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Database: UniProt
Entry: I9WNQ7_HELPX
LinkDB: I9WNQ7_HELPX
Original site: I9WNQ7_HELPX 
ID   I9WNQ7_HELPX            Unreviewed;       267 AA.
AC   I9WNQ7;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   24-JAN-2024, entry version 60.
DE   RecName: Full=Phosphatidylserine decarboxylase proenzyme {ECO:0000256|HAMAP-Rule:MF_00662};
DE            EC=4.1.1.65 {ECO:0000256|HAMAP-Rule:MF_00662};
DE   Contains:
DE     RecName: Full=Phosphatidylserine decarboxylase alpha chain {ECO:0000256|HAMAP-Rule:MF_00662};
DE   Contains:
DE     RecName: Full=Phosphatidylserine decarboxylase beta chain {ECO:0000256|HAMAP-Rule:MF_00662};
GN   Name=psd {ECO:0000256|HAMAP-Rule:MF_00662,
GN   ECO:0000313|EMBL:EJC05455.1};
GN   ORFNames=HPHPP13_1812 {ECO:0000313|EMBL:EJC05455.1};
OS   Helicobacter pylori Hp P-13.
OC   Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC   Helicobacteraceae; Helicobacter.
OX   NCBI_TaxID=992079 {ECO:0000313|EMBL:EJC05455.1, ECO:0000313|Proteomes:UP000005544};
RN   [1] {ECO:0000313|EMBL:EJC05455.1, ECO:0000313|Proteomes:UP000005544}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Hp P-13 {ECO:0000313|EMBL:EJC05455.1,
RC   ECO:0000313|Proteomes:UP000005544};
RX   PubMed=23661595; DOI=10.1111/2049-632X.12045;
RA   Blanchard T.G., Czinn S.J., Correa P., Nakazawa T., Keelan M.,
RA   Morningstar L., Santana-Cruz I., Maroo A., McCracken C., Shefchek K.,
RA   Daugherty S., Song Y., Fraser C.M., Fricke W.F.;
RT   "Genome sequences of 65 Helicobacter pylori strains isolated from
RT   asymptomatic individuals and patients with gastric cancer, peptic ulcer
RT   disease, or gastritis.";
RL   Pathog. Dis. 68:39-43(2013).
CC   -!- FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn)
CC       from phosphatidylserine (PtdSer). {ECO:0000256|HAMAP-Rule:MF_00662}.
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_00662};
CC   -!- COFACTOR:
CC       Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00662};
CC       Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00662};
CC   -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC       biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step
CC       2/2. {ECO:0000256|HAMAP-Rule:MF_00662}.
CC   -!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit and a
CC       small pyruvoyl-containing alpha subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_00662}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-Rule:MF_00662};
CC       Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_00662}.
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:0000256|HAMAP-Rule:MF_00662}.
CC   -!- SIMILARITY: Belongs to the phosphatidylserine decarboxylase family.
CC       PSD-B subfamily. Prokaryotic type I sub-subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_00662}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:EJC05455.1}.
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DR   EMBL; AKPO01000010; EJC05455.1; -; Genomic_DNA.
DR   AlphaFoldDB; I9WNQ7; -.
DR   PATRIC; fig|992079.3.peg.1771; -.
DR   UniPathway; UPA00558; UER00616.
DR   Proteomes; UP000005544; 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_00662; PS_decarb_PSD_B_type1; 1.
DR   InterPro; IPR003817; PS_Dcarbxylase.
DR   InterPro; IPR033177; PSD-B.
DR   InterPro; IPR033178; PSD_type1_pro.
DR   NCBIfam; TIGR00163; PS_decarb; 1.
DR   PANTHER; PTHR10067; PHOSPHATIDYLSERINE DECARBOXYLASE; 1.
DR   PANTHER; PTHR10067:SF6; PHOSPHATIDYLSERINE DECARBOXYLASE PROENZYME, MITOCHONDRIAL; 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_00662};
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW   Rule:MF_00662}; Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00662};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_00662};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00662};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_00662};
KW   Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00662};
KW   Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_00662};
KW   Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000256|HAMAP-Rule:MF_00662};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145, ECO:0000256|HAMAP-Rule:MF_00662}.
FT   CHAIN           1..235
FT                   /note="Phosphatidylserine decarboxylase beta chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00662"
FT                   /id="PRO_5023517778"
FT   CHAIN           236..267
FT                   /note="Phosphatidylserine decarboxylase alpha chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00662"
FT                   /id="PRO_5023517777"
FT   ACT_SITE        78
FT                   /note="Charge relay system; for autoendoproteolytic
FT                   cleavage activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00662"
FT   ACT_SITE        132
FT                   /note="Charge relay system; for autoendoproteolytic
FT                   cleavage activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00662"
FT   ACT_SITE        236
FT                   /note="Charge relay system; for autoendoproteolytic
FT                   cleavage activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00662"
FT   ACT_SITE        236
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid; for decarboxylase activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00662"
FT   SITE            235..236
FT                   /note="Cleavage (non-hydrolytic); by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00662"
FT   MOD_RES         236
FT                   /note="Pyruvic acid (Ser); by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00662"
SQ   SEQUENCE   267 AA;  30129 MW;  B8837D38F0E70075 CRC64;
     MVALSNALSR VFGSVAGYEF PSFIQKGINA LYVKIFKIDL SEFEPLENYK SLNALFTRSL
     KKERPFDKAP NICIAPCDAL ITECACLDND TALQIKGMPY KAHELVGEIN PLSLSFFYVN
     FYLSPKDYHH YHAPCDLEIL EARYFAGKLL PVNKPSLHKN NNLFVGNERV VLVARDIQGN
     QLYFVAVGAL NVGKMRFNFD KNIQTNAKAR FTQTYSYNPP IKVKKGDNLG NFEMGSTIVL
     FIQNTAFKDL KEKSVKFGES IGEFHAN
//
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