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PSD_CHLPN
ID   PSD_CHLPN               Reviewed;         301 AA.
AC   Q9Z767;
DT   03-JUL-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1999, sequence version 1.
DT   25-MAY-2022, entry version 121.
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}; Synonyms=psdD;
GN   OrderedLocusNames=CPn_0839, CP_1030, CpB0868;
OS   Chlamydia pneumoniae (Chlamydophila pneumoniae).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=83558;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CWL029;
RX   PubMed=10192388; DOI=10.1038/7716;
RA   Kalman S., Mitchell W.P., Marathe R., Lammel C.J., Fan J., Hyman R.W.,
RA   Olinger L., Grimwood J., Davis R.W., Stephens R.S.;
RT   "Comparative genomes of Chlamydia pneumoniae and C. trachomatis.";
RL   Nat. Genet. 21:385-389(1999).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AR39;
RX   PubMed=10684935; DOI=10.1093/nar/28.6.1397;
RA   Read T.D., Brunham R.C., Shen C., Gill S.R., Heidelberg J.F., White O.,
RA   Hickey E.K., Peterson J.D., Utterback T.R., Berry K.J., Bass S.,
RA   Linher K.D., Weidman J.F., Khouri H.M., Craven B., Bowman C., Dodson R.J.,
RA   Gwinn M.L., Nelson W.C., DeBoy R.T., Kolonay J.F., McClarty G.,
RA   Salzberg S.L., Eisen J.A., Fraser C.M.;
RT   "Genome sequences of Chlamydia trachomatis MoPn and Chlamydia pneumoniae
RT   AR39.";
RL   Nucleic Acids Res. 28:1397-1406(2000).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=J138;
RX   PubMed=10871362; DOI=10.1093/nar/28.12.2311;
RA   Shirai M., Hirakawa H., Kimoto M., Tabuchi M., Kishi F., Ouchi K.,
RA   Shiba T., Ishii K., Hattori M., Kuhara S., Nakazawa T.;
RT   "Comparison of whole genome sequences of Chlamydia pneumoniae J138 from
RT   Japan and CWL029 from USA.";
RL   Nucleic Acids Res. 28:2311-2314(2000).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=TW-183;
RA   Geng M.M., Schuhmacher A., Muehldorfer I., Bensch K.W., Schaefer K.P.,
RA   Schneider S., Pohl T., Essig A., Marre R., Melchers K.;
RT   "The genome sequence of Chlamydia pneumoniae TW183 and comparison with
RT   other Chlamydia strains based on whole genome sequence analysis.";
RL   Submitted (MAY-2002) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; AE001363; AAD18977.1; -; Genomic_DNA.
DR   EMBL; AE002161; AAF38806.1; -; Genomic_DNA.
DR   EMBL; BA000008; BAA99047.1; -; Genomic_DNA.
DR   EMBL; AE009440; AAP98797.1; -; Genomic_DNA.
DR   PIR; E86595; E86595.
DR   PIR; F72029; F72029.
DR   RefSeq; NP_225034.1; NC_000922.1.
DR   RefSeq; WP_010883476.1; NZ_LN847257.1.
DR   AlphaFoldDB; Q9Z767; -.
DR   SMR; Q9Z767; -.
DR   STRING; 115711.CP_1030; -.
DR   EnsemblBacteria; AAD18977; AAD18977; CPn_0839.
DR   EnsemblBacteria; AAF38806; AAF38806; CP_1030.
DR   GeneID; 45050893; -.
DR   KEGG; cpa:CP_1030; -.
DR   KEGG; cpj:psdD; -.
DR   KEGG; cpn:CPn_0839; -.
DR   KEGG; cpt:CpB0868; -.
DR   PATRIC; fig|115713.3.peg.919; -.
DR   eggNOG; COG0688; Bacteria.
DR   HOGENOM; CLU_029061_2_2_0; -.
DR   OrthoDB; 891720at2; -.
DR   UniPathway; UPA00558; UER00616.
DR   Proteomes; UP000000583; Chromosome.
DR   Proteomes; UP000000801; 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..257
FT                   /note="Phosphatidylserine decarboxylase beta chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00663"
FT                   /id="PRO_0000029731"
FT   CHAIN           258..301
FT                   /note="Phosphatidylserine decarboxylase alpha chain"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00663"
FT                   /id="PRO_0000029732"
FT   ACT_SITE        115
FT                   /note="Charge relay system; for autoendoproteolytic
FT                   cleavage activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00663"
FT   ACT_SITE        171
FT                   /note="Charge relay system; for autoendoproteolytic
FT                   cleavage activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00663"
FT   ACT_SITE        258
FT                   /note="Charge relay system; for autoendoproteolytic
FT                   cleavage activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00663"
FT   ACT_SITE        258
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid; for decarboxylase activity"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00663"
FT   SITE            257..258
FT                   /note="Cleavage (non-hydrolytic); by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00663"
FT   MOD_RES         258
FT                   /note="Pyruvic acid (Ser); by autocatalysis"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00663"
SQ   SEQUENCE   301 AA;  34827 MW;  26047659FE0B57F2 CRC64;
     MQKPQYIDRI TKKKVIEPIF YEKTMLFLYN SKLGKKLSVF LSTHPIFSRI YGWLQRCSWT
     RRQIRPFMNR YKISEKELTK PVADFTSFND FFTRKLKPEA RPIVGGKEVF ITPVDGRYLV
     YPNVSEFDKF IVKSKAFSLP KLLGDHELTK LYAHGSIVFA RLAPFDYHRF HFPCDCLPQK
     TRCVNGALFS VHPLAVKDNF ILFCENKRTV TVLETEQFGN VLYLEVGAMN VGSIVQTFSP
     NQTYAKGDEK GFFAFGGSTV ILLFLPNAIR FDNDLLKNSR MGFETRCLMG QSLGRSQREE
     I
 
 
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