ID A0A0V0QIY0_PSEPJ Unreviewed; 939 AA.
AC A0A0V0QIY0;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 26.
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=PPERSA_04827 {ECO:0000313|EMBL:KRX02205.1};
OS Pseudocohnilembus persalinus (Ciliate).
OC Eukaryota; Sar; Alveolata; Ciliophora; Intramacronucleata;
OC Oligohymenophorea; Scuticociliatia; Philasterida; Pseudocohnilembidae;
OC Pseudocohnilembus.
OX NCBI_TaxID=266149 {ECO:0000313|EMBL:KRX02205.1, ECO:0000313|Proteomes:UP000054937};
RN [1] {ECO:0000313|EMBL:KRX02205.1, ECO:0000313|Proteomes:UP000054937}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=36N120E {ECO:0000313|EMBL:KRX02205.1};
RX PubMed=26486372; DOI=10.1038/srep15470;
RA Xiong J., Wang G., Cheng J., Tian M., Pan X., Warren A., Jiang C., Yuan D.,
RA Miao W.;
RT "Genome of the facultative scuticociliatosis pathogen Pseudocohnilembus
RT persalinus provides insight into its virulence through horizontal gene
RT transfer.";
RL Sci. Rep. 5:15470-15470(2015).
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}.
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:KRX02205.1}.
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; LDAU01000156; KRX02205.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0V0QIY0; -.
DR EnsemblProtists; KRX02205; KRX02205; PPERSA_04827.
DR InParanoid; A0A0V0QIY0; -.
DR OrthoDB; 3024111at2759; -.
DR Proteomes; UP000054937; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0016830; F:carbon-carbon lyase activity; IEA:InterPro.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR GO; GO:0019752; P:carboxylic acid metabolic process; IEA:InterPro.
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}; Membrane {ECO:0000256|SAM:Phobius};
KW Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR602129-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000054937};
KW Transferase {ECO:0000313|EMBL:KRX02205.1};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 72..91
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT REGION 723..751
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 398
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR602129-50"
SQ SEQUENCE 939 AA; 108618 MW; 32233E31386B01CA CRC64;
MEQVTKIFND LQSHFQEQYQ PIIMHYLHKY NLPTSFQELR QDVYNIQRPF THGLETKLDY
FVKDYNITQF ELVILTIIVL IVVQKLVSFL ICREKYRLYR DVDDRTLGWF ETKKRDIQSG
IFQFLYNNIP FIRNKVDGKL AAAKEGFEKK MIEPFRNVTY QLPGNPLSND KIRQKMNEFY
VGDEKLSGQG KLSGTRYALS KYESEMKEFV KDFIFHNPLH AAEFPGSRQM EAEVIKMTCK
LYGSNDDFGI TTQGGTESIM MGVLAHRNYY QKKKGIQKPN IIMPLSSHIA FNKACYYYNI
VPIIVPLNES GDVNLKEVKK AINKNTIMIV GNSPSYAAGI QDDIPALAKL ALKHDIGLHV
DACLGSFIMP FAKQLGADIL PYDFTVKGVT SISCDHHKYG LAPKGISLCM FKTSELRQAA
YFSYSEWPGG LYATAQPAGS RSSAPIVGAW YAMMYHGEEK YRDNAKQIIK AVQMIRKEIE
ENIPELRIIG DPKLMVIAFY YKKGIKSSIY QLDNELHKRG WSLNGLQKPN SIHVAMTLPF
AQNISQFIKD LRDSVQLLRE DPTLHANSTS GSVGLYGASG EIPDSITKEK VLMQIVDTFT
TLGPEPQKKK NGDQTNQFSY NFPKNSTKIK IPFNQTHVQS SIFEQDLLDK KIFHPDIQSS
LCNLYDQLLQ KIQEKDINGI KNLTTPVFFN QLEKQGFIDF IQNKSTQIQV AKVQEDVQNK
ILEKNEKNGQ KQKNSMFSEK SQQEQEEKEQ NAKKNIFTSI EVIKTYKTLV GLNKLKLRPL
NNYFKIIFPP NMPMQWYFYL SKNPFKQNYN KTIVADCLIN TNNRIKFDNQ IVQNPKNTQQ
NQSKNTQYEN VQIQFTCKAQ HKKKPAPFVY DMEFNKKWEK KMGIKINEEN YNLQYFSSQK
QEDYEKNGWK ISNINNYHIQ DIIEDVLYNN QNGQNQQQN
//
