PSD2_TOXGG
ID PSD2_TOXGG Reviewed; 968 AA.
AC F6N7K6; S7WKF9;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 1.
DT 25-MAY-2022, entry version 29.
DE RecName: Full=Phosphatidylserine decarboxylase 2 proenzyme {ECO:0000303|PubMed:22563079};
DE EC=4.1.1.65;
DE AltName: Full=Phosphatidylserine decarboxylase 1, parasitophorous vacuolar {ECO:0000303|PubMed:24429285};
DE Contains:
DE RecName: Full=Phosphatidylserine decarboxylase 2 beta chain {ECO:0000305|PubMed:22563079};
DE Contains:
DE RecName: Full=Phosphatidylserine decarboxylase 2 alpha chain {ECO:0000305|PubMed:22563079};
DE Flags: Precursor;
GN Name=PSD1pv {ECO:0000303|PubMed:24429285};
GN Synonyms=PSD1 {ECO:0000303|PubMed:22563079}; ORFNames=TGGT1_269920;
OS Toxoplasma gondii (strain ATCC 50853 / GT1).
OC Eukaryota; Sar; Alveolata; Apicomplexa; Conoidasida; Coccidia;
OC Eucoccidiorida; Eimeriorina; Sarcocystidae; Toxoplasma.
OX NCBI_TaxID=507601;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 50853 / GT1;
RX PubMed=22563079; DOI=10.1074/jbc.m112.373639;
RA Gupta N., Hartmann A., Lucius R., Voelker D.R.;
RT "The obligate intracellular parasite Toxoplasma gondii secretes a soluble
RT phosphatidylserine decarboxylase.";
RL J. Biol. Chem. 287:22938-22947(2012).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 50853 / GT1;
RA Sibley D., Venepally P., Karamycheva S., Hadjithomas M., Khan A., Brunk B.,
RA Roos D., Caler E., Lorenzi H.;
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP SUBCELLULAR LOCATION.
RX PubMed=24429285; DOI=10.1074/jbc.m113.509406;
RA Hartmann A., Hellmund M., Lucius R., Voelker D.R., Gupta N.;
RT "Phosphatidylethanolamine synthesis in the parasite mitochondrion is
RT required for efficient growth but dispensable for survival of Toxoplasma
RT gondii.";
RL J. Biol. Chem. 289:6809-6824(2014).
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 Can act on liposomal and host cell PtdSer.
CC {ECO:0000269|PubMed:22563079}.
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;
CC Evidence={ECO:0000269|PubMed:22563079};
CC -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC Evidence={ECO:0000250|UniProtKB:P0A8K1};
CC Note=Binds 1 pyruvoyl group covalently per subunit.
CC {ECO:0000250|UniProtKB:P0A8K1};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=67 uM for phosphatidylserine {ECO:0000269|PubMed:22563079};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step
CC 2/2. {ECO:0000250|UniProtKB:P39006}.
CC -!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit and a
CC small pyruvoyl-containing alpha subunit.
CC {ECO:0000250|UniProtKB:P0A8K1}.
CC -!- SUBCELLULAR LOCATION: Parasitophorous vacuole
CC {ECO:0000269|PubMed:22563079, ECO:0000269|PubMed:24429285}. Cytoplasmic
CC vesicle, secretory vesicle {ECO:0000269|PubMed:22563079}. Note=The
CC protein is stored in dense granules in the parasite and secreted into
CC the parasitophorous vacuole via these granules after host infection.
CC {ECO:0000269|PubMed:22563079}.
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 (By similarity).
CC During this reaction, the Ser that is part of the protease active site
CC of the proenzyme becomes the pyruvoyl prosthetic group, which
CC constitutes an essential element of the active site of the mature
CC decarboxylase. {ECO:0000250|UniProtKB:B3L2V1,
CC ECO:0000250|UniProtKB:P0A8K1, ECO:0000250|UniProtKB:P39006}.
CC -!- SIMILARITY: Belongs to the phosphatidylserine decarboxylase family.
CC {ECO:0000305}.
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DR EMBL; JN003619; AEG64709.1; -; mRNA.
DR EMBL; AAQM03000013; EPR64713.1; -; Genomic_DNA.
DR AlphaFoldDB; F6N7K6; -.
DR EnsemblProtists; EPR64713; EPR64713; TGGT1_269920.
DR VEuPathDB; ToxoDB:TGGT1_269920; -.
DR HOGENOM; CLU_388599_0_0_1; -.
DR SABIO-RK; F6N7K6; -.
