PSD1_KOMPG
ID PSD1_KOMPG Reviewed; 547 AA.
AC C4QX80;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 07-JUL-2009, sequence version 1.
DT 25-MAY-2022, entry version 61.
DE RecName: Full=Phosphatidylserine decarboxylase proenzyme 1, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000303|PubMed:19656201};
DE EC=4.1.1.65 {ECO:0000255|HAMAP-Rule:MF_03208};
DE Contains:
DE RecName: Full=Phosphatidylserine decarboxylase 1 beta chain {ECO:0000255|HAMAP-Rule:MF_03208};
DE Contains:
DE RecName: Full=Phosphatidylserine decarboxylase 1 alpha chain {ECO:0000255|HAMAP-Rule:MF_03208};
DE Flags: Precursor;
GN Name=PSD1 {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000303|PubMed:19656201};
GN OrderedLocusNames=PAS_chr1-4_0019;
OS Komagataella phaffii (strain GS115 / ATCC 20864) (Yeast) (Pichia pastoris).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Phaffomycetaceae; Komagataella.
OX NCBI_TaxID=644223;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GS115 / ATCC 20864;
RX PubMed=19465926; DOI=10.1038/nbt.1544;
RA De Schutter K., Lin Y.-C., Tiels P., Van Hecke A., Glinka S.,
RA Weber-Lehmann J., Rouze P., Van de Peer Y., Callewaert N.;
RT "Genome sequence of the recombinant protein production host Pichia
RT pastoris.";
RL Nat. Biotechnol. 27:561-566(2009).
RN [2]
RP FUNCTION, DISRUPTION PHENOTYPE, AND SUBCELLULAR LOCATION.
RX PubMed=19656201; DOI=10.1111/j.1567-1364.2009.00544.x;
RA Wriessnegger T., Sunga A.J., Cregg J.M., Daum G.;
RT "Identification of phosphatidylserine decarboxylases 1 and 2 from Pichia
RT pastoris.";
RL FEMS Yeast Res. 9:911-922(2009).
CC -!- FUNCTION: Catalyzes the formation of phosphatidylethanolamine (PtdEtn)
CC from phosphatidylserine (PtdSer). Plays a central role in phospholipid
CC metabolism and in the interorganelle trafficking of phosphatidylserine.
CC {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:19656201}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-
CC diacyl-sn-glycero-3-phosphoethanolamine + CO2; Xref=Rhea:RHEA:20828,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:16526, ChEBI:CHEBI:57262,
CC ChEBI:CHEBI:64612; EC=4.1.1.65; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_03208};
CC -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03208};
CC Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_03208};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step
CC 2/2. {ECO:0000255|HAMAP-Rule:MF_03208}.
CC -!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit and a
CC small pyruvoyl-containing alpha subunit. {ECO:0000255|HAMAP-
CC Rule:MF_03208}.
CC -!- SUBCELLULAR LOCATION: [Phosphatidylserine decarboxylase 1 beta chain]:
CC Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208,
CC ECO:0000305|PubMed:19656201}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03208}; Intermembrane side
CC {ECO:0000255|HAMAP-Rule:MF_03208}.
CC -!- SUBCELLULAR LOCATION: [Phosphatidylserine decarboxylase 1 alpha chain]:
CC Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208,
CC ECO:0000305|PubMed:19656201}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03208}; Intermembrane side
CC {ECO:0000255|HAMAP-Rule:MF_03208}. Note=Anchored to the mitochondrial
CC inner membrane through its interaction with the integral membrane beta
CC chain. {ECO:0000255|HAMAP-Rule:MF_03208}.
CC -!- PTM: Is synthesized initially as an inactive proenzyme. Formation of
CC the active enzyme involves a self-maturation process in which the
CC active site pyruvoyl group is generated from an internal serine residue
CC via an autocatalytic post-translational modification. Two non-identical
CC subunits are generated from the proenzyme in this reaction, and the
CC pyruvate is formed at the N-terminus of the alpha chain, which is
CC derived from the carboxyl end of the proenzyme. The autoendoproteolytic
CC cleavage occurs by a canonical serine protease mechanism, in which the
CC side chain hydroxyl group of the serine supplies its oxygen atom to
CC form the C-terminus of the beta chain, while the remainder of the
CC serine residue undergoes an oxidative deamination to produce ammonia
CC and the pyruvoyl prosthetic group on the alpha chain. During this
CC reaction, the Ser that is part of the protease active site of the
CC proenzyme becomes the pyruvoyl prosthetic group, which constitutes an
CC essential element of the active site of the mature decarboxylase.
CC {ECO:0000255|HAMAP-Rule:MF_03208}.
