ID W0AE62_9SPHN Unreviewed; 244 AA.
AC W0AE62;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 24-JAN-2024, entry version 48.
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=NX02_14390 {ECO:0000313|EMBL:AHE54563.1};
OS Sphingomonas sanxanigenens DSM 19645 = NX02.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1123269 {ECO:0000313|EMBL:AHE54563.1, ECO:0000313|Proteomes:UP000018851};
RN [1] {ECO:0000313|EMBL:AHE54563.1, ECO:0000313|Proteomes:UP000018851}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NX02 {ECO:0000313|EMBL:AHE54563.1,
RC ECO:0000313|Proteomes:UP000018851};
RA Ma T., Huang H., Wu M., Li X., Li G.;
RT "Completed genome of Sphingomonas sanxanigenens NX02.";
RL Submitted (JUL-2013) 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; CP006644; AHE54563.1; -; Genomic_DNA.
DR RefSeq; WP_025292768.1; NZ_CP006644.1.
DR AlphaFoldDB; W0AE62; -.
DR STRING; 1123269.NX02_14390; -.
DR KEGG; ssan:NX02_14390; -.
DR PATRIC; fig|1123269.5.peg.2805; -.
DR eggNOG; COG0688; Bacteria.
DR HOGENOM; CLU_072492_0_0_5; -.
DR OrthoDB; 9790893at2; -.
DR UniPathway; UPA00558; UER00616.
DR Proteomes; UP000018851; 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_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:UP000018851};
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..202
FT /note="Phosphatidylserine decarboxylase beta chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00664"
FT /id="PRO_5023284102"
FT CHAIN 203..244
FT /note="Phosphatidylserine decarboxylase alpha chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00664"
FT /id="PRO_5023284101"
FT TRANSMEM 28..61
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 203
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00664"
FT SITE 202..203
FT /note="Cleavage (non-hydrolytic); by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00664"
FT MOD_RES 203
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00664"
SQ SEQUENCE 244 AA; 26213 MW; A3454D49DD17A934 CRC64;
MTSLEKPAVG TTTVKWRFPA VHPEGRKFVL IAAVITLAFA LMAWETVAWP MAGVTLWVAA
FFRDPVRTVP QGDNLIVAPA DGLVTLIERV PVPRELAGPD GLGNEPLVRV SIFMSVFDVH
INRSPIAGTV KAVVYIAGKF LNADLDKASE ENERQHLIVE RHDGLRIGFT QIAGLVARRI
LPFVKPGDIL AAGQRFGLIR FGSRVDVYLP AGTAPRITLG QRSIAGETVL AVIGDPVAGS
GVPQ
//
