PSD_PLAFA
ID PSD_PLAFA Reviewed; 362 AA.
AC Q9GPP8;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 2.
DT 25-MAY-2022, entry version 57.
DE RecName: Full=Phosphatidylserine decarboxylase proenzyme {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000303|PubMed:14651609};
DE EC=4.1.1.65 {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:14651609};
DE Contains:
DE RecName: Full=Phosphatidylserine decarboxylase beta chain {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000305|PubMed:14651609};
DE Contains:
DE RecName: Full=Phosphatidylserine decarboxylase alpha chain {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000305|PubMed:14651609};
DE Flags: Precursor;
OS Plasmodium falciparum.
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Laverania).
OX NCBI_TaxID=5833;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, CLEAVAGE SITE, SUBCELLULAR LOCATION, AND
RP MUTAGENESIS OF GLY-315 AND SER-316.
RC STRAIN=Nigerian;
RX PubMed=14651609; DOI=10.1046/j.1365-2958.2003.03822.x;
RA Baunaure F., Eldin P., Cathiard A.M., Vial H.;
RT "Characterization of a non-mitochondrial type I phosphatidylserine
RT decarboxylase in Plasmodium falciparum.";
RL Mol. Microbiol. 51:33-46(2004).
RN [2]
RP FUNCTION.
RX PubMed=26585333; DOI=10.1111/mmi.13280;
RA Choi J.Y., Kumar V., Pachikara N., Garg A., Lawres L., Toh J.,
RA Voelker D.R., Mamoun C.B.;
RT "Characterization of Plasmodium phosphatidylserine decarboxylase expressed
RT in yeast and application for inhibitor screening.";
RL Mol. Microbiol. 99:999-1014(2016).
CC -!- FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn)
CC from phosphatidylserine (PtdSer). Plays a central role in phospholipid
CC metabolism and in the interorganelle trafficking of phosphatidylserine.
CC {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:14651609,
CC ECO:0000269|PubMed:26585333}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-
CC diacyl-sn-glycero-3-phosphoethanolamine + CO2; Xref=Rhea:RHEA:20828,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57262,
CC ChEBI:CHEBI:64612; EC=4.1.1.65; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03208, ECO:0000269|PubMed:14651609};
CC -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03208,
CC ECO:0000305|PubMed:14651609};
CC Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_03208};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=63 uM for dioleoyl phosphatidylserine
CC {ECO:0000269|PubMed:14651609};
CC Vmax=680 nmol/h/mg enzyme {ECO:0000269|PubMed:14651609};
CC pH dependence:
CC Optimum pH is 6.8. {ECO:0000269|PubMed:14651609};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step
CC 2/2. {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000305|PubMed:14651609}.
CC -!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit and a
CC small pyruvoyl-containing alpha subunit. {ECO:0000255|HAMAP-
CC Rule:MF_03208}.
CC -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane
CC {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:14651609}; Single-
CC pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03208}. Note=Equally
CC found in the membrane-bound as well as in the soluble fraction.
CC {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:14651609}.
CC -!- PTM: Is synthesized initially as an inactive proenzyme. Formation of
CC the active enzyme involves a self-maturation process in which the
CC active site pyruvoyl group is generated from an internal serine residue
CC via an autocatalytic post-translational modification. Two non-identical
CC subunits are generated from the proenzyme in this reaction, and the
CC pyruvate is formed at the N-terminus of the alpha chain, which is
CC derived from the carboxyl end of the proenzyme. The autoendoproteolytic
CC cleavage occurs by a canonical serine protease mechanism, in which the
CC side chain hydroxyl group of the serine supplies its oxygen atom to
CC form the C-terminus of the beta chain, while the remainder of the
CC serine residue undergoes an oxidative deamination to produce ammonia
CC and the pyruvoyl prosthetic group on the alpha chain. During this
CC reaction, the Ser that is part of the protease active site of the
CC proenzyme becomes the pyruvoyl prosthetic group, which constitutes an
CC essential element of the active site of the mature decarboxylase.
CC {ECO:0000255|HAMAP-Rule:MF_03208}.
CC -!- SIMILARITY: Belongs to the phosphatidylserine decarboxylase family.
CC PSD-B subfamily. Eukaryotic type I sub-subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_03208}.
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DR EMBL; AF312489; AAG38562.2; -; mRNA.
DR EMBL; AY140651; AAN34609.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9GPP8; -.
DR SMR; Q9GPP8; -.
DR VEuPathDB; PlasmoDB:PF3D7_0927900; -.
DR VEuPathDB; PlasmoDB:Pf7G8-2_000275900; -.
