ID   PSD_BRUME               Reviewed;         232 AA.
AC   Q8YFM9;
DT   03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   03-JUL-2003, sequence version 2.
DT   04-NOV-2026, entry version 119.
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};
GN   OrderedLocusNames=BMEI1491;
OS   Brucella melitensis biotype 1 (strain ATCC 23456 / CCUG 17765 / NCTC 10094
OS   / 16M).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Alphaproteobacteria;
OC   Hyphomicrobiales; Brucellaceae; Brucella/Ochrobactrum group; Brucella;
OC   Brucella melitensis group.
OX   NCBI_TaxID=224914;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 23456 / CCUG 17765 / NCTC 10094 / 16M;
RX   PubMed=11756688; DOI=10.1073/pnas.221575398;
RA   DelVecchio V.G., Kapatral V., Redkar R.J., Patra G., Mujer C., Los T.,
RA   Ivanova N., Anderson I., Bhattacharyya A., Lykidis A., Reznik G.,
RA   Jablonski L., Larsen N., D'Souza M., Bernal A., Mazur M., Goltsman E.,
RA   Selkov E., Elzer P.H., Hagius S., O'Callaghan D., Letesson J.-J.,
RA   Haselkorn R., Kyrpides N.C., Overbeek R.;
RT   "The genome sequence of the facultative intracellular pathogen Brucella
RT   melitensis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 99:443-448(2002).
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; Evidence={ECO:0000255|HAMAP-
CC         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   -!- SEQUENCE CAUTION:
CC       Sequence=AAL52672.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE008917; AAL52672.1; ALT_INIT; Genomic_DNA.
DR   PIR; AE3438; AE3438.
DR   AlphaFoldDB; Q8YFM9; -.
DR   KEGG; bme:BMEI1491; -.
DR   KEGG; bmel:DK63_1999; -.
DR   PATRIC; fig|224914.52.peg.2101; -.
DR   eggNOG; COG0688; Bacteria.
DR   OMA; AAGNWYI; -.
DR   PhylomeDB; Q8YFM9; -.
DR   UniPathway; UPA00558; UER00616.
DR   Proteomes; UP000000419; Chromosome I.
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-UniRule.
DR   HAMAP; MF_00664; PS_decarb_PSD_A; 1.
DR   InterPro; IPR003817; PS_Dcarbxylase.
DR   InterPro; IPR033175; PSD-A.
DR   NCBIfam; NF003677; PRK05305.1-1; 1.
DR   NCBIfam; NF003678; PRK05305.1-2; 1.
DR   NCBIfam; NF003679; PRK05305.1-3; 1.
DR   NCBIfam; NF003685; PRK05305.2-5; 1.
DR   PANTHER; PTHR35809; ARCHAETIDYLSERINE DECARBOXYLASE PROENZYME-RELATED; 1.
DR   PANTHER; PTHR35809:SF1; ARCHAETIDYLSERINE DECARBOXYLASE PROENZYME-RELATED; 1.
DR   Pfam; PF02666; PS_Dcarbxylase; 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..189
FT                   /note="Phosphatidylserine decarboxylase beta chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
FT                   /id="PRO_0000029759"
FT   CHAIN           190..232
FT                   /note="Phosphatidylserine decarboxylase alpha chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00664"
FT                   /id="PRO_0000029760"
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;  25826 MW;  DF38984DE63E4526 CRC64;
     MSLTDTIRNT FVPIHREGYP FIAGFFVVSL MLGWLWDPLF WIGMVLTVWC IYFYRDPERV
     TPMDDDLVIS PADGKVSFVG LAVPPAELDL GYEPMTRVSV FMNVFSVHIN RSPVRGKIDK
     VVHRPGKFLN AELDKASTEN ERNSVLIESP HGKIGVVQIA GLVARRIVCW SNQDDELSVG
     ERFGLIRFGS RVDVYLPSDA TVRVAVGQTA IAGETVLADY GTERGEPVVR IA
//