A0A9Q5I1Z3 · A0A9Q5I1Z3_SANBA

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 site959Charge relay system; for autoendoproteolytic cleavage activity
Active site1017Charge relay system; for autoendoproteolytic cleavage activity
Site1103-1104Cleavage (non-hydrolytic); by autocatalysis
Active site1104Charge relay system; for autoendoproteolytic cleavage activity
Active site1104Schiff-base intermediate with substrate; via pyruvic acid; for decarboxylase activity

GO annotations

AspectTerm
Cellular Componentendosome membrane
Cellular ComponentGolgi membrane
Cellular ComponentGolgi stack
Molecular Functioncalcium ion binding
Molecular Functionphosphatidylserine decarboxylase activity
Biological Processphosphatidylethanolamine biosynthetic process
Biological Processprotein autoprocessing

Keywords

Enzyme and pathway databases

Names & Taxonomy

Protein names

Gene names

    • Name
      PSD2
    • ORF names
      A7U60_g2564

Organism names

Accessions

  • Primary accession
    A0A9Q5I1Z3

Proteomes

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_50405511631-1103Phosphatidylserine decarboxylase 2 beta chain
Modified residue1104Pyruvic acid (Ser); by autocatalysis
ChainPRO_50405511621104-1164Phosphatidylserine 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.

Family & Domains

Features

Showing features for domain, region, compositional bias.

TypeIDPosition(s)Description
Domain29-152C2
Region211-303Disordered
Compositional bias237-254Acidic residues
Compositional bias268-285Polar residues
Region327-383Disordered
Compositional bias330-369Polar residues
Domain387-506C2
Domain555-590EF-hand
Region629-684Disordered
Compositional bias648-669Polar residues
Region691-710Disordered
Compositional bias735-753Polar residues
Region735-761Disordered
Region1140-1164Disordered
Compositional bias1144-1164Polar 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

Family and domain databases

Sequence

  • Sequence status
    Complete
  • Length
    1,164
  • Mass (Da)
    128,165
  • Last updated
    2023-09-13 v1
  • Checksum
    A8B1C7BBAC166381
MPRKKQVFKIKKALKSAASLPKRVRVSAIRGNGRNTLNPIPGELPIVLLRVQILGCSNLLAKDKSGTSDPFVVVSLARNRNSTPVVKRTLNPVYVAKDATFDFPIYLSLAGRLGVLELIVWDKDMLKKDYLGEASLPLESWFKEESPKDFNDPRVEPVTVNIASTRANTSASGSIQVKLGFIRPENVNHALGFDEIYNELLRRAHGARTSLVSAPPTEGIGTVRSNDAIPAYEDDGLSSDEGSDDDDEDDEREEYEGLPVRIEGSSPGTPAPASSTGTETPKAESTPVPGVNVIAPSPTAGLPPAVVVPVPVSKPSLGAKIPRVFKKRPSLPTTPSTDSGVSSASAVTGTPSPAPSSLSRPSTPGTPSAAAPGSAKRNKFPRKWKSRKADFNFNAAHDILGIVMLEIKGATDLPKLKNMTRTGWDMDPFVVVSFGKKVFRTRVIRHSLNPVWDEKLFFHVRRYETNYKLQLSVLDWDKLSSNDHVGDASFNVNELVKNAPKKDEATSLYPEDAGKLESEMQDFKLNLSTEKEMPWETKHNPVLTVRAKYQPYDLLRQQFWREYLKEYDTDDTGTLSRLELTSMLDSLGSTLSKETIDSFFIRHGKKPEEDEITTNEAIQCLEEELCRPPAEKKRLSTEDAGGPDTSIPPTPTLVNNGNDGGQTPNLGLESIDFSGAPTHPTARRQGTLTEEAAQDQALSAHPTEPNQRPSASIIQPIIDSASTRVPVGYQAAGAIEQQTSSSSSNSSDNENDESSSPSSDETFERIINVKNCPLCHRPRINKRAEVDIITHLAVCASQDWGRVDRIVVNNYVTASQAQRKWYTKVISKVSAGNYKLGANSANIIVQNRMTGQLEEEKMQVYVRLGIRLLYKGAKGRMEGARARRLLKSLTIKQGQKYDAPESASEIPAFVQFHKLKVDEILDSIDSFKTFNEFFYRKLKPDARPAEEPENPSRLVSAADCRMMVFETMNEATRLWIKGREFSVARLLGEAYSDQWEKYNGGALCIFRLAPQDYHRFHSPVDGKVGPMTYIPGEYYTVNPQAIRTALDVYGENARKIVPIDSPIFGRVMAICIGAMMVGSIVTTVQEGEEVKRGQEFGYFAFGGSTIVCLFEKGVVEWDEDLLINGRACLETLVRVGMGTGRVRRPANSNGSGSSSRARTPAVQP

Features

Showing features for compositional bias.

TypeIDPosition(s)Description
Compositional bias237-254Acidic residues
Compositional bias268-285Polar residues
Compositional bias330-369Polar residues
Compositional bias648-669Polar residues
Compositional bias735-753Polar residues
Compositional bias1144-1164Polar residues

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
LNZH02000139
EMBL· GenBank· DDBJ
OCB90193.1
EMBL· GenBank· DDBJ
Genomic DNA

Similar Proteins

Disclaimer

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