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Database: UniProt
Entry: A0A093CIH2_TAUER
LinkDB: A0A093CIH2_TAUER
Original site: A0A093CIH2_TAUER 
ID   A0A093CIH2_TAUER        Unreviewed;       558 AA.
AC   A0A093CIH2;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   24-JAN-2024, entry version 24.
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=N340_04532 {ECO:0000313|EMBL:KFV12804.1};
OS   Tauraco erythrolophus (Red-crested turaco).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Musophagiformes; Musophagidae; Tauraco.
OX   NCBI_TaxID=121530 {ECO:0000313|EMBL:KFV12804.1, ECO:0000313|Proteomes:UP000053661};
RN   [1] {ECO:0000313|EMBL:KFV12804.1, ECO:0000313|Proteomes:UP000053661}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_N340 {ECO:0000313|EMBL:KFV12804.1};
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}.
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DR   EMBL; KL460790; KFV12804.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A093CIH2; -.
DR   Proteomes; UP000053661; 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:UP000053661}.
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:KFV12804.1"
FT   NON_TER         558
FT                   /evidence="ECO:0000313|EMBL:KFV12804.1"
SQ   SEQUENCE   558 AA;  61931 MW;  D1D2CD34D4925237 CRC64;
     AIIPYKEILQ MYWEKATSFV NAQCDGLEPW QLIALTFSST LLSVWLHGFL FQAESLTSRI
     KKQFFKLLRK MPFVGALIQK KIDEALNDVT SSLSFLKDEK DYIKALPEQG MSQPEVLEKM
     KEYSSKGDVR WQDGKVSGTV YSGEEKLTRL LVKVYEQFAW SNPLHPDIFP GLRKMEAEVV
     RIACTLFNGG PSSCGAMTSG GTESILMACK AYRDLAYERG IKQPEMLVPV SAHAAFDKAA
     HYFGLKLIHI PLTKAMEVDV QAMRRAISRN TAMLVCSAPQ FPHGIMDPIE EVAELAVKYK
     IPFHVDACLG GFLIAFMDKA GFPLKRLFDF RVKGVTSISA DTHKYGYAPK GSSVVLYSDK
     KYRSYQFFIA PDWQGGIYAS PSAAGSRPGG IIAACWATLM HIGESGYVEA TKRIIKTTRF
     LESELRKIDS IFIFGKPEVS VLSIGSDTFD IYRLSNLLAA KGWNLNALQF PSSIHLCVTQ
     LHTKSGVAEQ FVKDVKDSIE EIMKDLNAKT TGMGAIYGMA QSVPDRSLVA EISQAYLDGL
     YSTDVPCSEK HMNGSPGH
//
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