PISD_CAEEL
ID PISD_CAEEL Reviewed; 377 AA.
AC Q10949; Q6AHR5;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Phosphatidylserine decarboxylase proenzyme, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03208};
DE EC=4.1.1.65 {ECO:0000255|HAMAP-Rule:MF_03208};
DE Contains:
DE RecName: Full=Phosphatidylserine decarboxylase beta chain {ECO:0000255|HAMAP-Rule:MF_03208};
DE Contains:
DE RecName: Full=Phosphatidylserine decarboxylase alpha chain {ECO:0000255|HAMAP-Rule:MF_03208};
DE Flags: Precursor;
GN Name=psd-1 {ECO:0000255|HAMAP-Rule:MF_03208}; ORFNames=B0361.5;
OS Caenorhabditis elegans.
OC Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC Rhabditina; Rhabditomorpha; Rhabditoidea; Rhabditidae; Peloderinae;
OC Caenorhabditis.
OX NCBI_TaxID=6239;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND ALTERNATIVE SPLICING.
RC STRAIN=Bristol N2;
RX PubMed=9851916; DOI=10.1126/science.282.5396.2012;
RG The C. elegans sequencing consortium;
RT "Genome sequence of the nematode C. elegans: a platform for investigating
RT biology.";
RL Science 282:2012-2018(1998).
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}.
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 beta chain]:
CC Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208}; Single-
CC pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03208}; Intermembrane
CC side {ECO:0000255|HAMAP-Rule:MF_03208}.
CC -!- SUBCELLULAR LOCATION: [Phosphatidylserine decarboxylase alpha chain]:
CC Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03208};
CC Intermembrane side {ECO:0000255|HAMAP-Rule:MF_03208}. Note=Anchored to
CC the mitochondrial inner membrane through its interaction with the
CC integral membrane beta chain. {ECO:0000255|HAMAP-Rule:MF_03208}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=b;
CC IsoId=Q10949-1; Sequence=Displayed;
CC Name=a;
CC IsoId=Q10949-2; Sequence=VSP_013776, VSP_013777;
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 -!- 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; FO080185; CCD61819.1; -; Genomic_DNA.
DR EMBL; FO080185; CCD61820.1; -; Genomic_DNA.
DR PIR; A88504; A88504.
DR RefSeq; NP_001021127.1; NM_001025956.3. [Q10949-2]
DR RefSeq; NP_001021128.1; NM_001025957.3. [Q10949-1]
DR AlphaFoldDB; Q10949; -.
DR SMR; Q10949; -.
DR BioGRID; 41238; 1.
DR STRING; 6239.B0361.5b; -.
DR EPD; Q10949; -.
DR PaxDb; Q10949; -.
DR PeptideAtlas; Q10949; -.
DR PRIDE; Q10949; -.
DR EnsemblMetazoa; B0361.5a.1; B0361.5a.1; WBGene00015159. [Q10949-2]
DR EnsemblMetazoa; B0361.5b.1; B0361.5b.1; WBGene00015159. [Q10949-1]
DR GeneID; 176027; -.
DR KEGG; cel:CELE_B0361.5; -.
DR UCSC; B0361.5b; c. elegans. [Q10949-1]
DR CTD; 176027; -.
DR WormBase; B0361.5a; CE37696; WBGene00015159; psd-1. [Q10949-2]
DR WormBase; B0361.5b; CE37076; WBGene00015159; psd-1. [Q10949-1]
DR eggNOG; KOG2420; Eukaryota.
DR GeneTree; ENSGT00390000013484; -.
DR InParanoid; Q10949; -.
DR OMA; HNLFVLN; -.
DR OrthoDB; 1226492at2759; -.
DR PhylomeDB; Q10949; -.
DR UniPathway; UPA00558; UER00616.
DR PRO; PR:Q10949; -.
DR Proteomes; UP000001940; Chromosome III.
DR Bgee; WBGene00015159; Expressed in larva and 4 other tissues.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0004609; F:phosphatidylserine decarboxylase activity; IBA:GO_Central.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IBA:GO_Central.
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.
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 Alternative splicing; Decarboxylase; Lipid biosynthesis; Lipid metabolism;
KW Lyase; Membrane; Mitochondrion; Mitochondrion inner membrane;
KW Phospholipid biosynthesis; Phospholipid metabolism; Pyruvate;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix;
KW Zymogen.
FT TRANSIT 1..34
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT CHAIN 35..377
FT /note="Phosphatidylserine decarboxylase proenzyme,
FT mitochondrial"
FT /id="PRO_0000435637"
FT CHAIN 35..343
FT /note="Phosphatidylserine decarboxylase beta chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT /id="PRO_0000029841"
FT CHAIN 344..377
FT /note="Phosphatidylserine decarboxylase alpha chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT /id="PRO_0000029842"
FT TOPO_DOM 35..61
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT TRANSMEM 62..80
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT TOPO_DOM 81..377
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT ACT_SITE 181
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT ACT_SITE 238
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT ACT_SITE 344
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT ACT_SITE 344
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid; for decarboxylase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT SITE 343..344
FT /note="Cleavage (non-hydrolytic); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT MOD_RES 344
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT VAR_SEQ 2..30
FT /note="Missing (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_013776"
FT VAR_SEQ 31..57
FT /note="VRELTNQSKNVYATKEVIIGASQKKKR -> LDIYSGGFLHPDSLMALNPFL
FT IFVAFW (in isoform a)"
FT /evidence="ECO:0000305"
FT /id="VSP_013777"
SQ SEQUENCE 377 AA; 42487 MW; DDBD39AAC26C9D5B CRC64;
MMPLFNVLRS ARMLPAVSKK VVSPPMMLRS VRELTNQSKN VYATKEVIIG ASQKKKRSWV
KWLSVSTLII GGASYVGYLF TPDWREIVDS KHYYSNWKIR VYLSLPFNTA SRVIGGLANQ
EIPVWLREHL LGGFARMYDC RMDDCVDPDF KNYPSFAAFF NRKLKESTRP ISASPLVSPA
DGTVLHFGKV EDNKIEYVKG HDYDVDKFLG DVDLPQKDEL DLYQVVIYLA PGDYHAFHSP
ARWVANQCRH VPGLLLSVRP TLLSHVPHLF CLNERVVLNG SWRHGFFSMS AVAATNVGDI
VVDAEPSLRT NIVRRKTQKI MNTETEIHAP YVSGERVGEF RLGSTIVLVF QAPPTIKFAI
KAGDPLRYGQ SLVADGV
