PSD_PLAKH
ID PSD_PLAKH Reviewed; 354 AA.
AC B3L2V1;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 02-SEP-2008, sequence version 1.
DT 25-MAY-2022, entry version 60.
DE RecName: Full=Phosphatidylserine decarboxylase proenzyme {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000303|PubMed:22057268};
DE EC=4.1.1.65 {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:22057268, ECO:0000269|PubMed:25724650};
DE Contains:
DE RecName: Full=Phosphatidylserine decarboxylase beta chain {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000305|PubMed:25724650};
DE Contains:
DE RecName: Full=Phosphatidylserine decarboxylase alpha chain {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000305|PubMed:25724650};
DE Flags: Precursor;
GN ORFNames=PKH_072580;
OS Plasmodium knowlesi (strain H).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Aconoidasida; Haemosporida;
OC Plasmodiidae; Plasmodium; Plasmodium (Plasmodium).
OX NCBI_TaxID=5851;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H;
RA Pain A., Boehme U., Berry A.E., Mungall K., Finn R., Jackson A.P.,
RA Mourier T., Mistry J., Pasini E.M., Aslett M., Balasubrammaniam S.,
RA Borgwardt K., Brooks K., Carret C., Carver T.J., Cherevach I.,
RA Chillingworth T., Clarke T.G., Galinski M.R., Hall N., Harper D.,
RA Harris D., Hauser H., Ivens A., Janssen C.S., Keane T., Larke N., Lapp S.,
RA Marti M., Moule S., Meyer I.M., Ormond D., Peters N., Sanders M.,
RA Sanders S., Sergeant T.J., Simmonds M., Smith F., Squares R., Thurston S.,
RA Tivey A.R., Walker D., White B., Zuiderwijk E., Churcher C., Quail M.A.,
RA Cowman A.F., Turner C.M.R., Rajandream M.A., Kocken C.H.M., Thomas A.W.,
RA Newbold C.I., Barrell B.G., Berriman M.;
RT "The genome of Plasmodium knowlesi strain H, a zoonotic malaria parasite
RT with host range from monkey to man.";
RL Nature 455:799-803(2008).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=22057268; DOI=10.1074/jbc.m111.313676;
RA Choi J.Y., Augagneur Y., Ben Mamoun C., Voelker D.R.;
RT "Identification of gene encoding Plasmodium knowlesi phosphatidylserine
RT decarboxylase by genetic complementation in yeast and characterization of
RT in vitro maturation of encoded enzyme.";
RL J. Biol. Chem. 287:222-232(2012).
RN [3]
RP ACTIVE SITE, CATALYTIC ACTIVITY, CLEAVAGE SITE, COFACTOR, PYRUVATE
RP FORMATION AT SER-308, ACTIVITY REGULATION, AND MUTAGENESIS OF ASP-139;
RP HIS-195; HIS-198; GLY-307; SER-308 AND SER-309.
RX PubMed=25724650; DOI=10.1074/jbc.m115.642413;
RA Choi J.Y., Duraisingh M.T., Marti M., Ben Mamoun C., Voelker D.R.;
RT "From protease to decarboxylase: the molecular metamorphosis of
RT phosphatidylserine decarboxylase.";
RL J. Biol. Chem. 290:10972-10980(2015).
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:22057268}.
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:22057268,
CC ECO:0000269|PubMed:25724650};
CC -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03208,
CC ECO:0000269|PubMed:25724650};
CC Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_03208, ECO:0000269|PubMed:25724650};
CC -!- ACTIVITY REGULATION: Protease activity is inhibited by PMSF.
CC {ECO:0000269|PubMed:25724650}.
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step
CC 2/2. {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000305|PubMed:22057268}.
CC -!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit and a
CC small pyruvoyl-containing alpha subunit. {ECO:0000250|UniProtKB:P0A8K1,
CC ECO:0000255|HAMAP-Rule:MF_03208}.
CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000269|PubMed:22057268}.
CC Endoplasmic reticulum membrane {ECO:0000250|UniProtKB:Q9GPP8,
CC ECO:0000255|HAMAP-Rule:MF_03208}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03208}. Note=Equally found in the membrane-
CC bound as well as in the soluble fraction. {ECO:0000255|HAMAP-
CC Rule:MF_03208, ECO:0000269|PubMed:22057268}.
