A0A5M9MVJ4 · A0A5M9MVJ4_9EURO
- ProteinPhosphatidylserine decarboxylase proenzyme 2
- GenePSD2
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1857 (go to sequence)
- Protein existenceInferred from homology
- Annotation score4/5
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.
Catalytic activity
- a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H+ = a 1,2-diacyl-sn-glycero-3-phosphoethanolamine + CO2
Cofactor
Note: Binds 1 pyruvoyl group covalently per subunit.
Pathway
Lipid metabolism.
Phospholipid metabolism; phosphatidylethanolamine biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step 2/2.
Features
Showing features for active site, site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Active site | 854 | Charge relay system; for autoendoproteolytic cleavage activity | ||||
Sequence: D | ||||||
Active site | 912 | Charge relay system; for autoendoproteolytic cleavage activity | ||||
Sequence: H | ||||||
Site | 998-999 | Cleavage (non-hydrolytic); by autocatalysis | ||||
Sequence: GS | ||||||
Active site | 999 | Charge relay system; for autoendoproteolytic cleavage activity | ||||
Sequence: S | ||||||
Active site | 999 | Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity | ||||
Sequence: S |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | endosome membrane | |
Cellular Component | Golgi membrane | |
Cellular Component | Golgi stack | |
Cellular Component | MIS12/MIND type complex | |
Molecular Function | calcium ion binding | |
Molecular Function | phosphatidylserine decarboxylase activity | |
Biological Process | cell division | |
Biological Process | chromosome segregation | |
Biological Process | phosphatidylethanolamine biosynthetic process | |
Biological Process | protein autoprocessing |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePhosphatidylserine decarboxylase proenzyme 2
- EC number
- Cleaved into 2 chains
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Circumdati
Accessions
- Primary accessionA0A5M9MVJ4
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Golgi apparatus membrane ; Peripheral membrane protein
Endosome membrane ; Peripheral membrane protein
Keywords
- Cellular component
PTM/Processing
Features
Showing features for chain, modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Chain | PRO_5024518410 | 1-998 | Phosphatidylserine decarboxylase 2 beta chain | |||
