematode supports both metabolic and defensive roles within the
RT symbiosis.";
RL Genome Res. 22:2467-2477(2012).
RN [2] {ECO:0000313|WBParaSite:nOo.2.0.1.t03010-RA}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (JUN-2016) to UniProtKB.
RN [3] {ECO:0000313|EMBL:VDK67655.1, ECO:0000313|Proteomes:UP000271087}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Laetsch R D., Stevens L., Kumar S., Blaxter L. M.;
RL Submitted (AUG-2018) 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; UYRW01000532; VDK67655.1; -; Genomic_DNA.
DR STRING; 42157.A0A182E4T6; -.
DR WBParaSite; nOo.2.0.1.t03010-RA; nOo.2.0.1.t03010-RA; nOo.2.0.1.g03010.
DR Proteomes; UP000077448; Unassembled WGS sequence.
DR Proteomes; UP000271087; 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:SF16; SPHINGOSINE PHOSPHATE LYASE; 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:UP000271087}.
FT MOD_RES 351
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 570 AA; 64331 MW; EADA37A67B18B613 CRC64;
MDEWWTLDGG HTWRLVAQVV DDGRVAFNRA FVHLEPWQIV SYTLSIACLF IWLQRLLKAD
RPLSTRIRAA IFSAFRMIPW VKAQIKEEME KARRDLEETI HQYDKKKEFY KFLPEHGLAS
SNIIHEAELY KTMSEFSFYD GRVSGVIFAD VDEEHRALLQ KMFELFAYSD PLYPNLFPGC
RKMEAEIVRI IASLLHGGPG SCGTVTSNDT ESNMLACFAY RNRAFARGIR HPEMLVPVTA
HAAFDKAAKV LQMRIRHISV DKNHRVDVGA MKRAINNETC MLVASAPNYS FGTIDNIEAI
SELSQRYGIP LHVDASLGGF ILSIMERCDF AVKSFDFRVP GVTSISCDVQ KYGFAPNGTS
LILYRDSSLL HHQYFCNSEW PGGIYMTPTL AGNRDGCAIA LTWATLLYNG RQGYTERIEA
IINTVREIRT GIEKCPHMQL LCESDVATVV FTTRGLNVYA LADRMNKLGW VLTTLQNPPA
VNVCVTLNHT KSGVVENFIR ELNMACEDLV LNPEFSQQSR TAAIYGMVSA VPDLVEEVSH
MYLDSCYAMP LPPTGRTLSF EGRKKSLIPD
//
