PSD_SOLM1
ID PSD_SOLM1 Reviewed; 214 AA.
AC C4XPA6;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 28-JUL-2009, sequence version 1.
DT 03-AUG-2022, entry version 66.
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=DMR_15960;
OS Solidesulfovibrio magneticus (strain ATCC 700980 / DSM 13731 / RS-1)
OS (Desulfovibrio magneticus).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Solidesulfovibrio.
OX NCBI_TaxID=573370;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700980 / DSM 13731 / RS-1;
RX PubMed=19675025; DOI=10.1101/gr.088906.108;
RA Nakazawa H., Arakaki A., Narita-Yamada S., Yashiro I., Jinno K., Aoki N.,
RA Tsuruyama A., Okamura Y., Tanikawa S., Fujita N., Takeyama H.,
RA Matsunaga T.;
RT "Whole genome sequence of Desulfovibrio magneticus strain RS-1 revealed
RT common gene clusters in magnetotactic bacteria.";
RL Genome Res. 19:1801-1808(2009).
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; AP010904; BAH75087.1; -; Genomic_DNA.
DR RefSeq; WP_015860292.1; NC_012796.1.
DR AlphaFoldDB; C4XPA6; -.
DR SMR; C4XPA6; -.
DR STRING; 573370.DMR_15960; -.
DR EnsemblBacteria; BAH75087; BAH75087; DMR_15960.
DR KEGG; dma:DMR_15960; -.
DR eggNOG; COG0688; Bacteria.
DR HOGENOM; CLU_072492_0_0_7; -.
DR OMA; VSIFMSP; -.
DR UniPathway; UPA00558; UER00616.
DR Proteomes; UP000009071; 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_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..181
FT /note="Phosphatidylserine decarboxylase beta chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
FT /id="PRO_1000212493"
FT CHAIN 182..214
FT /note="Phosphatidylserine decarboxylase alpha chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
FT /id="PRO_1000212494"
FT ACT_SITE 182
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
FT SITE 181..182
FT /note="Cleavage (non-hydrolytic); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
FT MOD_RES 182
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
SQ SEQUENCE 214 AA; 23096 MW; 15AFAECD708D1851 CRC64;
MYKPICGLAR DGLPIIGVFA LATLVFALLR WPCLATISLL STIFSFNFFR DPDRTSPTEN
GIAVSPADGV VCKLGEAADP ITGEMRQVVC VFMNVFNVHV NRSPVTGVVS EVRYIPGKFF
NASLDKASTD NERNVIVVTD AEGARFTVVQ IAGLIARRIV CPAKAGDTLS RGERYGMIKF
GSRLDVYLPH GYHPAVAMGQ KTMAGVTVLA KKAD
