ID   C7MPZ1_SACVD            Unreviewed;       233 AA.
AC   C7MPZ1;
DT   13-OCT-2009, integrated into UniProtKB/TrEMBL.
DT   13-OCT-2009, sequence version 1.
DT   08-OCT-2025, entry version 88.
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=Svir_34500 {ECO:0000313|EMBL:ACU98414.1};
OS   Saccharomonospora viridis (strain ATCC 15386 / DSM 43017 / JCM 3036 / CCUG
OS   5913 / NBRC 12207 / NCIMB 9602 / P101) (Thermoactinomyces viridis).
OC   Bacteria; Bacillati; Actinomycetota; Actinomycetes; Pseudonocardiales;
OC   Pseudonocardiaceae; Saccharomonospora.
OX   NCBI_TaxID=471857 {ECO:0000313|EMBL:ACU98414.1, ECO:0000313|Proteomes:UP000000841};
RN   [1] {ECO:0000313|EMBL:ACU98414.1, ECO:0000313|Proteomes:UP000000841}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15386 / DSM 43017 / JCM 3036 / NBRC 12207 / P101
RC   {ECO:0000313|Proteomes:UP000000841};
RX   PubMed=21304650; DOI=10.4056/sigs.20263;
RA   Pati A., Sikorski J., Nolan M., Lapidus A., Copeland A.,
RA   Glavina Del Rio T., Lucas S., Chen F., Tice H., Pitluck S., Cheng J.F.,
RA   Chertkov O., Brettin T., Han C., Detter J.C., Kuske C., Bruce D.,
RA   Goodwin L., Chain P., D'haeseleer P., Chen A., Palaniappan K., Ivanova N.,
RA   Mavromatis K., Mikhailova N., Rohde M., Tindall B.J., Goker M., Bristow J.,
RA   Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT   "Complete genome sequence of Saccharomonospora viridis type strain
RT   (P101).";
RL   Stand. Genomic Sci. 1:141-149(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; CP001683; ACU98414.1; -; Genomic_DNA.
DR   RefSeq; WP_015787724.1; NC_013159.1.
DR   AlphaFoldDB; C7MPZ1; -.
DR   STRING; 471857.Svir_34500; -.
DR   KEGG; svi:Svir_34500; -.
DR   eggNOG; COG0688; Bacteria.
DR   HOGENOM; CLU_072492_0_0_11; -.
DR   UniPathway; UPA00558; UER00616.
DR   Proteomes; UP000000841; 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; NF003679; PRK05305.1-3; 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:UP000000841};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145, ECO:0000256|HAMAP-Rule:MF_00664}.
FT   CHAIN           1..196
FT                   /note="Phosphatidylserine decarboxylase beta chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00664"
FT                   /id="PRO_5023225127"
FT   CHAIN           197..233
FT                   /note="Phosphatidylserine decarboxylase alpha chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00664"
FT                   /id="PRO_5023225128"
FT   ACT_SITE        197
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00664"
FT   SITE            196..197
FT                   /note="Cleavage (non-hydrolytic); by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00664"
FT   MOD_RES         197
FT                   /note="Pyruvic acid (Ser); by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00664"
SQ   SEQUENCE   233 AA;  24948 MW;  73A6F25E231E200F CRC64;
     MSANSLGHAA RLIRETLPPI HPAGRPFIAG GVAATLLLRK LSPRLGLLAG LGTLATAAFF
     REPRRVPPLR DDLVLSAADG VVSLIEEASP PAELGLPDQP LTRVSVFLSV FDVHVQRMPV
     RGTVEKVAYR PGKFLSADLD KASEDNERNS VLLRTASGQR LVVVQIAGLV ARRIVCQVGE
     GEHVEAGSTY GLIRFGSRVD TYLPPGSRVL VREGQRTIGG ETPLAELEIA KKD
//