ID A0A182NQQ8_9DIPT Unreviewed; 485 AA.
AC A0A182NQQ8;
DT 07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT 07-SEP-2016, sequence version 1.
DT 13-SEP-2023, entry version 40.
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 Anopheles dirus.
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC Anophelinae; Anopheles.
OX NCBI_TaxID=7168 {ECO:0000313|EnsemblMetazoa:ADIR009993-PA, ECO:0000313|Proteomes:UP000075884};
RN [1] {ECO:0000313|Proteomes:UP000075884}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=WRAIR2 {ECO:0000313|Proteomes:UP000075884};
RG The Broad Institute Genomics Platform;
RA Neafsey D.E., Walton C., Walker B., Young S.K., Zeng Q., Gargeya S.,
RA Fitzgerald M., Haas B., Abouelleil A., Allen A.W., Alvarado L.,
RA Arachchi H.M., Berlin A.M., Chapman S.B., Gainer-Dewar J., Goldberg J.,
RA Griggs A., Gujja S., Hansen M., Howarth C., Imamovic A., Ireland A.,
RA Larimer J., McCowan C., Murphy C., Pearson M., Poon T.W., Priest M.,
RA Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Anopheles dirus WRAIR2.";
RL Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EnsemblMetazoa:ADIR009993-PA}
RP IDENTIFICATION.
RC STRAIN=WRAIR2 {ECO:0000313|EnsemblMetazoa:ADIR009993-PA};
RG EnsemblMetazoa;
RL Submitted (MAY-2020) 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; A0A182NQQ8; -.
DR STRING; 7168.A0A182NQQ8; -.
DR EnsemblMetazoa; ADIR009993-RA; ADIR009993-PA; ADIR009993.
DR VEuPathDB; VectorBase:ADIR009993; -.
DR OrthoDB; 1216391at2759; -.
DR UniPathway; UPA00558; UER00616.
DR Proteomes; UP000075884; 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; 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};
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..425
FT /note="Phosphatidylserine decarboxylase beta chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT /id="PRO_5023325912"
FT CHAIN 426..485
FT /note="Phosphatidylserine decarboxylase alpha chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT /id="PRO_5023325913"
FT TOPO_DOM 1..125
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT TOPO_DOM 145..485
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT REGION 41..84
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 66..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 243
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT ACT_SITE 314
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT ACT_SITE 426
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT ACT_SITE 426
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid; for decarboxylase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT SITE 425..426
FT /note="Cleavage (non-hydrolytic); by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT MOD_RES 426
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
SQ SEQUENCE 485 AA; 56077 MW; 0BF67E24EBA3D84E CRC64;
MAVFMPKYRL FSKAVNLKPT PRQWSARWTI VQRSIYGTRQ LQQQPNATST NQHQHHQHQH
HHQQQQHQQH QQQFHQRQST TGKSRSKVYR RWSWQAGAGW TILSVLDWWL LAAGGWLTWR
GVFLRWTPIG ICMVVAAKWH LHNRELDKKG LPRTAAKWQA KMYCSLPLRL MSRCWGWMAD
RKVPTPARPM VYGLYSTTFG VKMEEAATDN FKEYRSLGEF FTRPLKEDAR PIDPKISFVS
PCDGRILHFG PATSSQIEQV KGVSYSLEAF LGPPTWTKKD APEMVEKVKK KSSPDSVLYQ
CVIYLAPGDY HRFHSPTLWK PELRRHFSGE LLSVSPKIAG WIPGLFCLNE RAVYIGRWKH
GFFSYTAVGA TNVGSVEIFM DEKLKTNKWV GLACGSHKKK EYDELELPND KYLDKGELVG
QFRMGSTIVL IFEAPKEFKF NLFPGQRVKV GERLGTFEGT EEQVEDTEEV KRVIESLCDS
EMTKL
//
