PSD_CLOPE
ID PSD_CLOPE Reviewed; 294 AA.
AC Q8XPD5;
DT 03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 25-MAY-2022, entry version 98.
DE RecName: Full=Phosphatidylserine decarboxylase proenzyme {ECO:0000255|HAMAP-Rule:MF_00663};
DE EC=4.1.1.65 {ECO:0000255|HAMAP-Rule:MF_00663};
DE Contains:
DE RecName: Full=Phosphatidylserine decarboxylase alpha chain {ECO:0000255|HAMAP-Rule:MF_00663};
DE Contains:
DE RecName: Full=Phosphatidylserine decarboxylase beta chain {ECO:0000255|HAMAP-Rule:MF_00663};
GN Name=psd {ECO:0000255|HAMAP-Rule:MF_00663}; Synonyms=psdD;
GN OrderedLocusNames=CPE0028;
OS Clostridium perfringens (strain 13 / Type A).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=195102;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=13 / Type A;
RX PubMed=11792842; DOI=10.1073/pnas.022493799;
RA Shimizu T., Ohtani K., Hirakawa H., Ohshima K., Yamashita A., Shiba T.,
RA Ogasawara N., Hattori M., Kuhara S., Hayashi H.;
RT "Complete genome sequence of Clostridium perfringens, an anaerobic flesh-
RT eater.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:996-1001(2002).
CC -!- FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn)
CC from phosphatidylserine (PtdSer). {ECO:0000255|HAMAP-Rule:MF_00663}.
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_00663};
CC -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00663};
CC Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00663};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step
CC 2/2. {ECO:0000255|HAMAP-Rule:MF_00663}.
CC -!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit and a
CC small pyruvoyl-containing alpha subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00663}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00663};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00663}.
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_00663}.
CC -!- SIMILARITY: Belongs to the phosphatidylserine decarboxylase family.
CC PSD-B subfamily. Prokaryotic type II sub-subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_00663}.
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DR EMBL; BA000016; BAB79734.1; -; Genomic_DNA.
DR RefSeq; WP_003458234.1; NC_003366.1.
DR AlphaFoldDB; Q8XPD5; -.
DR SMR; Q8XPD5; -.
DR STRING; 195102.gene:10489257; -.
DR EnsemblBacteria; BAB79734; BAB79734; BAB79734.
DR KEGG; cpe:CPE0028; -.
DR HOGENOM; CLU_029061_2_2_9; -.
DR OMA; KDYHHYH; -.
DR UniPathway; UPA00558; UER00616.
DR Proteomes; UP000000818; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004609; F:phosphatidylserine decarboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IEA:UniProtKB-UniPathway.
DR HAMAP; MF_00663; PS_decarb_PSD_B_type2; 1.
DR InterPro; IPR003817; PS_Dcarbxylase.
DR InterPro; IPR033177; PSD.
DR InterPro; IPR033179; PSD_type2_pro.
DR PANTHER; PTHR10067; PTHR10067; 1.
DR Pfam; PF02666; PS_Dcarbxylase; 1.
DR TIGRFAMs; TIGR00163; PS_decarb; 1.
PE 3: Inferred from homology;
KW Cell membrane; Decarboxylase; Lipid biosynthesis; Lipid metabolism; Lyase;
KW Membrane; Phospholipid biosynthesis; Phospholipid metabolism; Pyruvate;
KW Reference proteome; Zymogen.
FT CHAIN 1..255
FT /note="Phosphatidylserine decarboxylase beta chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00663"
FT /id="PRO_0000029741"
FT CHAIN 256..294
FT /note="Phosphatidylserine decarboxylase alpha chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00663"
FT /id="PRO_0000029742"
FT ACT_SITE 113
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00663"
FT ACT_SITE 169
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00663"
FT ACT_SITE 256
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00663"
FT ACT_SITE 256
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid; for decarboxylase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00663"
FT SITE 255..256
FT /note="Cleavage (non-hydrolytic); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00663"
FT MOD_RES 256
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00663"
SQ SEQUENCE 294 AA; 33620 MW; E43346A2C43D1721 CRC64;
MIKIYNRKTK AYDVEQVAGL KYINWSYASP IGKSFLELFI KKKMFSKLYG NFCDSSLSKK
KIKAFIDEFN IDMSLCNKNI DEFENFNDFF ARTLTPEARP IDYSENILIS PGDGRLSAFE
NIDLDKVVQI KGYTYSLKEL IDDPKVAEEF EGGTCLILRL CPTDYHRFHF VDSGTCSESK
KISGFYYSVN PIALNNVSEL FCKNKREWSI FNSDNFGEIL HVEVGATCVG TILQTYSPEK
RVKKGEEKGY FKFGGSTTIL FFKKDTIKID SDIVEQTKLG FETKVNMGET IGHK