DR UniPathway; UPA00558; UER00616.
DR Proteomes; UP000005641; Unassembled WGS sequence.
DR GO; GO:0020003; C:symbiont-containing vacuole; IEA:UniProtKB-SubCell.
DR GO; GO:0030133; C:transport vesicle; IEA:UniProtKB-SubCell.
DR GO; GO:0004609; F:phosphatidylserine decarboxylase activity; IEA:UniProtKB-EC.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR InterPro; IPR003817; PS_Dcarbxylase.
DR InterPro; IPR033177; PSD.
DR PANTHER; PTHR10067; PTHR10067; 1.
DR Pfam; PF02666; PS_Dcarbxylase; 1.
DR TIGRFAMs; TIGR00163; PS_decarb; 1.
PE 1: Evidence at protein level;
KW Cytoplasmic vesicle; Decarboxylase; Lipid biosynthesis; Lipid metabolism;
KW Lyase; Phospholipid biosynthesis; Phospholipid metabolism; Pyruvate;
KW Signal; Zymogen.
FT SIGNAL 1..25
FT /evidence="ECO:0000255"
FT CHAIN 26..968
FT /note="Phosphatidylserine decarboxylase 2 proenzyme"
FT /id="PRO_5005677250"
FT CHAIN 26..682
FT /note="Phosphatidylserine decarboxylase 2 beta chain"
FT /id="PRO_0000435586"
FT CHAIN 683..968
FT /note="Phosphatidylserine decarboxylase 2 alpha chain"
FT /id="PRO_0000435587"
FT ACT_SITE 500
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000250|UniProtKB:B3L2V1"
FT ACT_SITE 570
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000250|UniProtKB:B3L2V1"
FT ACT_SITE 683
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000250|UniProtKB:B3L2V1"
FT ACT_SITE 683
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid; for decarboxylase activity"
FT /evidence="ECO:0000250|UniProtKB:P0A8K1"
FT SITE 682..683
FT /note="Cleavage (non-hydrolytic); by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P0A8K1"
FT MOD_RES 683
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000250|UniProtKB:P0A8K1"
SQ SEQUENCE 968 AA; 108073 MW; C3E01B039072696D CRC64;
MAKVMRLIIF VCVALVAISV PAASSVQSQQ ERIRPGFRQQ LPSSIRPFSA FRRRGQEASD
SVVYLNIVYL RLVGTRQCAT GELTVVVHGK ALNNATLGDV QTSLTRTFAS SLKEPSSTLA
IRRWSWKDPL FLMLTLNRRA VRTGTGLPRS TPLYQVAKQR LFVFVRKPTP TSSCRRAALD
PRPLYGVPKV GVQDKYTLHV SMDVLGMSLR EPLEHQEEEP GPASVSTYAA AQAILDGASS
FGIGAFGSAK PNLKQISMYA SGAELEKQVY TPTTSQLALF LPSKTFFGVE VTSVSDGTFR
IPVSASRLVP FSAMSYMCTG SQTHKLTQTG MNVLEKRVHG KENPPSEGAE VLLNLLAARK
PVNGVFEQDP TVVLLQLWRT PEGSESWQET PLMWEFPDTL EAIEDAGEYR SGILSSIAAN
TRIIGKMAGW LASRSFSRRF IRTLIRLNNI DLEEAFSMSD KDRRHSAADF RSVQEFFTRP
INYHVYRDMD PRASIMAPAD SLIQNIYTIR PDFKGEISHP IIPQVKSTSF NLREFLYGAR
QVPPLQLQSP SNRLFVSILY LAPSDYHRVH SPADWRVTSQ TYIPGCTPSV SRRNLEAGDL
LHRYERTALI GHWDPEKNGQ QLFFSVTMVA AMFVGGLRLS WEEEPLGASM RLGRCTRYTE
SYEKQVDVEL CASQEIGAFR FGSTVVMIFE APEDFDMTSV GQCSHVAAGQ PAGYLGQGRE
RPLQERCNAF RGNFESPFHF WKHLQKTSSV DDILKQNTLA PRAWRQEPGR VWAEVLRATE
RGLLYGFALS HYLLKRWATE NGNLGELVLG QPEVLRQNIN GSDSVIREGF RCFAAKDKKQ
IRLQMSGRQS QVSLTATVTP DEQFLFQHPF YGCVGDEKLG KLVRGIDATW ILLPERAVLL
TLKVSTGSKQ EDGRVLRVAT TKIEVQTEPC QGGWEESRVG TTSTTCAIRT VEKREESISE
GVLTNGDL
