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Phosphatidylserine decarboxylase proenzyme 1, mitochondrial (EC 4.1.1.65) [Cleaved into: Phosphatidylserine decarboxylase 1 beta chain; Phosphatidylserine decarboxylase 1 alpha chain]

 A0A084GH87_9PEZI        Unreviewed;       459 AA.
A0A084GH87;
29-OCT-2014, integrated into UniProtKB/TrEMBL.
29-OCT-2014, sequence version 1.
22-NOV-2017, entry version 17.
RecName: Full=Phosphatidylserine decarboxylase proenzyme 1, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03208};
EC=4.1.1.65 {ECO:0000256|HAMAP-Rule:MF_03208};
Contains:
RecName: Full=Phosphatidylserine decarboxylase 1 alpha chain {ECO:0000256|HAMAP-Rule:MF_03208};
Contains:
RecName: Full=Phosphatidylserine decarboxylase 1 beta chain {ECO:0000256|HAMAP-Rule:MF_03208};
Name=PSD1 {ECO:0000256|HAMAP-Rule:MF_03208};
ORFNames=SAPIO_CDS0544 {ECO:0000313|EMBL:KEZ46699.1};
Scedosporium apiospermum.
Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina;
Sordariomycetes; Hypocreomycetidae; Microascales; Microascaceae;
Scedosporium.
NCBI_TaxID=563466 {ECO:0000313|EMBL:KEZ46699.1, ECO:0000313|Proteomes:UP000028545};
[1] {ECO:0000313|EMBL:KEZ46699.1, ECO:0000313|Proteomes:UP000028545}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=IHEM 14462 {ECO:0000313|EMBL:KEZ46699.1,
ECO:0000313|Proteomes:UP000028545};
Vandeputte P., Rechenmann M., Bouchara J.-P.;
Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Catalyzes the formation of phosphatidylethanolamine
(PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in
phospholipid metabolism and in the interorganelle trafficking of
phosphatidylserine. {ECO:0000256|HAMAP-Rule:MF_03208}.
-!- CATALYTIC ACTIVITY: Phosphatidyl-L-serine =
phosphatidylethanolamine + CO(2). {ECO:0000256|HAMAP-
Rule:MF_03208}.
-!- COFACTOR:
Name=pyruvate; Xref=ChEBI:CHEBI:15361;
Evidence={ECO:0000256|HAMAP-Rule:MF_03208};
Note=Binds 1 pyruvoyl group covalently per subunit.
{ECO:0000256|HAMAP-Rule:MF_03208};
-!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol:
step 2/2. {ECO:0000256|HAMAP-Rule:MF_03208}.
-!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit
and a small pyruvoyl-containing alpha subunit. {ECO:0000256|HAMAP-
Rule:MF_03208}.
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
{ECO:0000256|HAMAP-Rule:MF_03208}; Peripheral membrane protein
{ECO:0000256|HAMAP-Rule:MF_03208}; Intermembrane side
{ECO:0000256|HAMAP-Rule:MF_03208}. Note=Anchored to the
mitochondrial inner membrane through its interaction with the
integral membrane beta chain. {ECO:0000256|HAMAP-Rule:MF_03208}.
-!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
{ECO:0000256|HAMAP-Rule:MF_03208}; Single-pass membrane protein
{ECO:0000256|HAMAP-Rule:MF_03208}; Intermembrane side
{ECO:0000256|HAMAP-Rule:MF_03208}.
-!- 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:0000256|HAMAP-Rule:MF_03208}.
-!- SIMILARITY: Belongs to the phosphatidylserine decarboxylase
family. PSD-B subfamily. Eukaryotic type I sub-subfamily.
{ECO:0000256|HAMAP-Rule:MF_03208}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:KEZ46699.1}.
-----------------------------------------------------------------------
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EMBL; JOWA01000022; KEZ46699.1; -; Genomic_DNA.
RefSeq; XP_016646498.1; XM_016783298.1.
EnsemblFungi; KEZ46699; KEZ46699; SAPIO_CDS0544.
GeneID; 27718696; -.
UniPathway; UPA00558; UER00616.