Sequence: MVRLPIPQRLTSHLSTRSNASTPGQSRSTSPMRLPESKPLVLKVSVLRGRNLAPKDRNGRSDPYLIVTLGDARQSTPMIPKTLNPEWNVTFEMPVVGVPLLECICWDHDRFGKDYMGEFDIPLEEIFSPGEVYQQPQWYTLTSKRKTIKKKDSTVSGEILLQFSLIDTSNPTASPTDTYNKYKNLVCAGEEEDDFPQIPPLGLDGVDRDEETSDETDDPSKPEVVEKRRRRLRLARLKRKSIAARAYQFSGAGNGVQGIVFMEIVKVTDLPPERNVTRTSFDMDPFVVTSLGRKTLRTPVIRHNLNPVYNEKMVFQVMKHEQSYTIGFTVMDRDKFSGNDFVASAGFPLQTLVQAAPDADPETGLYKFLDSTLDPTGSEHSGSDNTAGIKIDISPSPSHNSLSNMSNKVRSRSSTASISAQSVQSAHSGQELSTSSPPAIVTEEGSSDSISNAPTMTNNGNYVASSLDSDGLQAYRIPLTLKNKERWEDKHSPLLVVKAKYMPYRALRQQFWRLMLRQYDADDSGRIDKVELTTMLDTLGSTLKESTIDSFFERFSVENEPCETMDLTFDQAVICLEDTLQALQIANRAGPKNHALTSSAISQESEDPSSCDEDIETSAAIPPTTAPQALAVPILASDQLAMDEELEPDDLGDERGEEHVIEIRECPLCHQPRLSKRSDADIITHIATCASRDWRQVDNLVMGGFVTSSQAQRKWYTKVITKISYGGYKLGANSANILVQDRITGQINEERMSVYVRLGIRLLYRGLKSREMEKKRIRKILKSMSVKQGKKYDDPASASQIQDFINFHQLDLSEVLLPLDKFKNFNEFFYRQLKPGARPCSAPNEPRIVVSPADCRSVVFDRMNEATGIWVKGREFSIDRLLGDAYPEDVQRYRNGALGIFRLAPQDYHRFHIPVDGVLGTPKTIGGEYYTVNPMAIRSALDVYGENVRVLVPIDSVAHGRVMVVCVGAMMVGSTVITRQGGEKVSRGDELGYFKFGG | ||||||
Modified residue | 999 | Pyruvic acid (Ser); by autocatalysis | ||||
Sequence: S | ||||||
Chain | PRO_5024518409 | 999-1857 | Phosphatidylserine decarboxylase 2 alpha chain | |||
Sequence: STLLLLFEEGTIKFDSDLVGNSKGPLETLIRVGMSVGHSPDIPQFEPDMPKKPESLTSEDIQAARRRIEGSLAPLADGRFRNSQRSLAPHPTRHYQNNRVLRRLARANPRQPDAGLYALLRKERFSIPQTVYESDLIVSSGRCQLRLVVESAPRTLRHVASPPPFFVTGLADRPSSQLRPREIRAPTTNSSERISTAQNSRLVESFLVVLCFGEVKFVKGYLKKRAAGSSQLLEQRGHSSQYHDCCLETSKEKSAKRLFPTFRQLFELLLLLLPTTPPLSLGPDMIVTVLATTTTKTERRQPLRQIDMVTSQAQARFVSSSSGKHDRIGTRASTRLSLTSQEKEENASRTKRKSSFDEDVDDFQFTRIKPKKAKPTVDAIPEVPQPLPEKSAPQQSPKRGRPPKKRQEPKPDSSGEVQNTIESKPKRQTRGAAKAALVEPETQPASATRSTRKGDHVEPVPKEKKRRKGRPSKSNDEPQQQNGFVSPEPPKAGTATIALPIADTPVMQRNKEMRGQTKSGKGNRRSSLGMRGRRASSLIDSGASNALPHKEVDTADFYKHIASDGLPEPRRMRQLLTWCATRALGEKPSGSSTEDASERLAARVIQEELLKDFSTNSELSNWFAREEVDSPSVVVKKPNPKNVQNTEKIKELEEQIQKLQKQKQALNALLRPPPSPSIKPASKQLDTAQNGQSGPPPSQAESNTNKRARSPEPDPIDLSLLEPSQQQLYALIDPNAATRHPDTELQKAQSSWEPNSLSTVTPSTISTRLSRIAAGLVPTLDSFAAGVHDIELYRAMSDSVSSRVLRICAERLDERDARNSLRRLAIEEEEGDHQNISIRQRPREDLGMILGALSRVERR |
Post-translational modification
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.
Keywords
- PTM
Interaction
Subunit
Heterodimer of a large membrane-associated beta subunit and a small pyruvoyl-containing alpha subunit. Interacts with pstB2. This interaction may be a means to structurally tether the donor membrane (ER) harboring PstB2 to acceptor membranes (Golgi/endosomes) harboring PSD2 during PtdSer transport to the site of PtdEtn synthesis.
