D3ZAW2
uniprot
D3ZAW2
canonical
activity_regulation
ACTIVITY REGULATION: Inhibited by hydroxylamine. {ECO:0000269|PubMed:2618245}.
uniprot
proteins
amino_acid_sequence
MAVAGGRGCVRSLREGVLWRSSPCHCDYTATRHFLGALQKLPLQAWVRKVHTAPLRTLFLLRPVPILLAAGGGYAGYRQYEKYRERQLEKLGLEIPPKLASHWEVSLYKSVPTRLLSRACGRLNQVELPSWLRRPVYSLYIWTFGVNMTEAAVEDLQHYRNLSEFFRRKLKPQARPVCGLHSVISPSDGKILTFGQVKNSEVEQVKGVTYSLESFLGPRACTEDLPFPPASSCDSFRNQLVTREGNELYHCVIYLAPGDYHCFHSPTDWTVSHRRHFPGSLMSVNPGMARWIKELFCHNERVVLTGDWKHGFFSLTAVGATNVGSIRIHFDQDLHTNSPSYSKGSYNDLSFVTHANKEGIPMRKGEPLGEFNLGSTIVLIFEAPKDFNFRLKAGQKILFGEALGSL
uniprot
proteins
ec_number
4.1.1.65
uniprot
proteins
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. May be involved in lipid droplet biogenesis at the endoplasmic reticulum membrane (By similarity). {ECO:0000250|UniProtKB:A0A8H4BVL9, ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:2618245}.
uniprot
proteins
mass_dalton
45824
uniprot
proteins
pathway_participation
PATHWAY: Phospholipid metabolism; phosphatidylethanolamine biosynthesis. {ECO:0000305|PubMed:2618245}.
uniprot
proteins
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}.
uniprot
proteins
protein_family
Eukaryotic type I sub-subfamily
uniprot
proteins
protein_family
PSD-B subfamily
uniprot
proteins
protein_family
Phosphatidylserine decarboxylase family
uniprot
proteins
pubmed
15057822
uniprot
proteins
pubmed
2618245
uniprot
proteins
pubmed
6862014
uniprot
proteins
sequence_length
406
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: [Phosphatidylserine decarboxylase beta chain]: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:6862014}; Single-pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03208}; Intermembrane side {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:6862014}.; SUBCELLULAR LOCATION: [Phosphatidylserine decarboxylase alpha chain]: Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:6862014}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:6862014}; Intermembrane side {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:6862014}. Cytoplasm {ECO:0000250|UniProtKB:Q9UG56}. Note=Anchored to the mitochondrial inner membrane through its interaction with the integral membrane beta chain. {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000305|PubMed:6862014}.; SUBCELLULAR LOCATION: Mitochondrion inner membrane {ECO:0000250|UniProtKB:Q9UG56}. Lipid droplet {ECO:0000250|UniProtKB:Q9UG56}. Note=Predominantly localizes to lipid droplets in lipid-replete conditions, and to mitochondria in lipid-deplete conditions. {ECO:0000250|UniProtKB:Q9UG56}.
uniprot
proteins
transmembrane_region
TRANSMEM 61..79; /note="Helical"; /evidence="ECO:0000255|HAMAP-Rule:MF_03208
uniprot
proteins