| IED ID | IndEnz0002004436 |
| Enzyme Type ID | protease004436 |
| Protein Name |
Putative archaetidylserine decarboxylase proenzyme EC 4.1.1.- Cleaved into: Archaetidylserine decarboxylase alpha chain; Archaetidylserine decarboxylase beta chain |
| Gene Name | asd AF_2045 |
| Organism | Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16) |
| Taxonomic Lineage | cellular organisms Archaea Euryarchaeota Archaeoglobi Archaeoglobales Archaeoglobaceae Archaeoglobus Archaeoglobus fulgidus Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16) |
| Enzyme Sequence | MIERSGYGIIAASLLLSAVAYLLHPLISALFVGFALFTAYFFRDPERKIGEGVVSPADGRIDYLEGRRLEIFMSPFDCHINRAPWGGKVLSVKFIEGSTPPAFIRKSGVRTNEILIETEHGVFRVLQMAGIFARRIVSYVSEGDVVKKGQKIGMIRFGSRVVLEVPEGFRFVRGVGEKVKAGETVALRDESFQGS |
| Enzyme Length | 195 |
| Uniprot Accession Number | O28234 |
| Absorption | |
| Active Site | ACT_SITE 159; /note=Schiff-base intermediate with substrate; via pyruvic acid; /evidence=ECO:0000255|HAMAP-Rule:MF_00664 |
| Activity Regulation | |
| Binding Site | |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=archaetidylserine + H(+) = archaetidylethanolamine + CO2; Xref=Rhea:RHEA:51488, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:71517, ChEBI:CHEBI:134176; Evidence={ECO:0000255|HAMAP-Rule:MF_00664, ECO:0000305|PubMed:16243780}; |
| DNA Binding | |
| EC Number | 4.1.1.- |
| Enzyme Function | FUNCTION: Catalyzes the formation of archaetidylethanolamine (PtdEtn) from archaetidylserine (PtdSer). {ECO:0000255|HAMAP-Rule:MF_00664, ECO:0000305|PubMed:16243780}. |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (1); Chain (2); Modified residue (1); Site (1) |
| Keywords | Cell membrane;Decarboxylase;Lipid biosynthesis;Lipid metabolism;Lyase;Membrane;Phospholipid biosynthesis;Phospholipid metabolism;Pyruvate;Reference proteome;Zymogen |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Cell membrane {ECO:0000255|HAMAP-Rule:MF_00664}; Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_00664}. |
| Modified Residue | MOD_RES 159; /note=Pyruvic acid (Ser); by autocatalysis; /evidence=ECO:0000255|HAMAP-Rule:MF_00664 |
| 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 (By similarity). {ECO:0000250|UniProtKB:B3L2V1, ECO:0000250|UniProtKB:P0A8K1}.; 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 post-translation cleavage follows an unusual pathway, termed non-hydrolytic serinolysis, 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. {ECO:0000255|HAMAP-Rule:MF_00664}. |
| Signal Peptide | |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 21,558 |
| Kinetics | |
| Metal Binding | |
| Rhea ID | RHEA:51488 |
| Cross Reference Brenda |