ID A0A1I8INB4_9PLAT Unreviewed; 506 AA.
AC A0A1I8INB4;
DT 18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT 18-JAN-2017, sequence version 1.
DT 13-SEP-2023, entry version 31.
DE RecName: Full=Phosphatidylserine decarboxylase proenzyme, 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 beta chain {ECO:0000256|HAMAP-Rule:MF_03208};
DE Contains:
DE RecName: Full=Phosphatidylserine decarboxylase alpha chain {ECO:0000256|HAMAP-Rule:MF_03208};
OS Macrostomum lignano.
OC Eukaryota; Metazoa; Spiralia; Lophotrochozoa; Platyhelminthes;
OC Rhabditophora; Macrostomorpha; Macrostomida; Macrostomidae; Macrostomum.
OX NCBI_TaxID=282301 {ECO:0000313|Proteomes:UP000095280, ECO:0000313|WBParaSite:maker-uti_cns_0014669-snap-gene-0.3-mRNA-1};
RN [1] {ECO:0000313|WBParaSite:maker-uti_cns_0014669-snap-gene-0.3-mRNA-1}
RP IDENTIFICATION.
RG WormBaseParasite;
RL Submitted (NOV-2016) to UniProtKB.
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 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 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 AlphaFoldDB; A0A1I8INB4; -.
DR WBParaSite; maker-uti_cns_0014669-snap-gene-0.3-mRNA-1; maker-uti_cns_0014669-snap-gene-0.3-mRNA-1; maker-uti_cns_0014669-snap-gene-0.3.
DR UniPathway; UPA00558; UER00616.
DR Proteomes; UP000095280; Unplaced.
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; 1.
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, ECO:0000256|SAM:Phobius};
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 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..324
FT /note="Phosphatidylserine decarboxylase beta chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT /id="PRO_5023519182"
FT CHAIN 325..506
FT /note="Phosphatidylserine decarboxylase alpha chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT /id="PRO_5023519181"
FT TOPO_DOM 1..19
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT TOPO_DOM 39..506
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT TRANSMEM 425..450
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 477..498
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT ACT_SITE 142
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT ACT_SITE 217
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT ACT_SITE 325
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT ACT_SITE 325
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid; for decarboxylase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT SITE 324..325
FT /note="Cleavage (non-hydrolytic); by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT MOD_RES 325
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
SQ SEQUENCE 506 AA; 55898 MW; 1CF633540A61CA96 CRC64;
MFKYMLIPVQ SAMRIIKMMT IASASGTIAY SSWLAFRPLT NEEKANWNAI YMEDSSIRLR
VYRRLPLNAL SRLWGRCQHV ELPEFARQPA YSLYARLFHC NLTEVANSDL TGYRNLSEFF
RRELRPDARP VAAKVGLVAP ADGLVLHLGR AEPDGRLEQV KGVDYTLQSF LGPLSSDNSN
PRLPDSEYYS RLKTHSSGSS LYHCVIYLSP GDYHRFHSPT DWQASRRRHY PGYLMSVSPG
VAGLVRGLFC LNERAVFTGS WRHGFFAYAA VGATNVGNIR VYADQDLVTN AGGPLAPYRD
LDLQSKQGGL RLSKGELFGE FDLGSTIVLV FEAPDNFEFK VHPGQRVRVG EALSNFRPAA
GSSGTGDLQN CSNRLRLLML LVVWLSLEYW RSSDLTLAFI STANGSASAN FASRLLSSRT
SVFRIASALI LPGVVAGVCV TTGAAPVILV DAERRRHAHG VSLCQQNLLY TQRRPTAATV
SFSIAFIAIS CGLCLRWQSG CTGGVF
//
