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PSD_PARD8
ID   PSD_PARD8               Reviewed;         220 AA.
AC   A6LF25;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   24-JUL-2007, sequence version 1.
DT   03-AUG-2022, entry version 73.
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=BDI_2570;
OS   Parabacteroides distasonis (strain ATCC 8503 / DSM 20701 / CIP 104284 / JCM
OS   5825 / NCTC 11152).
OC   Bacteria; Bacteroidetes; Bacteroidia; Bacteroidales; Tannerellaceae;
OC   Parabacteroides.
OX   NCBI_TaxID=435591;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 8503 / DSM 20701 / CIP 104284 / JCM 5825 / NCTC 11152;
RX   PubMed=17579514; DOI=10.1371/journal.pbio.0050156;
RA   Xu J., Mahowald M.A., Ley R.E., Lozupone C.A., Hamady M., Martens E.C.,
RA   Henrissat B., Coutinho P.M., Minx P., Latreille P., Cordum H.,
RA   Van Brunt A., Kim K., Fulton R.S., Fulton L.A., Clifton S.W., Wilson R.K.,
RA   Knight R.D., Gordon J.I.;
RT   "Evolution of symbiotic bacteria in the distal human intestine.";
RL   PLoS Biol. 5:1574-1586(2007).
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; CP000140; ABR44289.1; -; Genomic_DNA.
DR   RefSeq; WP_005861238.1; NZ_LR215978.1.
DR   AlphaFoldDB; A6LF25; -.
DR   SMR; A6LF25; -.
DR   STRING; 435591.BDI_2570; -.
DR   EnsemblBacteria; ABR44289; ABR44289; BDI_2570.
DR   GeneID; 57235554; -.
DR   KEGG; pdi:BDI_2570; -.
DR   eggNOG; COG0688; Bacteria.
DR   HOGENOM; CLU_072492_1_0_10; -.
DR   OMA; VSIFMSP; -.
DR   OrthoDB; 891720at2; -.
DR   BioCyc; PDIS435591:G1G5A-2640-MON; -.
DR   UniPathway; UPA00558; UER00616.
DR   Proteomes; UP000000566; 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..187
FT                   /note="Phosphatidylserine decarboxylase beta chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
FT                   /id="PRO_1000026672"
FT   CHAIN           188..220
FT                   /note="Phosphatidylserine decarboxylase alpha chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
FT                   /id="PRO_1000026673"
FT   ACT_SITE        188
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
FT   SITE            187..188
FT                   /note="Cleavage (non-hydrolytic); by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
FT   MOD_RES         188
FT                   /note="Pyruvic acid (Ser); by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
SQ   SEQUENCE   220 AA;  24641 MW;  6670F01BF8BB0FC3 CRC64;
     MKVHKEGTGL LLTLFTILFI VNITLYHTVG KGMLFYSVAF VSTVLFLLVL NFFRSPFRRF
     PYDSEGLVIA PADGTIVAIE EVMENEILHK KCLQISIFMS IFNVHANWFP VNGTVKHVSH
     QNGRFMAAYL PKSSTENERS AVVITTRNGV DVLARQIAGA MARRIVTYAK PGEKCHVDEQ
     MGFIKFGSRV DVYLPVGTEV LIEMDQKVTG NQTPIARLSK
 
 
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