PSD_RHOP5
ID PSD_RHOP5 Reviewed; 232 AA.
AC Q07Q32;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 31-OCT-2006, sequence version 1.
DT 25-MAY-2022, entry version 78.
DE RecName: Full=Phosphatidylserine decarboxylase proenzyme {ECO:0000255|HAMAP-Rule:MF_00664};
DE EC=4.1.1.65 {ECO:0000255|HAMAP-Rule:MF_00664};
DE Contains:
DE RecName: Full=Phosphatidylserine decarboxylase alpha chain {ECO:0000255|HAMAP-Rule:MF_00664};
DE Contains:
DE RecName: Full=Phosphatidylserine decarboxylase beta chain {ECO:0000255|HAMAP-Rule:MF_00664};
GN Name=psd {ECO:0000255|HAMAP-Rule:MF_00664}; OrderedLocusNames=RPE_2008;
OS Rhodopseudomonas palustris (strain BisA53).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Rhodopseudomonas.
OX NCBI_TaxID=316055;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisA53;
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Kim E., Harwood C.S., Oda Y.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisA53.";
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn)
CC from phosphatidylserine (PtdSer). {ECO:0000255|HAMAP-Rule:MF_00664}.
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_00664};
CC -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00664};
CC Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00664};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step
CC 2/2. {ECO:0000255|HAMAP-Rule:MF_00664}.
CC -!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit and a
CC small pyruvoyl-containing alpha subunit. {ECO:0000255|HAMAP-
CC Rule:MF_00664}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00664};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00664}.
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 post-translation
CC cleavage follows an unusual pathway, termed non-hydrolytic serinolysis,
CC in which the side chain hydroxyl group of the serine supplies its
CC oxygen atom to form the C-terminus of the beta chain, while the
CC remainder of the serine residue undergoes an oxidative deamination to
CC produce ammonia and the pyruvoyl prosthetic group on the alpha chain.
CC {ECO:0000255|HAMAP-Rule:MF_00664}.
CC -!- SIMILARITY: Belongs to the phosphatidylserine decarboxylase family.
CC PSD-A subfamily. {ECO:0000255|HAMAP-Rule:MF_00664}.
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DR EMBL; CP000463; ABJ05952.1; -; Genomic_DNA.
DR RefSeq; WP_011663436.1; NC_008435.1.
DR AlphaFoldDB; Q07Q32; -.
DR STRING; 316055.RPE_2008; -.
DR EnsemblBacteria; ABJ05952; ABJ05952; RPE_2008.
DR KEGG; rpe:RPE_2008; -.
DR eggNOG; COG0688; Bacteria.
DR HOGENOM; CLU_072492_0_0_5; -.
DR OMA; VSIFMSP; -.
DR OrthoDB; 891720at2; -.
DR UniPathway; UPA00558; UER00616.
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_00664; PS_decarb_PSD_A; 1.
DR InterPro; IPR003817; PS_Dcarbxylase.
DR InterPro; IPR033175; PSD-A.
DR PANTHER; PTHR35809; PTHR35809; 1.
DR Pfam; PF02666; PS_Dcarbxylase; 1.
DR TIGRFAMs; TIGR00164; PS_decarb_rel; 1.
PE 3: Inferred from homology;
KW Cell membrane; Decarboxylase; Lipid biosynthesis; Lipid metabolism; Lyase;
KW Membrane; Phospholipid biosynthesis; Phospholipid metabolism; Pyruvate;
KW Zymogen.
FT CHAIN 1..189
FT /note="Phosphatidylserine decarboxylase beta chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
FT /id="PRO_1000026678"
FT CHAIN 190..232
FT /note="Phosphatidylserine decarboxylase alpha chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
FT /id="PRO_1000026679"
FT ACT_SITE 190
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
FT SITE 189..190
FT /note="Cleavage (non-hydrolytic); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
FT MOD_RES 190
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
SQ SEQUENCE 232 AA; 25231 MW; D3738FBDD655EDD0 CRC64;
MSIVNSIRAQ IPPVHPEGYP FIGGFALVTL LFFWLWSPLG WIALVLTIWC ALFFRNPVRV
TPVRDDLVVS PADGRISMVT PVVPPAELGL GDKPLLRISI FMSVFNCHVN RAPVGGRIEK
IVYTPGKFIN AELDKASEDN ERNAMVISTP SGQIGVVQIA GLIARRIVSF VRVGQTLATG
ERFGLIRFGS RLDVFLPEGS KALVSVGQTA IAGETVLADF RQGDGGRTYR AD
