ID A0A151X3N5_9HYME Unreviewed; 544 AA.
AC A0A151X3N5;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 25.
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=ALC60_06130 {ECO:0000313|EMBL:KYQ55001.1};
OS Trachymyrmex zeteki.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Hymenoptera; Apocrita; Aculeata; Formicoidea;
OC Formicidae; Myrmicinae; Trachymyrmex.
OX NCBI_TaxID=64791 {ECO:0000313|EMBL:KYQ55001.1, ECO:0000313|Proteomes:UP000075809};
RN [1] {ECO:0000313|EMBL:KYQ55001.1, ECO:0000313|Proteomes:UP000075809}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Tzet28-1 {ECO:0000313|EMBL:KYQ55001.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KYQ55001.1};
RA Nygaard S., Hu H., Boomsma J., Zhang G.;
RT "Trachymyrmex zeteki WGS genome.";
RL Submitted (SEP-2015) 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; KQ982558; KYQ55001.1; -; Genomic_DNA.
DR RefSeq; XP_018304225.1; XM_018448723.1.
DR AlphaFoldDB; A0A151X3N5; -.
DR STRING; 64791.A0A151X3N5; -.
DR GeneID; 108723179; -.
DR OrthoDB; 3024111at2759; -.
DR Proteomes; UP000075809; 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:UP000075809}.
FT MOD_RES 344
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 544 AA; 61422 MW; 341295188E479AF1 CRC64;
MIYFKKNMYF HVDTIPRAIN HIFQNKEPWQ IAAMTSTATL ATVWLWTFIY QDESLLERGK
KQMFRLARYI PSIRDKINEE LAKVNETFEN DVLRRFKETS FIVHLPKNGL KNDELLSLVN
QYIYLGDYDW KRGRVSGAVY RTNSKLTELI GNVYAIASYT NPLHPDVFPG ICKMEAEVVR
IACHLFNGDK DSCGTMTSGG TESILLACKA YRDYARDVKG IKKPEIVLPV TAHAAFDKAA
QYLKIKVCYV PVHSHSFTVC IQTMKKSITK NTIMLVGSAP NFPYGTMDNI EAISEVGIKY
DIPVHVDGCL GGFLACFMSD AGYPLSPFDF KLSGVTSISA DTHKYAYAPK GSSLILYRNK
EYRHYQYTIT TDWPGGIYGS PTISGSRAGG IIATCWATLL HYGFDEYVES TKKIIETTRY
IERKLREMDG IFIFGTPATS VIAIGSNDFH IYRLSEALIN KGWNLNPLQF PCGIHICVTH
VHTEPGVADQ FLENVNAELE IIMKDRNVPV KGKLAMYGMS QSIPDRSVVS EITKSFLDSM
YYTE
//