Structure
Family & Domains
Features
Showing features for region, compositional bias, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-35 | Disordered | ||||
Sequence: MVRLPIPQRLTSHLSTRSNASTPGQSRSTSPMRLP | ||||||
Compositional bias | 9-33 | Polar residues | ||||
Sequence: RLTSHLSTRSNASTPGQSRSTSPMR | ||||||
Domain | 22-139 | C2 | ||||
Sequence: TPGQSRSTSPMRLPESKPLVLKVSVLRGRNLAPKDRNGRSDPYLIVTLGDARQSTPMIPKTLNPEWNVTFEMPVVGVPLLECICWDHDRFGKDYMGEFDIPLEEIFSPGEVYQQPQWY | ||||||
Region | 192-226 | Disordered | ||||
Sequence: EDDFPQIPPLGLDGVDRDEETSDETDDPSKPEVVE | ||||||
Domain | 237-362 | C2 | ||||
Sequence: LKRKSIAARAYQFSGAGNGVQGIVFMEIVKVTDLPPERNVTRTSFDMDPFVVTSLGRKTLRTPVIRHNLNPVYNEKMVFQVMKHEQSYTIGFTVMDRDKFSGNDFVASAGFPLQTLVQAAPDADPE | ||||||
Region | 367-457 | Disordered | ||||
Sequence: KFLDSTLDPTGSEHSGSDNTAGIKIDISPSPSHNSLSNMSNKVRSRSSTASISAQSVQSAHSGQELSTSSPPAIVTEEGSSDSISNAPTMT | ||||||
Compositional bias | 374-457 | Polar residues | ||||
Sequence: DPTGSEHSGSDNTAGIKIDISPSPSHNSLSNMSNKVRSRSSTASISAQSVQSAHSGQELSTSSPPAIVTEEGSSDSISNAPTMT | ||||||
Domain | 507-542 | EF-hand | ||||
Sequence: LRQQFWRLMLRQYDADDSGRIDKVELTTMLDTLGST | ||||||
Compositional bias | 1312-1339 | Polar residues | ||||
Sequence: QARFVSSSSGKHDRIGTRASTRLSLTSQ | ||||||
Region | 1312-1542 | Disordered | ||||
Sequence: QARFVSSSSGKHDRIGTRASTRLSLTSQEKEENASRTKRKSSFDEDVDDFQFTRIKPKKAKPTVDAIPEVPQPLPEKSAPQQSPKRGRPPKKRQEPKPDSSGEVQNTIESKPKRQTRGAAKAALVEPETQPASATRSTRKGDHVEPVPKEKKRRKGRPSKSNDEPQQQNGFVSPEPPKAGTATIALPIADTPVMQRNKEMRGQTKSGKGNRRSSLGMRGRRASSLIDSGAS | ||||||
Compositional bias | 1340-1374 | Basic and acidic residues | ||||
Sequence: EKEENASRTKRKSSFDEDVDDFQFTRIKPKKAKPT | ||||||
Compositional bias | 1449-1472 | Basic and acidic residues | ||||
Sequence: TRKGDHVEPVPKEKKRRKGRPSKS | ||||||
Region | 1626-1645 | Disordered | ||||
Sequence: VDSPSVVVKKPNPKNVQNTE | ||||||
Region | 1667-1716 | Disordered | ||||
Sequence: LLRPPPSPSIKPASKQLDTAQNGQSGPPPSQAESNTNKRARSPEPDPIDL | ||||||
Compositional bias | 1678-1704 | Polar residues | ||||
Sequence: PASKQLDTAQNGQSGPPPSQAESNTNK | ||||||
Region | 1738-1757 | Disordered | ||||
Sequence: HPDTELQKAQSSWEPNSLST | ||||||
Compositional bias | 1740-1757 | Polar residues | ||||
Sequence: DTELQKAQSSWEPNSLST |
Domain
The C2 domains have an essential, but non-catalytic function. They may facilitate interactions with other proteins and are required for lipid transport function.
Sequence similarities
Belongs to the phosphatidylserine decarboxylase family. PSD-B subfamily. Eukaryotic type II sub-subfamily.
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,857
- Mass (Da)206,855
- Last updated2020-02-26 v1
- Checksum341E4C4BFE082EE6
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 9-33 | Polar residues | ||||
Sequence: RLTSHLSTRSNASTPGQSRSTSPMR | ||||||
Compositional bias | 374-457 | Polar residues | ||||
Sequence: DPTGSEHSGSDNTAGIKIDISPSPSHNSLSNMSNKVRSRSSTASISAQSVQSAHSGQELSTSSPPAIVTEEGSSDSISNAPTMT | ||||||
Compositional bias | 1312-1339 | Polar residues | ||||
Sequence: QARFVSSSSGKHDRIGTRASTRLSLTSQ | ||||||
Compositional bias | 1340-1374 | Basic and acidic residues | ||||
Sequence: EKEENASRTKRKSSFDEDVDDFQFTRIKPKKAKPT | ||||||
Compositional bias | 1449-1472 | Basic and acidic residues | ||||
Sequence: TRKGDHVEPVPKEKKRRKGRPSKS | ||||||
Compositional bias | 1678-1704 | Polar residues | ||||
Sequence: PASKQLDTAQNGQSGPPPSQAESNTNK | ||||||
Compositional bias | 1740-1757 | Polar residues | ||||
Sequence: DTELQKAQSSWEPNSLST |