ID   C6VTZ6_DYAFD            Unreviewed;       219 AA.
AC   C6VTZ6;
DT   22-SEP-2009, integrated into UniProtKB/TrEMBL.
DT   22-SEP-2009, sequence version 1.
DT   08-OCT-2025, entry version 86.
DE   RecName: Full=Phosphatidylserine decarboxylase proenzyme {ECO:0000256|HAMAP-Rule:MF_00664};
DE            EC=4.1.1.65 {ECO:0000256|HAMAP-Rule:MF_00664};
DE   Contains:
DE     RecName: Full=Phosphatidylserine decarboxylase alpha chain {ECO:0000256|HAMAP-Rule:MF_00664};
DE   Contains:
DE     RecName: Full=Phosphatidylserine decarboxylase beta chain {ECO:0000256|HAMAP-Rule:MF_00664};
GN   Name=psd {ECO:0000256|HAMAP-Rule:MF_00664};
GN   OrderedLocusNames=Dfer_3556 {ECO:0000313|EMBL:ACT94764.1};
OS   Dyadobacter fermentans (strain ATCC 700827 / DSM 18053 / CIP 107007 /
OS   KCTC 52180 / NS114).
OC   Bacteria; Pseudomonadati; Bacteroidota; Cytophagia; Cytophagales;
OC   Spirosomataceae; Dyadobacter.
OX   NCBI_TaxID=471854 {ECO:0000313|EMBL:ACT94764.1, ECO:0000313|Proteomes:UP000002011};
RN   [1] {ECO:0000313|EMBL:ACT94764.1, ECO:0000313|Proteomes:UP000002011}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 700827 / DSM 18053 / CIP 107007 / KCTC 52180 / NS114
RC   {ECO:0000313|Proteomes:UP000002011};
RX   PubMed=21304649; DOI=10.4056/sigs.19262;
RA   Lang E., Lapidus A., Chertkov O., Brettin T., Detter J.C., Han C.,
RA   Copeland A., Glavina Del Rio T., Nolan M., Chen F., Lucas S., Tice H.,
RA   Cheng J.F., Land M., Hauser L., Chang Y.J., Jeffries C.D., Kopitz M.,
RA   Bruce D., Goodwin L., Pitluck S., Ovchinnikova G., Pati A., Ivanova N.,
RA   Mavrommatis K., Chen A., Palaniappan K., Chain P., Bristow J., Eisen J.A.,
RA   Markowitz V., Hugenholtz P., Goker M., Rohde M., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Dyadobacter fermentans type strain (NS114).";
RL   Stand. Genomic Sci. 1:133-140(2009).
CC   -!- FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn)
CC       from phosphatidylserine (PtdSer). {ECO:0000256|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:0000256|HAMAP-
CC         Rule:MF_00664};
CC   -!- COFACTOR:
CC       Name=pyruvate; Xref=ChEBI:CHEBI:15361; Evidence={ECO:0000256|HAMAP-
CC         Rule:MF_00664};
CC       Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00664};
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC       biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step
CC       2/2. {ECO:0000256|HAMAP-Rule:MF_00664}.
CC   -!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit and a
CC       small pyruvoyl-containing alpha subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00664}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00664};
CC       Peripheral membrane protein {ECO:0000256|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:0000256|HAMAP-Rule:MF_00664}.
CC   -!- SIMILARITY: Belongs to the phosphatidylserine decarboxylase family.
CC       PSD-A subfamily. {ECO:0000256|HAMAP-Rule:MF_00664}.
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DR   EMBL; CP001619; ACT94764.1; -; Genomic_DNA.
DR   RefSeq; WP_015813008.1; NC_013037.1.
DR   AlphaFoldDB; C6VTZ6; -.
DR   STRING; 471854.Dfer_3556; -.
DR   KEGG; dfe:Dfer_3556; -.
DR   eggNOG; COG0688; Bacteria.
DR   HOGENOM; CLU_072492_1_0_10; -.
DR   OrthoDB; 9790893at2; -.
DR   UniPathway; UPA00558; UER00616.
DR   Proteomes; UP000002011; 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-UniRule.
DR   HAMAP; MF_00664; PS_decarb_PSD_A; 1.
DR   InterPro; IPR003817; PS_Dcarbxylase.
DR   InterPro; IPR033175; PSD-A.
DR   NCBIfam; NF003678; PRK05305.1-2; 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 {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW   Rule:MF_00664};
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW   Rule:MF_00664};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW   Rule:MF_00664};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW   Rule:MF_00664};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00664};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_00664};
KW   Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209,
KW   ECO:0000256|HAMAP-Rule:MF_00664};
KW   Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264, ECO:0000256|HAMAP-
KW   Rule:MF_00664};
KW   Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000256|HAMAP-Rule:MF_00664};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002011};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145, ECO:0000256|HAMAP-Rule:MF_00664}.
FT   CHAIN           1..187
FT                   /note="Phosphatidylserine decarboxylase beta chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00664"
FT                   /id="PRO_5023277621"
FT   CHAIN           188..219
FT                   /note="Phosphatidylserine decarboxylase alpha chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00664"
FT                   /id="PRO_5023277622"
FT   TRANSMEM        7..28
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        34..54
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   ACT_SITE        188
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00664"
FT   SITE            187..188
FT                   /note="Cleavage (non-hydrolytic); by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00664"
FT   MOD_RES         188
FT                   /note="Pyruvic acid (Ser); by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00664"
SQ   SEQUENCE   219 AA;  24998 MW;  C98D4CE45514A5AC CRC64;
     MKLHREGYTI MAITAIILII INLGINYLLP DGYWIPRLVL IGSIIVFFLV VQFFRVPTRV
     VHKSDREIVA PCDGKVVVIE EVVETEYFKG PRRQISIFMS PLNVHVNWNP ISGVIQYFKY
     HPGLYLVAWH PKSSTDNERT TVVIRTIEGV EVLFRQIAGA AARRIRWYVK EGDKVEQSTE
     MGFIKFGSRV DIFVPLDAEI KVNLQDKTVG SVTVLAQLK
//