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, ECO:0000305|PubMed:25724650}.
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; AM910989; CAQ39327.1; -; Genomic_DNA.
DR RefSeq; XP_002258555.1; XM_002258519.1.
DR AlphaFoldDB; B3L2V1; -.
DR SMR; B3L2V1; -.
DR STRING; 5850.PKH_072580; -.
DR PRIDE; B3L2V1; -.
DR EnsemblProtists; CAQ39327; CAQ39327; PKH_072580.
DR GeneID; 7320008; -.
DR KEGG; pkn:PKNH_0726300; -.
DR VEuPathDB; PlasmoDB:PKNH_0726300; -.
DR HOGENOM; CLU_029061_3_1_1; -.
DR InParanoid; B3L2V1; -.
DR OMA; AIEWQLH; -.
DR PhylomeDB; B3L2V1; -.
DR BRENDA; 4.1.1.65; 4891.
DR UniPathway; UPA00558; UER00616.
DR Proteomes; UP000031513; Chromosome 7.
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; Reference proteome; Transmembrane; Transmembrane helix; Zymogen.
FT CHAIN 1..354
FT /note="Phosphatidylserine decarboxylase proenzyme"
FT /id="PRO_0000435577"
FT CHAIN 1..307
FT /note="Phosphatidylserine decarboxylase beta chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT /id="PRO_0000435578"
FT CHAIN 308..354
FT /note="Phosphatidylserine decarboxylase alpha chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT /id="PRO_0000435579"
FT TRANSMEM 18..36
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT ACT_SITE 139
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208,
FT ECO:0000305|PubMed:25724650"
FT ACT_SITE 198
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208,
FT ECO:0000305|PubMed:25724650"
FT ACT_SITE 308
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208,
FT ECO:0000305|PubMed:25724650"
FT ACT_SITE 308
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid; for decarboxylase activity"
FT /evidence="ECO:0000250|UniProtKB:P0A8K1, ECO:0000255|HAMAP-
FT Rule:MF_03208"
FT SITE 307..308
FT /note="Cleavage (non-hydrolytic); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208,
FT ECO:0000269|PubMed:25724650"
FT MOD_RES 308
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208,
FT ECO:0000269|PubMed:25724650"
FT MUTAGEN 139
FT /note="D->A,N: Prevents processing of the proenzyme."
FT /evidence="ECO:0000269|PubMed:25724650"
FT MUTAGEN 195
FT /note="H->A: Not essential for proenzyme processing, but
FT important for decarboxylase activity of the mature enzyme."
FT /evidence="ECO:0000269|PubMed:25724650"
FT MUTAGEN 198
FT /note="H->A: Prevents processing of the proenzyme."
FT /evidence="ECO:0000269|PubMed:25724650"
FT MUTAGEN 307
FT /note="G->A,P: Prevents processing of the proenzyme."
FT /evidence="ECO:0000269|PubMed:25724650"
FT MUTAGEN 308
FT /note="S->A,T: Prevents processing of the proenzyme."
FT /evidence="ECO:0000269|PubMed:25724650"
FT MUTAGEN 309
FT /note="S->A,T: Not essential for either proenzyme
FT processing or decarboxylase activity."
FT /evidence="ECO:0000269|PubMed:25724650"
SQ SEQUENCE 354 AA; 41524 MW; 11892FC4872BE9D5 CRC64;
MKKNGRDNNF YHLYKNKYLI TGVTILSFIL MFQYKYHEVL TLHDNSENAV QSSKLFWARL
LFGRTRSRIT GQILKMEIPN TYRLFIFNFL IKYMHINKEE IKYPIESYKS IGDFFSRYIR
EETRPIGDVS DYSIVSPCDS ELIDYGELTS EYLENIKGVK FNVNTFLGSK FQKKHNDGST
KFFYAIFYLS PKKYHHFHAP FNFKYKIRRH ISGELFPVFQ GMFKFINNLF NINERVILSG
EWKGGNVYYA AISAYNVGNI KIINDEELVT NNLRHQLSYM GGDINTKIFD SYKSVEVGDE
IGEFRMGSSI VVIFENKKDF SWNVNQNQTV SVGQRLGGIG EPVKEENRFI KIRS
