ID A0A1R3JL82_COCAP Unreviewed; 542 AA.
AC A0A1R3JL82;
DT 12-APR-2017, integrated into UniProtKB/TrEMBL.
DT 12-APR-2017, sequence version 1.
DT 27-MAR-2024, entry version 32.
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=CCACVL1_05340 {ECO:0000313|EMBL:OMO95632.1};
OS Corchorus capsularis (Jute).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; malvids; Malvales; Malvaceae; Grewioideae; Apeibeae; Corchorus.
OX NCBI_TaxID=210143 {ECO:0000313|EMBL:OMO95632.1, ECO:0000313|Proteomes:UP000188268};
RN [1] {ECO:0000313|EMBL:OMO95632.1, ECO:0000313|Proteomes:UP000188268}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=cv. CVL-1 {ECO:0000313|Proteomes:UP000188268};
RC TISSUE=Whole seedling {ECO:0000313|EMBL:OMO95632.1};
RA Alam M., Haque M.S., Islam M.S., Emdad E.M., Islam M.M., Ahmed B.,
RA Halim A., Hossen Q.M.M., Hossain M.Z., Ahmed R., Khan M.M., Islam R.,
RA Rashid M.M., Khan S.A., Rahman M.S., Alam M.;
RT "Corchorus capsularis genome sequencing.";
RL Submitted (SEP-2013) 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OMO95632.1}.
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DR EMBL; AWWV01007617; OMO95632.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1R3JL82; -.
DR STRING; 210143.A0A1R3JL82; -.
DR EnsemblPlants; OMO95632; OMO95632; CCACVL1_05340.
DR Gramene; OMO95632; OMO95632; CCACVL1_05340.
DR OMA; DPHKMGL; -.
DR OrthoDB; 3024111at2759; -.
DR Proteomes; UP000188268; 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 GO; GO:1901564; P:organonitrogen compound metabolic process; IEA:UniProt.
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:UP000188268}.
FT MOD_RES 347
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 542 AA; 59066 MW; 0B8E91856F9CADAC CRC64;
MDSSPSTASF LIRFRGSANS FLSQFEPLAL LLAPFLTLLV ARVFHSFLSV TVEKGLKASL
IGFFMSSIKL FPGVKSYIDA EKQKVVDKLQ SGSKSKRENS RTELPTTGLG VGVIEEMKHE
KSKDVDWQGK CSGTVYIGGS ESEGHFSLIN EACSMFAHTN PLHLDVFQSV ARFEAEVVAM
TAALLGSKEK ASGGQVCGNM TSGGTESILL AVKTSRDFMK MKKGITKPEM IIAESAHSAY
DKAAQYFNIK LRRVPVNKEY QADVKAIRKH INRNTILIVG SAPGFPHGII DPIEDLGKLA
HSYGICLHVD LCLGGFVLPF ARKLGYPIPS FDFTVMGVTS ISVDVHKYGL APKGTSIVLY
RNHDIRKHQF VAVTEWSGGL YVSPTIAGSR PGGLIAGAWA AMMSLGQEGY MEHTRKIMEV
SKMIQKGINE IPEFFIIGRP DMTIVAFGSA VLDIFEVNDI MSAKGWHLNA LQRPNSLHIC
VTLQHVPFVD AFIQDLRDAV KTVKENPGPI SGGLAPIYGA AGRMPDRGMV QELLVNYMDG
TC
//
