Detail Information for IndEnz0002001714
IED ID IndEnz0002001714
Enzyme Type ID protease001714
Protein Name Phosphatidylserine decarboxylase proenzyme
EC 4.1.1.65

Cleaved into: Phosphatidylserine decarboxylase alpha chain; Phosphatidylserine decarboxylase beta chain
Gene Name psd HPSH_07025
Organism Helicobacter pylori (strain Shi470)
Taxonomic Lineage cellular organisms Bacteria Proteobacteria delta/epsilon subdivisions Epsilonproteobacteria Campylobacterales Helicobacteraceae Helicobacter Helicobacter pylori (Campylobacter pylori) Helicobacter pylori (strain Shi470)
Enzyme Sequence MIALSNALSRVFGSVAGYEFPSFIQKGINALYVKIFKIDLSEFEPLENYKSLNALFTRSLKKERPFDKTPNACIAPCDALITECAFLDNDSALQIKGMPYKAHELVGEINPLSPSFFYVNFYLSPKDYHHYHAPCDLEILEARCFAGKLLPVNKPSLHKNKNLFVGNERVALVAKDIQGNRLYFVAVGALNVGKMRFNFDKNIQTNAKAHLTQAYSYNPPIKVKKGDNLGNFEMGSTIVLFVQNTAFKDLKEKSVKFGESIGEFHAN
Enzyme Length 267
Uniprot Accession Number B2UVC1
Absorption
Active Site ACT_SITE 78; /note=Charge relay system; for autoendoproteolytic cleavage activity; /evidence=ECO:0000255|HAMAP-Rule:MF_00662; ACT_SITE 132; /note=Charge relay system; for autoendoproteolytic cleavage activity; /evidence=ECO:0000255|HAMAP-Rule:MF_00662; ACT_SITE 236; /note=Charge relay system; for autoendoproteolytic cleavage activity; /evidence=ECO:0000255|HAMAP-Rule:MF_00662; ACT_SITE 236; /note=Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity; /evidence=ECO:0000255|HAMAP-Rule:MF_00662
Activity Regulation
Binding Site
Calcium Binding
catalytic Activity CATALYTIC ACTIVITY: Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2; Xref=Rhea:RHEA:20828, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57262, ChEBI:CHEBI:64612; EC=4.1.1.65; Evidence={ECO:0000255|HAMAP-Rule:MF_00662};
DNA Binding
EC Number 4.1.1.65
Enzyme Function FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). {ECO:0000255|HAMAP-Rule:MF_00662}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2. {ECO:0000255|HAMAP-Rule:MF_00662}.
nucleotide Binding
Features Active site (4); Chain (2); Modified residue (1); Site (1)
Keywords Cell membrane;Decarboxylase;Lipid biosynthesis;Lipid metabolism;Lyase;Membrane;Phospholipid biosynthesis;Phospholipid metabolism;Pyruvate;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00662}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00662}.
Modified Residue MOD_RES 236; /note=Pyruvic acid (Ser); by autocatalysis; /evidence=ECO:0000255|HAMAP-Rule:MF_00662
Post Translational Modification PTM: Is synthesized initially as an inactive proenzyme. Formation of the active enzyme involves a self-maturation process in which the active site pyruvoyl group is generated from an internal serine residue via an autocatalytic post-translational modification. Two non-identical subunits are generated from the proenzyme in this reaction, and the pyruvate is formed at the N-terminus of the alpha chain, which is derived from the carboxyl end of the proenzyme. The autoendoproteolytic cleavage occurs by a canonical serine protease mechanism, in which the side chain hydroxyl group of the serine supplies its oxygen atom to form the C-terminus of the beta chain, while the remainder of the serine residue undergoes an oxidative deamination to produce ammonia and the pyruvoyl prosthetic group on the alpha chain. During this reaction, the Ser that is part of the protease active site of the proenzyme becomes the pyruvoyl prosthetic group, which constitutes an essential element of the active site of the mature decarboxylase. {ECO:0000255|HAMAP-Rule:MF_00662}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 29,974
Kinetics
Metal Binding
Rhea ID RHEA:20828
Cross Reference Brenda