Detail Information for IndEnz0002000973
IED ID IndEnz0002000973
Enzyme Type ID protease000973
Protein Name Phosphatidylserine decarboxylase proenzyme 1, mitochondrial
EC 4.1.1.65

Cleaved into: Phosphatidylserine decarboxylase 1 beta chain; Phosphatidylserine decarboxylase 1 alpha chain
Gene Name PSD1 PAS_chr1-4_0019
Organism Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris)
Taxonomic Lineage cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Phaffomycetaceae Komagataella Komagataella phaffii Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris)
Enzyme Sequence MPNRSFGVFPSVIYETRLGLSHQMRRPIGQPLSKLSQVSQPNQILQRNYQYKFPRIPRPKRNVLYYTFKRPQLSSATILRTVPSKIRNFSSRAKSKVKSSGRRRKFMSRWLALSSISVVLYGVVNKIKHKGIQRNSSLEPDENHSVKPNSWTLYAYSTLPLKAISRVWGQFNSFELPIWLRSPSYKFYAYVFGVNLDEVAEPDLSKFRNLGEFFYRTIKPETRPIDIDAEMVSPCDGKVLKFGIIENGEIEQVKGMTYSINALLGQQKLAAPVHRINYQLDDDDVVRRHEEFARLNGISYTIDDIIGGRGENIHHSYMNQGDQSLRKSSASQVYEVSNDIAKKSSFDKQLYFAVIYLAPGDYHRFHSPSNWVTTLRRHFVGELFSVAPFFQKTLQNLFILNERVALLGYWKHGFFSMIPVGATNVGSIKINFDKDLVTNSIYESDSYAQTSFPSSDTSSCREEDESTPLIKRSSSRTKKVIKNSCYEATYANASKILRGQPLSKGQEIGGFKLGSTVVLVFEAPKTFHFTLAENMKLKMGQRIGELR
Enzyme Length 547
Uniprot Accession Number C4QX80
Absorption
Active Site ACT_SITE 236; /note=Charge relay system; for autoendoproteolytic cleavage activity; /evidence=ECO:0000255|HAMAP-Rule:MF_03208; ACT_SITE 366; /note=Charge relay system; for autoendoproteolytic cleavage activity; /evidence=ECO:0000255|HAMAP-Rule:MF_03208; ACT_SITE 515; /note=Charge relay system; for autoendoproteolytic cleavage activity; /evidence=ECO:0000255|HAMAP-Rule:MF_03208; ACT_SITE 515; /note=Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity; /evidence=ECO:0000255|HAMAP-Rule:MF_03208
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_03208};
DNA Binding
EC Number 4.1.1.65
Enzyme Function FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in phospholipid metabolism and in the interorganelle trafficking of phosphatidylserine. {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:19656201}.
Temperature Dependency
PH Dependency
Pathway PATHWAY: Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2. {ECO:0000255|HAMAP-Rule:MF_03208}.
nucleotide Binding
Features Active site (4); Chain (3); Modified residue (1); Site (1); Topological domain (2); Transit peptide (1); Transmembrane (1)
Keywords Decarboxylase;Lipid biosynthesis;Lipid metabolism;Lyase;Membrane;Mitochondrion;Mitochondrion inner membrane;Phospholipid biosynthesis;Phospholipid metabolism;Pyruvate;Reference proteome;Transit peptide;Transmembrane;Transmembrane helix;Zymogen
Interact With
Induction
Subcellular Location SUBCELLULAR LOCATION: [Phosphatidylserine decarboxylase 1 beta chain]: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000305|PubMed:19656201}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03208}; Intermembrane side {ECO:0000255|HAMAP-Rule:MF_03208}.; SUBCELLULAR LOCATION: [Phosphatidylserine decarboxylase 1 alpha chain]: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000305|PubMed:19656201}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03208}; Intermembrane side {ECO:0000255|HAMAP-Rule:MF_03208}. Note=Anchored to the mitochondrial inner membrane through its interaction with the integral membrane beta chain. {ECO:0000255|HAMAP-Rule:MF_03208}.
Modified Residue MOD_RES 515; /note=Pyruvic acid (Ser); by autocatalysis; /evidence=ECO:0000255|HAMAP-Rule:MF_03208
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_03208}.
Signal Peptide
Structure 3D
Cross Reference PDB -
Mapped Pubmed ID -
Motif
Gene Encoded By
Mass 62,528
Kinetics
Metal Binding
Rhea ID RHEA:20828
Cross Reference Brenda