Proteomes; UP000028545; Unassembled WGS sequence.
GO; GO:0031305; C:integral component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
GO; GO:0004609; F:phosphatidylserine decarboxylase activity; IEA:UniProtKB-UniRule.
GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IEA:UniProtKB-UniRule.
GO; GO:0016540; P:protein autoprocessing; IEA:UniProtKB-UniRule.
HAMAP; MF_03208; PS_decarb_PSD_B_type1_euk; 1.
InterPro; IPR003817; PS_Dcarbxylase.
InterPro; IPR033177; PSD.
InterPro; IPR033661; PSD_type1_euk.
PANTHER; PTHR10067; PTHR10067; 1.
Pfam; PF02666; PS_Dcarbxylase; 1.
TIGRFAMs; TIGR00163; PS_decarb; 1.
3: Inferred from homology;
Complete proteome {ECO:0000313|Proteomes:UP000028545};
Decarboxylase {ECO:0000256|HAMAP-Rule:MF_03208};
Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03208};
Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_03208};
Lyase {ECO:0000256|HAMAP-Rule:MF_03208};
Membrane {ECO:0000256|HAMAP-Rule:MF_03208};
Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03208};
Mitochondrion inner membrane {ECO:0000256|HAMAP-Rule:MF_03208};
Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03208};
Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_03208};
Pyruvate {ECO:0000256|HAMAP-Rule:MF_03208};
Reference proteome {ECO:0000313|Proteomes:UP000028545};
Transmembrane {ECO:0000256|HAMAP-Rule:MF_03208};
Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_03208};
Zymogen {ECO:0000256|HAMAP-Rule:MF_03208}.
TOPO_DOM 1 35 Mitochondrial matrix. {ECO:0000256|HAMAP-
Rule:MF_03208}.
TOPO_DOM 55 459 Mitochondrial intermembrane.
{ECO:0000256|HAMAP-Rule:MF_03208}.
ACT_SITE 143 143 Charge relay system; for
autoendoproteolytic cleavage activity.
{ECO:0000256|HAMAP-Rule:MF_03208}.
ACT_SITE 287 287 Charge relay system; for
autoendoproteolytic cleavage activity.
{ECO:0000256|HAMAP-Rule:MF_03208}.
ACT_SITE 415 415 Charge relay system; for
autoendoproteolytic cleavage activity.
{ECO:0000256|HAMAP-Rule:MF_03208}.
ACT_SITE 415 415 Schiff-base intermediate with substrate;
via pyruvic acid; for decarboxylase
activity. {ECO:0000256|HAMAP-
Rule:MF_03208}.
SITE 414 415 Cleavage (non-hydrolytic); by
autocatalysis. {ECO:0000256|HAMAP-
Rule:MF_03208}.
MOD_RES 415 415 Pyruvic acid (Ser); by autocatalysis.
{ECO:0000256|HAMAP-Rule:MF_03208}.
SEQUENCE 459 AA; 52003 MW; 8B617C7D7F2A8AE2 CRC64;
MRLSLRRRRV PEASRREYHQ QSRQRPRNPQ GSKIQWYSIP VSVGIGVVGF LHLYKSYKTT
GKDLEPVRIE QQEQNERPEI QEERSTKRPK KRPRVRPDGP CLDEVAEPDL RSYKNLAAFF
YRTLKPGVRP LDPRPDALLS PSDGRILQFG QIDGNDIEQV KGMTYTIDGL LGKHTPPPSI
TPWPSDPRDP NDMAKDEVLV NEHEEFARLN GISYTLPNLF TGQATNGRKG SLRDQAVRRD
SESAVAAVEA DLARGEPQWY DMLSPDKQTV LYYAVIYLAP GDYHRFHSPA NWVVERRRHF
AGELYSVSPY LQRTLPGLFT LNERVVLLGR WRWGFFSYVP VGATNVGSIK INFDRELRTN
SLTTDTAADR AAEEAAAKGE TYLGFSEATY ASASPVLHGH CVRRGEEMGG FQLGSTIVLV
FEAPVEKKEE DGTRSGWVWE VEKGQKIKMG QALGYTTRV


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