ID   PSD_CHLTA               Reviewed;         301 AA.
AC   Q3KKZ5;
DT   15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT   08-NOV-2005, sequence version 1.
DT   25-MAY-2022, entry version 81.
DE   RecName: Full=Phosphatidylserine decarboxylase proenzyme {ECO:0000255|HAMAP-Rule:MF_00663};
DE            EC=4.1.1.65 {ECO:0000255|HAMAP-Rule:MF_00663};
DE   Contains:
DE     RecName: Full=Phosphatidylserine decarboxylase alpha chain {ECO:0000255|HAMAP-Rule:MF_00663};
DE   Contains:
DE     RecName: Full=Phosphatidylserine decarboxylase beta chain {ECO:0000255|HAMAP-Rule:MF_00663};
GN   Name=psd {ECO:0000255|HAMAP-Rule:MF_00663}; OrderedLocusNames=CTA_0760;
OS   Chlamydia trachomatis serovar A (strain ATCC VR-571B / DSM 19440 / HAR-13).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=315277;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC VR-571B / DSM 19440 / HAR-13;
RX   PubMed=16177312; DOI=10.1128/iai.73.10.6407-6418.2005;
RA   Carlson J.H., Porcella S.F., McClarty G., Caldwell H.D.;
RT   "Comparative genomic analysis of Chlamydia trachomatis oculotropic and
RT   genitotropic strains.";
RL   Infect. Immun. 73:6407-6418(2005).
CC   -!- FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn)
CC       from phosphatidylserine (PtdSer). {ECO:0000255|HAMAP-Rule:MF_00663}.
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_00663};
CC   -!- COFACTOR:
CC       Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00663};
CC       Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00663};
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC       biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step
CC       2/2. {ECO:0000255|HAMAP-Rule:MF_00663}.
CC   -!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit and a
CC       small pyruvoyl-containing alpha subunit. {ECO:0000255|HAMAP-
CC       Rule:MF_00663}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00663};
CC       Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00663}.
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 autoendoproteolytic
CC       cleavage occurs by a canonical serine protease mechanism, in which the
CC       side chain hydroxyl group of the serine supplies its oxygen atom to
CC       form the C-terminus of the beta chain, while the remainder of the
CC       serine residue undergoes an oxidative deamination to produce ammonia
CC       and the pyruvoyl prosthetic group on the alpha chain. During this
CC       reaction, the Ser that is part of the protease active site of the
CC       proenzyme becomes the pyruvoyl prosthetic group, which constitutes an
CC       essential element of the active site of the mature decarboxylase.
CC       {ECO:0000255|HAMAP-Rule:MF_00663}.
CC   -!- SIMILARITY: Belongs to the phosphatidylserine decarboxylase family.
CC       PSD-B subfamily. Prokaryotic type II sub-subfamily. {ECO:0000255|HAMAP-
CC       Rule:MF_00663}.
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; CP000051; AAX50977.1; -; Genomic_DNA.
DR   RefSeq; WP_009873305.1; NC_007429.1.
DR   AlphaFoldDB; Q3KKZ5; -.
DR   SMR; Q3KKZ5; -.
DR   EnsemblBacteria; AAX50977; AAX50977; CTA_0760.
DR   KEGG; cta:CTA_0760; -.
DR   HOGENOM; CLU_029061_2_2_0; -.
DR   OMA; KDYHHYH; -.
DR   UniPathway; UPA00558; UER00616.
DR   Proteomes; UP000002532; 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_00663; PS_decarb_PSD_B_type2; 1.
DR   InterPro; IPR003817; PS_Dcarbxylase.
DR   InterPro; IPR033177; PSD.
DR   InterPro; IPR033179; PSD_type2_pro.
DR   PANTHER; PTHR10067; PTHR10067; 1.
DR   Pfam; PF02666; PS_Dcarbxylase; 1.
DR   TIGRFAMs; TIGR00163; PS_decarb; 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..259
FT                   /note="Phosphatidylserine decarboxylase beta chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00663"
FT                   /id="PRO_1000026606"
FT   CHAIN           260..301
FT                   /note="Phosphatidylserine decarboxylase alpha chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00663"
FT                   /id="PRO_1000026607"
FT   ACT_SITE        117
FT                   /note="Charge relay system; for autoendoproteolytic
FT                   cleavage activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00663"
FT   ACT_SITE        173
FT                   /note="Charge relay system; for autoendoproteolytic
FT                   cleavage activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00663"
FT   ACT_SITE        260
FT                   /note="Charge relay system; for autoendoproteolytic
FT                   cleavage activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00663"
FT   ACT_SITE        260
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid; for decarboxylase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00663"
FT   SITE            259..260
FT                   /note="Cleavage (non-hydrolytic); by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00663"
FT   MOD_RES         260
FT                   /note="Pyruvic acid (Ser); by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00663"
SQ   SEQUENCE   301 AA;  34076 MW;  D82A7E0272CCC896 CRC64;
     MAAREMLYVN RETGKVEQER IICSSLVKFF IETRIGRALY SVLCKNSLFS RIVGWCQRLR
     VTRYFIKPFV TKYRICIEES ASPLHDYASF NDFFVRKLKP DARPICQGED ICVTPADGAY
     LVFPSMADLS LFTIKNKPFS LESFLGDPQL AHQYAQGSMA IARLAPFDYH RFHFPIAGIA
     EAPRRINGHL FSIHPLMLKR NFEVFTENKR EITIITSKEF GEVAYVEVGA LNVGSIHQTF
     SPGSYVKKGA EKGFFAFGGS TVVLLFQPQR IIFDADLVGY SAQGLETRCR MGQSLGKRFS
     S