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Entry: A0A1G9GW59_9ACTN
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ID   A0A1G9GW59_9ACTN        Unreviewed;       213 AA.
AC   A0A1G9GW59;
DT   22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT   22-NOV-2017, sequence version 1.
DT   24-JAN-2024, entry version 22.
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   ORFNames=SAMN05421869_121162 {ECO:0000313|EMBL:SDL04898.1};
OS   Nonomuraea jiangxiensis.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Streptosporangiaceae; Nonomuraea.
OX   NCBI_TaxID=633440 {ECO:0000313|EMBL:SDL04898.1, ECO:0000313|Proteomes:UP000199202};
RN   [1] {ECO:0000313|EMBL:SDL04898.1, ECO:0000313|Proteomes:UP000199202}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CGMCC 4.6533 {ECO:0000313|EMBL:SDL04898.1,
RC   ECO:0000313|Proteomes:UP000199202};
RA   de Groot N.N.;
RL   Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
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;
CC         Evidence={ECO:0000256|HAMAP-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; FNDJ01000021; SDL04898.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1G9GW59; -.
DR   STRING; 633440.SAMN05421869_121162; -.
DR   UniPathway; UPA00558; UER00616.
DR   Proteomes; UP000199202; Unassembled WGS sequence.
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_00664; PS_decarb_PSD_A; 1.
DR   InterPro; IPR003817; PS_Dcarbxylase.
DR   InterPro; IPR033175; PSD-A.
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|HAMAP-Rule:MF_00664};
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW   Rule:MF_00664}; Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00664};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_00664};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00664};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00664, ECO:0000256|SAM:Phobius};
KW   Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00664};
KW   Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_00664};
KW   Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000256|HAMAP-Rule:MF_00664};
KW   Reference proteome {ECO:0000313|Proteomes:UP000199202};
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..182
FT                   /note="Phosphatidylserine decarboxylase beta chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00664"
FT                   /id="PRO_5023246989"
FT   CHAIN           183..213
FT                   /note="Phosphatidylserine decarboxylase alpha chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00664"
FT                   /id="PRO_5023246990"
FT   TRANSMEM        17..34
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        41..59
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   ACT_SITE        183
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00664"
FT   SITE            182..183
FT                   /note="Cleavage (non-hydrolytic); by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00664"
FT   MOD_RES         183
FT                   /note="Pyruvic acid (Ser); by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00664"
SQ   SEQUENCE   213 AA;  22735 MW;  4E8B151C7EA056D4 CRC64;
     MSDDSAKPSR LRLARGVSPW LIPTAAAAAA TALLTRKDRR WALAAVPLSA LTGGMLWFFR
     DPDRSPGTGR ILSPADGVVQ SIDPWPDGRT RVAIFMSPLN VHVNRAPLAG NVASVQHVPG
     GFLPAFNKDS DQNERVVWHF ETALGDIEMV QIAGAVARRI VPYVNVGAKV AQAERIGLIR
     FGSRVDIYLP GGLSPAVSVG QKTVAGVTRI DRG
//
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