ID A0A087QMU9_APTFO Unreviewed; 559 AA.
AC A0A087QMU9;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 23.
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};
DE Flags: Fragment;
GN ORFNames=AS27_09478 {ECO:0000313|EMBL:KFM02553.1};
OS Aptenodytes forsteri (Emperor penguin).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC Aptenodytes.
OX NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM02553.1, ECO:0000313|Proteomes:UP000053286};
RN [1] {ECO:0000313|EMBL:KFM02553.1, ECO:0000313|Proteomes:UP000053286}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM02553.1};
RA Zhang G., Li C.;
RT "Genome evolution of avian class.";
RL Submitted (APR-2014) 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}.
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; KL225745; KFM02553.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A087QMU9; -.
DR STRING; 9233.A0A087QMU9; -.
DR Proteomes; UP000053286; 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 CDD; cd06450; DOPA_deC_like; 1.
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:UP000053286}.
FT MOD_RES 344
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KFM02553.1"
FT NON_TER 559
FT /evidence="ECO:0000313|EMBL:KFM02553.1"
SQ SEQUENCE 559 AA; 62152 MW; 6B5A24BF7080BF30 CRC64;
AIIPYKEILQ MYWEKATSFV NAQCNGLEPW QLIGLTFSST LISVWLHGFL FQSESLTSRT
KKQFFKLLRK MPFIGAIIQK KIDEALNDVT SSLSFLKDEK DYIKALPEKG MSQPEVLEKM
KEYSSKGDVR WQDGKVSGTV YSGEEKLTHL LVKVYEEFAW SNPLHPDIFP GLRKMEAEVV
RIACTLFNGG PNSCGAMTSG GTESILMACK AYRDLAYERG IKQPEMLVPV SAHAAFDKAA
HYFGLKLIHI PLTKAMEVDV QAMRRAISKN TAMLVCSAPQ FPHGIMDPIE EVAELAVKYK
IPFHIDACLG GFLIAFMDKA GFPLKRPFDF RVKGVTSISA DTHKYGYAPK GSSVVLYSDK
KYRSYQFFIA ADWQGGIYAS PSVAGSRPGG IIAACWATLM HIGESGYVEA TKRIIKTARF
LESELRKIDS IFIFGKPEVS VLSIGSDTFD IYRLSNFLAA KGWNLNVLQF PSSIHLCITQ
LHTKPGVAEQ FLKDVKDSIE EIMKDLNAKT TGMGAIYGMA QSVPDRSLVA EISQAYLDSL
YSTDVPCSEK HMNGSPGHH
//
