ID A0A0D2EGM0_9EURO Unreviewed; 559 AA.
AC A0A0D2EGM0;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 44.
DE RecName: Full=Phosphatidylserine decarboxylase proenzyme 1, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03208};
DE EC=4.1.1.65 {ECO:0000256|HAMAP-Rule:MF_03208};
DE Contains:
DE RecName: Full=Phosphatidylserine decarboxylase 1 beta chain {ECO:0000256|HAMAP-Rule:MF_03208};
DE Contains:
DE RecName: Full=Phosphatidylserine decarboxylase 1 alpha chain {ECO:0000256|HAMAP-Rule:MF_03208};
GN Name=PSD1 {ECO:0000256|HAMAP-Rule:MF_03208};
GN ORFNames=PV05_06910 {ECO:0000313|EMBL:KIW54558.1};
OS Exophiala xenobiotica.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=348802 {ECO:0000313|EMBL:KIW54558.1, ECO:0000313|Proteomes:UP000054342};
RN [1] {ECO:0000313|EMBL:KIW54558.1, ECO:0000313|Proteomes:UP000054342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 118157 {ECO:0000313|EMBL:KIW54558.1,
RC ECO:0000313|Proteomes:UP000054342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala xenobiotica CBS118157.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_03208}.
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:0000256|HAMAP-
CC Rule:MF_03208};
CC -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_03208};
CC Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000256|HAMAP-
CC Rule:MF_03208};
CC -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step
CC 2/2. {ECO:0000256|HAMAP-Rule:MF_03208}.
CC -!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit and a
CC small pyruvoyl-containing alpha subunit. {ECO:0000256|HAMAP-
CC Rule:MF_03208}.
CC -!- SUBCELLULAR LOCATION: [Phosphatidylserine decarboxylase 1 alpha chain]:
CC Mitochondrion inner membrane {ECO:0000256|HAMAP-Rule:MF_03208};
CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_03208};
CC Intermembrane side {ECO:0000256|HAMAP-Rule:MF_03208}. Note=Anchored to
CC the mitochondrial inner membrane through its interaction with the
CC integral membrane beta chain. {ECO:0000256|HAMAP-Rule:MF_03208}.
CC -!- SUBCELLULAR LOCATION: [Phosphatidylserine decarboxylase 1 beta chain]:
CC Mitochondrion inner membrane {ECO:0000256|HAMAP-Rule:MF_03208}; Single-
CC pass membrane protein {ECO:0000256|HAMAP-Rule:MF_03208}; Intermembrane
CC side {ECO:0000256|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:0000256|HAMAP-Rule:MF_03208}.
CC -!- SIMILARITY: Belongs to the phosphatidylserine decarboxylase family.
CC PSD-B subfamily. Eukaryotic type I sub-subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_03208}.
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DR EMBL; KN847320; KIW54558.1; -; Genomic_DNA.
DR RefSeq; XP_013315142.1; XM_013459688.1.
DR AlphaFoldDB; A0A0D2EGM0; -.
DR STRING; 348802.A0A0D2EGM0; -.
DR GeneID; 25328818; -.
DR HOGENOM; CLU_029061_1_1_1; -.
DR OrthoDB; 1216391at2759; -.
DR UniPathway; UPA00558; UER00616.
DR Proteomes; UP000054342; Unassembled WGS sequence.
DR GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0004609; F:phosphatidylserine decarboxylase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0016540; P:protein autoprocessing; IEA:UniProtKB-UniRule.
DR HAMAP; MF_03208; PS_decarb_PSD_B_type1_euk; 1.
DR InterPro; IPR003817; PS_Dcarbxylase.
DR InterPro; IPR033177; PSD-B.
DR InterPro; IPR033661; PSD_type1_euk.
DR NCBIfam; TIGR00163; PS_decarb; 1.
DR PANTHER; PTHR10067; PHOSPHATIDYLSERINE DECARBOXYLASE; 1.
DR PANTHER; PTHR10067:SF6; PHOSPHATIDYLSERINE DECARBOXYLASE PROENZYME, MITOCHONDRIAL; 1.
DR Pfam; PF02666; PS_Dcarbxylase; 2.
PE 3: Inferred from homology;
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW Rule:MF_03208}; Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03208};
KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_03208};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_03208};
KW Membrane {ECO:0000256|HAMAP-Rule:MF_03208};
KW Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03208};
KW Mitochondrion inner membrane {ECO:0000256|HAMAP-Rule:MF_03208};
KW Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03208};
KW Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_03208};
KW Pyruvate {ECO:0000256|HAMAP-Rule:MF_03208};
KW Reference proteome {ECO:0000313|Proteomes:UP000054342};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_03208};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_03208}; Zymogen {ECO:0000256|HAMAP-Rule:MF_03208}.
FT CHAIN 1..504
FT /note="Phosphatidylserine decarboxylase 1 beta chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT /id="PRO_5023484004"
FT CHAIN 505..559
FT /note="Phosphatidylserine decarboxylase 1 alpha chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT /id="PRO_5023484003"
FT TOPO_DOM 1..90
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT TOPO_DOM 110..559
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT REGION 110..131
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 257..286
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 311..334
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 113..131
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 258..274
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 225
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT ACT_SITE 377
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT ACT_SITE 505
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT ACT_SITE 505
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid; for decarboxylase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT SITE 504..505
FT /note="Cleavage (non-hydrolytic); by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT MOD_RES 505
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
SQ SEQUENCE 559 AA; 62242 MW; C69638DA0895858C CRC64;
MATATRVGRA CLYRRSPTTP SIPWHLTRPL FEPVPSYRQP QFHIQLRVHQ RRPFTCTSRR
CKEDRQNHEE SFSSRLGKAW RATRIEWKPI PIGLGIGFLG LVQFMRIRNR EGGAQEGPGE
TDGKRPPKRE RIYPTGGGWQ VQIMSTLPLK AISRVWGRFN ELTIPYYLRV PGFKLYGWIF
GVNFSEIGEP DLHAYPNLAS FFYRELKPGL RPLDPNPNAV LSPADATVLQ FGNIENGKVE
QVKGMTYSVD ALLGKIAPTT PNPQSPSSIF AAPKDQQSRP EDDPDLEAKS IRADEEFANM
NGISYTLPNL FSGTQSSPKS QSKQDASTKS LPSSEAAVSA DLASTQPWWS PFSSPSTNTK
LHYCVVYLAP GDYHRFHSPV SWVCSARRHF AGELYSVSPY VQRMLPGLFT LNERVVLLGR
WKYGFFSYTA VGATNVGSIV INFDKELRTN SLTTDTEADR QAAAAAERGE PYSGFSEATY
DNASKVLKGH ALRRGEEMGG FKLGSSIVLV FETPAGRKKD SLDEGATVDA ESSSGFRWNV
ERGQKVKVGQ ALGYVLDEE
//
