PSD_AROAE
ID PSD_AROAE Reviewed; 215 AA.
AC Q5NXP3;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 04-JAN-2005, sequence version 1.
DT 25-MAY-2022, entry version 91.
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=AZOSEA40460;
GN ORFNames=ebA7135;
OS Aromatoleum aromaticum (strain EbN1) (Azoarcus sp. (strain EbN1)).
OC Bacteria; Proteobacteria; Betaproteobacteria; Rhodocyclales;
OC Rhodocyclaceae; Aromatoleum.
OX NCBI_TaxID=76114;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EbN1;
RX PubMed=15551059; DOI=10.1007/s00203-004-0742-9;
RA Rabus R., Kube M., Heider J., Beck A., Heitmann K., Widdel F.,
RA Reinhardt R.;
RT "The genome sequence of an anaerobic aromatic-degrading denitrifying
RT bacterium, strain EbN1.";
RL Arch. Microbiol. 183:27-36(2005).
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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CR555306; CAI10171.1; -; Genomic_DNA.
DR RefSeq; WP_011239816.1; NC_006513.1.
DR AlphaFoldDB; Q5NXP3; -.
DR STRING; 76114.ebA7135; -.
DR PRIDE; Q5NXP3; -.
DR EnsemblBacteria; CAI10171; CAI10171; ebA7135.
DR KEGG; eba:ebA7135; -.
DR eggNOG; COG0688; Bacteria.
DR HOGENOM; CLU_072492_0_0_4; -.
DR OMA; VSIFMSP; -.
DR OrthoDB; 891720at2; -.
DR UniPathway; UPA00558; UER00616.
DR Proteomes; UP000006552; 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 Reference proteome; Zymogen.
FT CHAIN 1..183
FT /note="Phosphatidylserine decarboxylase beta chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
FT /id="PRO_0000262183"
FT CHAIN 184..215
FT /note="Phosphatidylserine decarboxylase alpha chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
FT /id="PRO_0000262184"
FT ACT_SITE 184
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
FT SITE 183..184
FT /note="Cleavage (non-hydrolytic); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
FT MOD_RES 184
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
SQ SEQUENCE 215 AA; 23644 MW; 9ADC7D65420E37C5 CRC64;
MSNNYPHPLL AREGWPFIAI ALAVALVING AAGFGWALPF WLLFIFVVQF FRDPPRPIPQ
GAKDVLSPAD GRIVAIEPVR DPYLDRDSVK ISVFMNVFNV HSNRSPVDGE VVARWYNAGR
FVNAALDKAS VENERNALHL RTRDGHDVTC VQVAGLIARR ILCYVEAGAS LARGQRYGFI
RFGSRVDVYL PAGSRARVTI GDKVSASSTI LAELP