DR VEuPathDB; PlasmoDB:Pf7G8_090032700; -.
DR VEuPathDB; PlasmoDB:PfCD01_090032200; -.
DR VEuPathDB; PlasmoDB:PfDd2_090032900; -.
DR VEuPathDB; PlasmoDB:PfGA01_090032100; -.
DR VEuPathDB; PlasmoDB:PfGB4_090032800; -.
DR VEuPathDB; PlasmoDB:PfGN01_090032700; -.
DR VEuPathDB; PlasmoDB:PfHB3_090032500; -.
DR VEuPathDB; PlasmoDB:PfIT_090032400; -.
DR VEuPathDB; PlasmoDB:PfKE01_090032200; -.
DR VEuPathDB; PlasmoDB:PfKH01_090032100; -.
DR VEuPathDB; PlasmoDB:PfKH02_090032600; -.
DR VEuPathDB; PlasmoDB:PfML01_090032300; -.
DR VEuPathDB; PlasmoDB:PfNF135_090031500; -.
DR VEuPathDB; PlasmoDB:PfNF166_090031900; -.
DR VEuPathDB; PlasmoDB:PfNF54_090033000; -.
DR VEuPathDB; PlasmoDB:PfSD01_090032800; -.
DR VEuPathDB; PlasmoDB:PfSN01_090032400; -.
DR VEuPathDB; PlasmoDB:PfTG01_090032200; -.
DR BRENDA; 4.1.1.65; 4889.
DR UniPathway; UPA00558; UER00616.
DR GO; GO:0030176; C:integral component of endoplasmic reticulum membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005739; C:mitochondrion; IEA:InterPro.
DR GO; GO:0004609; F:phosphatidylserine decarboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016540; P:protein autoprocessing; IEA:UniProtKB-UniRule.
DR HAMAP; MF_03208; PS_decarb_PSD_B_type1_euk; 1.
DR InterPro; IPR003817; PS_Dcarbxylase.
DR InterPro; IPR033177; PSD.
DR InterPro; IPR033661; PSD_type1_euk.
DR PANTHER; PTHR10067; PTHR10067; 1.
DR Pfam; PF02666; PS_Dcarbxylase; 1.
DR TIGRFAMs; TIGR00163; PS_decarb; 1.
PE 1: Evidence at protein level;
KW Decarboxylase; Endoplasmic reticulum; Lipid biosynthesis; Lipid metabolism;
KW Lyase; Membrane; Phospholipid biosynthesis; Phospholipid metabolism;
KW Pyruvate; Transmembrane; Transmembrane helix; Zymogen.
FT CHAIN 1..362
FT /note="Phosphatidylserine decarboxylase proenzyme"
FT /id="PRO_0000435580"
FT CHAIN 1..315
FT /note="Phosphatidylserine decarboxylase beta chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT /id="PRO_0000435581"
FT CHAIN 316..362
FT /note="Phosphatidylserine decarboxylase alpha chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT /id="PRO_0000435582"
FT TRANSMEM 26..44
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT ACT_SITE 147
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT ACT_SITE 206
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT ACT_SITE 316
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT ACT_SITE 316
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid; for decarboxylase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT SITE 315..316
FT /note="Cleavage (non-hydrolytic); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208,
FT ECO:0000269|PubMed:14651609, ECO:0000305|PubMed:26585333"
FT MOD_RES 316
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT MUTAGEN 315
FT /note="G->A: Prevents processing of the proenzyme."
FT /evidence="ECO:0000269|PubMed:14651609"
FT MUTAGEN 316
FT /note="S->A,T: Prevents processing of the proenzyme."
FT /evidence="ECO:0000269|PubMed:14651609"
SQ SEQUENCE 362 AA; 42636 MW; 6F2F911C158F3035 CRC64;
MLSKFYYCKM RKGKSPSSFF SLHKKYLLTG VTILSFIFMF QYKYHEVLTV YEDKTNVQQS
SRLFWTRLLF GRTRSRITGR IFNIEIPHSS RLYVYNFFIK YLNINKEEIK YPIESYKSLG
DFFSRYIRED TRPIGDLNEY SIVSPCDSEI VDFGELTSNY LDNVKGIKFN IKTFLGSDMI
KKYNDDSTSF YYAIFYLSPK KYHHFHAPFN FKYKIRRHIS GEVFPVFQGM FKIINNLFDI
NERVILSGEW KGGHVYYAAI SAYNVGNIKI VNDEDLLTNN LRTQLSYMGG DINTKIYDHY
KDLEIGDEVG EFKVGSSIIV IFENKKNFKW NVKPNQQISV GERIGGVDQP KQPQNKFIKI
RS
