A0A5M9MVJ4 · A0A5M9MVJ4_9EURO

  • Protein
    Phosphatidylserine decarboxylase proenzyme 2
  • Gene
    PSD2
  • Status
    UniProtKB unreviewed (TrEMBL)
  • Amino acids
  • Protein existence
    Inferred from homology
  • Annotation score
    4/5

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.

Caution

The sequence shown here is derived from an EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is preliminary data.

Catalytic activity

Cofactor

pyruvate (UniProtKB | Rhea| CHEBI:15361 )

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.

TypeIDPosition(s)Description
Active site854Charge relay system; for autoendoproteolytic cleavage activity
Active site912Charge relay system; for autoendoproteolytic cleavage activity
Site998-999Cleavage (non-hydrolytic); by autocatalysis
Active site999Charge relay system; for autoendoproteolytic cleavage activity
Active site999Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity

GO annotations

AspectTerm
Cellular Componentendosome membrane
Cellular ComponentGolgi membrane
Cellular ComponentGolgi stack
Cellular ComponentMIS12/MIND type complex
Molecular Functioncalcium ion binding
Molecular Functionphosphatidylserine decarboxylase activity
Biological Processcell division
Biological Processchromosome segregation
Biological Processphosphatidylethanolamine biosynthetic process
Biological Processprotein autoprocessing

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

Gene names

    • Name
      PSD2
    • ORF names
      ATNIH1004_007930

Organism names

  • Taxonomic identifier
  • Organism
  • Strain
    • NIH1004
  • Taxonomic lineage
    Eukaryota > Fungi > Dikarya > Ascomycota > Pezizomycotina > Eurotiomycetes > Eurotiomycetidae > Eurotiales > Aspergillaceae > Aspergillus > Aspergillus subgen. Circumdati

Accessions

  • Primary accession
    A0A5M9MVJ4

Proteomes

Organism-specific databases

Subcellular Location

Golgi apparatus membrane
; Peripheral membrane protein
Endosome membrane
; Peripheral membrane protein

Keywords

PTM/Processing

Features

Showing features for chain, modified residue.

TypeIDPosition(s)Description
ChainPRO_50245184101-998Phosphatidylserine decarboxylase 2 beta chain
Modified residue999Pyruvic acid (Ser); by autocatalysis
ChainPRO_5024518409999-1857Phosphatidylserine decarboxylase 2 alpha chain

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

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.

Family & Domains

Features

Showing features for region, compositional bias, domain.

TypeIDPosition(s)Description
Region1-35Disordered
Compositional bias9-33Polar residues
Domain22-139C2
Region192-226Disordered
Domain237-362C2
Region367-457Disordered
Compositional bias374-457Polar residues
Domain507-542EF-hand
Compositional bias1312-1339Polar residues
Region1312-1542Disordered
Compositional bias1340-1374Basic and acidic residues
Compositional bias1449-1472Basic and acidic residues
Region1626-1645Disordered
Region1667-1716Disordered
Compositional bias1678-1704Polar residues
Region1738-1757Disordered
Compositional bias1740-1757Polar residues

