ID A0A0D9UVQ2_9ORYZ Unreviewed; 948 AA.
AC A0A0D9UVQ2;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 05-FEB-2025, entry version 43.
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};
OS Leersia perrieri.
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC Oryzoideae; Oryzeae; Oryzinae; Leersia.
OX NCBI_TaxID=77586 {ECO:0000313|EnsemblPlants:LPERR01G00060.2, ECO:0000313|Proteomes:UP000032180};
RN [1] {ECO:0000313|EnsemblPlants:LPERR01G00060.2, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Wing R.A.;
RT "Oryza genome evolution.";
RL Submitted (AUG-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblPlants:LPERR01G00060.2, ECO:0000313|Proteomes:UP000032180}
RP NUCLEOTIDE SEQUENCE.
RA Yu Y., Lee S., de Baynast K., Wissotski M., Liu L., Talag J.,
RA Goicoechea J., Angelova A., Jetty R., Kudrna D., Golser W., Rivera L.,
RA Zhang J., Wing R.;
RL Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EnsemblPlants:LPERR01G00060.2}
RP IDENTIFICATION.
RG EnsemblPlants;
RL Submitted (APR-2015) to UniProtKB.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR602129-50};
CC -!- SIMILARITY: Belongs to the group II decarboxylase family. Sphingosine-
CC 1-phosphate lyase subfamily. {ECO:0000256|ARBA:ARBA00038302}.
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DR AlphaFoldDB; A0A0D9UVQ2; -.
DR STRING; 77586.A0A0D9UVQ2; -.
DR EnsemblPlants; LPERR01G00060.2; LPERR01G00060.2; LPERR01G00060.
DR Gramene; LPERR01G00060.2; LPERR01G00060.2; LPERR01G00060.
DR eggNOG; KOG1383; Eukaryota.
DR HOGENOM; CLU_310447_0_0_1; -.
DR Proteomes; UP000032180; Chromosome 1.
DR GO; GO:0005783; C:endoplasmic reticulum; IEA:TreeGrafter.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008117; F:sphinganine-1-phosphate aldolase activity; IEA:TreeGrafter.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
DR GO; GO:0030149; P:sphingolipid catabolic process; IEA:TreeGrafter.
DR FunFam; 3.40.640.10:FF:000020; sphingosine-1-phosphate lyase 1; 1.
DR FunFam; 3.90.1150.10:FF:000020; Sphingosine-1-phosphate lyase 1; 1.
DR FunFam; 6.10.140.2150:FF:000001; Sphingosine-1-phosphate lyase 1; 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; IPR012458; DUF1664.
DR InterPro; IPR050477; GrpII_AminoAcid_Decarb.
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; PF07889; DUF1664; 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}; Membrane {ECO:0000256|SAM:Phobius};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR602129-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000032180};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 87..109
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 183..303
FT /note="DUF1664"
FT /evidence="ECO:0000259|Pfam:PF07889"
FT REGION 1..81
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 309..418
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..22
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 41..57
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 326..339
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 375..394
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 397..418
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 753
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 948 AA; 102614 MW; F6AA6AB37D1D3825 CRC64;
MVMDSKVKSM KRDEEESYRR DEEATDLPWR TRTGESGPSR QRFDEQSNAK EGNEHRPALL
ARGRSGAGKR VPNPSCPDDR AGVRRPVAAA MVLGKIAIVI GSGIVGTILT SGDSKIALPD
FRGVLSGALK FVTKQDKKDG PSTSSPHTDH LLSQVNHLRE ELQQLARSNQ VAIVTVDGRP
GPGAYGITAV VAGAIGYLYI RWKGWKLSDL MFVTKRGLSD ACNVVGSQLD QVSENVNAAK
KHLAGRIDRV DCTLDECQEI TEATRKEVTV IHGDISAFQE EMQSVHLVVR TLETKLGRLA
YTQVLPSTPL PAIESPERLT RAASLPPNSE PESSGTRSPV TEAPKVVRSP TAMSASGLSM
LIETSMPPKR GAFSRASSMK EGSQEPSNRA SSSGEPIIER HVSNSRLREE KRREKRMDSA
ARRLRDAANE HLARCEPLVL LIAPLLALLA ARTLHAAAAA VADRGLLALA MAAIKLLPGV
SAYIDAEKRK VVDQLQSGGT STKSSLRTEL PTVGLSNEVI SDLETLKARD VTWQGKCSGT
VYIAGSESEG HFALVNKAYS MFSHTNPLHQ DVFKSVAQLE AEVVAMTAAL LGSKEKSSGG
QICGNMTSGG TESILLAVKT SRDYMRSKKG ITKPEMIIAE SAHSAYDKAA QYFNIKVRRV
PVNKEFLADV KGFKRCINGN TIMMVGSAPG FPHGLIDPIE ELGELASRYD ICLHVDLCLG
GFVLPFARKL GYPIPPFDFC VKGVTSISSD VHKYGLAPKG TSIVLYRNHE IRKHQFVAVT
EWTGGLYVSP TIAGSRPGGL IAGAWAAMMS LGLNGYMENT GHIMEVSKKI QRGIEDIPGL
FVIGKPDMTV VAFGSDMVDI FEVNDIMSSK GWHLNALQRP NSIHICVTLQ HTSVYEEFLK
DLKDSVDTVK ANPGPISGGR APIYGAAGKM PDRGMIRELL VEFMDTSC
//
