ID A0A091K9W3_COLST Unreviewed; 559 AA.
AC A0A091K9W3;
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=N325_10071 {ECO:0000313|EMBL:KFP32983.1};
OS Colius striatus (Speckled mousebird).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC Coelurosauria; Aves; Neognathae; Coliiformes; Coliidae; Colius.
OX NCBI_TaxID=57412 {ECO:0000313|EMBL:KFP32983.1, ECO:0000313|Proteomes:UP000053615};
RN [1] {ECO:0000313|EMBL:KFP32983.1, ECO:0000313|Proteomes:UP000053615}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BGI_N325 {ECO:0000313|EMBL:KFP32983.1};
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; KK548204; KFP32983.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A091K9W3; -.
DR Proteomes; UP000053615; 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:UP000053615}.
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:KFP32983.1"
FT NON_TER 559
FT /evidence="ECO:0000313|EMBL:KFP32983.1"
SQ SEQUENCE 559 AA; 62062 MW; CD19457AB126989A CRC64;
AILPYKEVFQ MYWEKTTSFV NACCDGLEPW QLVGLTFSST LLSVWLHGFL FQSESLTSRI
KKQFFKLLRK MPFVGAIIQK KIDEALNDVT SSLSFLKDEK DYIKALPEQG MSQPEVLEKM
KEYSSKGDVR WQDGKVSGTV YSGEENLTRL LVKVYEEFAW SNPLHPDIFP GLRKMEAEVV
RIACTLFNGG PNSCGAMTSG GTESILMACK AYRDLAYERG IKQPEMLVPV SAHAAFDKAA
HYFGLKLIHI PLTKAMEVDV QAMKRAISKN TAMLVCSAPQ FPHGIMDPIE EVAELAVKYK
IPFHVDACLG GFLIAFMDKA GFPLKRPFDF RVKGVTSISA DTHKYGYAPK GSSVVLYSDK
KYRSYQFFIA PDWQGGIYAS PSVAGSRPGG IIAACWATLL HIGESGYVEA TKRIIKTARF
LESELRKIDS IFIFGKPEVS VISIGSHTFD IYRLSNLLAA KGWNLNVLQF PSSIHLCITQ
LHTKSGVAEQ FLKDVKDSIE EIKKDLNAKT TGMGAIYGMA QSVPDRSLIA EISQAYLDGL
YSTDVPCGEK HMNGSPGHH
//