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

Phylogenomic databases

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,857
  • Mass (Da)
    206,855
  • Last updated
    2020-02-26 v1
  • Checksum
    341E4C4BFE082EE6
MVRLPIPQRLTSHLSTRSNASTPGQSRSTSPMRLPESKPLVLKVSVLRGRNLAPKDRNGRSDPYLIVTLGDARQSTPMIPKTLNPEWNVTFEMPVVGVPLLECICWDHDRFGKDYMGEFDIPLEEIFSPGEVYQQPQWYTLTSKRKTIKKKDSTVSGEILLQFSLIDTSNPTASPTDTYNKYKNLVCAGEEEDDFPQIPPLGLDGVDRDEETSDETDDPSKPEVVEKRRRRLRLARLKRKSIAARAYQFSGAGNGVQGIVFMEIVKVTDLPPERNVTRTSFDMDPFVVTSLGRKTLRTPVIRHNLNPVYNEKMVFQVMKHEQSYTIGFTVMDRDKFSGNDFVASAGFPLQTLVQAAPDADPETGLYKFLDSTLDPTGSEHSGSDNTAGIKIDISPSPSHNSLSNMSNKVRSRSSTASISAQSVQSAHSGQELSTSSPPAIVTEEGSSDSISNAPTMTNNGNYVASSLDSDGLQAYRIPLTLKNKERWEDKHSPLLVVKAKYMPYRALRQQFWRLMLRQYDADDSGRIDKVELTTMLDTLGSTLKESTIDSFFERFSVENEPCETMDLTFDQAVICLEDTLQALQIANRAGPKNHALTSSAISQESEDPSSCDEDIETSAAIPPTTAPQALAVPILASDQLAMDEELEPDDLGDERGEEHVIEIRECPLCHQPRLSKRSDADIITHIATCASRDWRQVDNLVMGGFVTSSQAQRKWYTKVITKISYGGYKLGANSANILVQDRITGQINEERMSVYVRLGIRLLYRGLKSREMEKKRIRKILKSMSVKQGKKYDDPASASQIQDFINFHQLDLSEVLLPLDKFKNFNEFFYRQLKPGARPCSAPNEPRIVVSPADCRSVVFDRMNEATGIWVKGREFSIDRLLGDAYPEDVQRYRNGALGIFRLAPQDYHRFHIPVDGVLGTPKTIGGEYYTVNPMAIRSALDVYGENVRVLVPIDSVAHGRVMVVCVGAMMVGSTVITRQGGEKVSRGDELGYFKFGGSTLLLLFEEGTIKFDSDLVGNSKGPLETLIRVGMSVGHSPDIPQFEPDMPKKPESLTSEDIQAARRRIEGSLAPLADGRFRNSQRSLAPHPTRHYQNNRVLRRLARANPRQPDAGLYALLRKERFSIPQTVYESDLIVSSGRCQLRLVVESAPRTLRHVASPPPFFVTGLADRPSSQLRPREIRAPTTNSSERISTAQNSRLVESFLVVLCFGEVKFVKGYLKKRAAGSSQLLEQRGHSSQYHDCCLETSKEKSAKRLFPTFRQLFELLLLLLPTTPPLSLGPDMIVTVLATTTTKTERRQPLRQIDMVTSQAQARFVSSSSGKHDRIGTRASTRLSLTSQEKEENASRTKRKSSFDEDVDDFQFTRIKPKKAKPTVDAIPEVPQPLPEKSAPQQSPKRGRPPKKRQEPKPDSSGEVQNTIESKPKRQTRGAAKAALVEPETQPASATRSTRKGDHVEPVPKEKKRRKGRPSKSNDEPQQQNGFVSPEPPKAGTATIALPIADTPVMQRNKEMRGQTKSGKGNRRSSLGMRGRRASSLIDSGASNALPHKEVDTADFYKHIASDGLPEPRRMRQLLTWCATRALGEKPSGSSTEDASERLAARVIQEELLKDFSTNSELSNWFAREEVDSPSVVVKKPNPKNVQNTEKIKELEEQIQKLQKQKQALNALLRPPPSPSIKPASKQLDTAQNGQSGPPPSQAESNTNKRARSPEPDPIDLSLLEPSQQQLYALIDPNAATRHPDTELQKAQSSWEPNSLSTVTPSTISTRLSRIAAGLVPTLDSFAAGVHDIELYRAMSDSVSSRVLRICAERLDERDARNSLRRLAIEEEEGDHQNISIRQRPREDLGMILGALSRVERR

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias9-33Polar residues
Compositional bias374-457Polar residues
Compositional bias1312-1339Polar residues
Compositional bias1340-1374Basic and acidic residues
Compositional bias1449-1472Basic and acidic residues
Compositional bias1678-1704Polar residues
Compositional bias1740-1757Polar residues

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
QUQM01000007
EMBL· GenBank· DDBJ
KAA8646497.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

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