CC -!- DISRUPTION PHENOTYPE: Results in an almost complete loss of
CC mitochondrial phosphatidylserine decarboxylase activity.
CC {ECO:0000269|PubMed:19656201}.
CC -!- SIMILARITY: Belongs to the phosphatidylserine decarboxylase family.
CC PSD-B subfamily. Eukaryotic type I sub-subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_03208}.
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DR EMBL; FN392319; CAY67853.1; -; Genomic_DNA.
DR RefSeq; XP_002490134.1; XM_002490089.1.
DR AlphaFoldDB; C4QX80; -.
DR SMR; C4QX80; -.
DR STRING; 644223.C4QX80; -.
DR EnsemblFungi; CAY67853; CAY67853; PAS_chr1-4_0019.
DR GeneID; 8196859; -.
DR KEGG; ppa:PAS_chr1-4_0019; -.
DR eggNOG; KOG2420; Eukaryota.
DR HOGENOM; CLU_029061_1_0_1; -.
DR InParanoid; C4QX80; -.
DR OMA; RWWTLTS; -.
DR UniPathway; UPA00558; UER00616.
DR Proteomes; UP000000314; Chromosome 1.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0042393; F:histone binding; IEA:EnsemblFungi.
DR GO; GO:0004609; F:phosphatidylserine decarboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IEA:EnsemblFungi.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0010636; P:positive regulation of mitochondrial fusion; IEA:EnsemblFungi.
DR GO; GO:0010954; P:positive regulation of protein processing; IEA:EnsemblFungi.
DR GO; GO:0016540; P:protein autoprocessing; IEA:UniProtKB-UniRule.
DR GO; GO:0009268; P:response to pH; IEA:EnsemblFungi.
DR HAMAP; MF_03208; PS_decarb_PSD_B_type1_euk; 1.
DR InterPro; IPR003817; PS_Dcarbxylase.
DR InterPro; IPR033177; PSD.
DR InterPro; IPR033661; PSD_type1_euk.
DR PANTHER; PTHR10067; PTHR10067; 1.
DR Pfam; PF02666; PS_Dcarbxylase; 1.
DR TIGRFAMs; TIGR00163; PS_decarb; 1.
PE 3: Inferred from homology;
KW Decarboxylase; Lipid biosynthesis; Lipid metabolism; Lyase; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Pyruvate; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix; Zymogen.
FT TRANSIT 1..27
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT CHAIN 28..547
FT /note="Phosphatidylserine decarboxylase proenzyme 1,
FT mitochondrial"
FT /id="PRO_0000435594"
FT CHAIN 28..514
FT /note="Phosphatidylserine decarboxylase 1 beta chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT /id="PRO_0000435595"
FT CHAIN 515..547
FT /note="Phosphatidylserine decarboxylase 1 alpha chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT /id="PRO_0000435596"
FT TOPO_DOM 28..110
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT TRANSMEM 111..129
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT TOPO_DOM 130..547
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT ACT_SITE 236
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT ACT_SITE 366
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT ACT_SITE 515
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT ACT_SITE 515
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid; for decarboxylase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT SITE 514..515
FT /note="Cleavage (non-hydrolytic); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT MOD_RES 515
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
SQ SEQUENCE 547 AA; 62528 MW; 0C849B633C3F350A CRC64;
MPNRSFGVFP SVIYETRLGL SHQMRRPIGQ PLSKLSQVSQ PNQILQRNYQ YKFPRIPRPK
RNVLYYTFKR PQLSSATILR TVPSKIRNFS SRAKSKVKSS GRRRKFMSRW LALSSISVVL
YGVVNKIKHK GIQRNSSLEP DENHSVKPNS WTLYAYSTLP LKAISRVWGQ FNSFELPIWL
RSPSYKFYAY VFGVNLDEVA EPDLSKFRNL GEFFYRTIKP ETRPIDIDAE MVSPCDGKVL
KFGIIENGEI EQVKGMTYSI NALLGQQKLA APVHRINYQL DDDDVVRRHE EFARLNGISY
TIDDIIGGRG ENIHHSYMNQ GDQSLRKSSA SQVYEVSNDI AKKSSFDKQL YFAVIYLAPG
DYHRFHSPSN WVTTLRRHFV GELFSVAPFF QKTLQNLFIL NERVALLGYW KHGFFSMIPV
GATNVGSIKI NFDKDLVTNS IYESDSYAQT SFPSSDTSSC REEDESTPLI KRSSSRTKKV
IKNSCYEATY ANASKILRGQ PLSKGQEIGG FKLGSTVVLV FEAPKTFHFT LAENMKLKMG
QRIGELR
