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Database: UniProt
Entry: A0A182PRT9_9DIPT
LinkDB: A0A182PRT9_9DIPT
Original site: A0A182PRT9_9DIPT 
ID   A0A182PRT9_9DIPT        Unreviewed;       496 AA.
AC   A0A182PRT9;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   13-SEP-2023, entry version 41.
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 epiroticus.
OC   Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC   Neoptera; Endopterygota; Diptera; Nematocera; Culicoidea; Culicidae;
OC   Anophelinae; Anopheles.
OX   NCBI_TaxID=199890 {ECO:0000313|EnsemblMetazoa:AEPI009674-PA, ECO:0000313|Proteomes:UP000075885};
RN   [1] {ECO:0000313|Proteomes:UP000075885}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Epiroticus2 {ECO:0000313|Proteomes:UP000075885};
RG   The Broad Institute Genomics Platform;
RA   Neafsey D.E., Howell P., 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 epiroticus epiroticus2.";
RL   Submitted (MAR-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EnsemblMetazoa:AEPI009674-PA}
RP   IDENTIFICATION.
RC   STRAIN=Epiroticus2 {ECO:0000313|EnsemblMetazoa:AEPI009674-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; A0A182PRT9; -.
DR   STRING; 199890.A0A182PRT9; -.
DR   EnsemblMetazoa; AEPI009674-RA; AEPI009674-PA; AEPI009674.
DR   VEuPathDB; VectorBase:AEPI009674; -.
DR   OrthoDB; 1216391at2759; -.
DR   UniPathway; UPA00558; UER00616.
DR   Proteomes; UP000075885; 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, 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..414
FT                   /note="Phosphatidylserine decarboxylase beta chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT                   /id="PRO_5023308038"
FT   CHAIN           415..496
FT                   /note="Phosphatidylserine decarboxylase alpha chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT                   /id="PRO_5023308037"
FT   TOPO_DOM        1..114
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT   TRANSMEM        81..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TOPO_DOM        134..496
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT   REGION          31..72
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        31..45
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        46..60
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        232
FT                   /note="Charge relay system; for autoendoproteolytic
FT                   cleavage activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT   ACT_SITE        303
FT                   /note="Charge relay system; for autoendoproteolytic
FT                   cleavage activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT   ACT_SITE        415
FT                   /note="Charge relay system; for autoendoproteolytic
FT                   cleavage activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT   ACT_SITE        415
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid; for decarboxylase activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT   SITE            414..415
FT                   /note="Cleavage (non-hydrolytic); by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT   MOD_RES         415
FT                   /note="Pyruvic acid (Ser); by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
SQ   SEQUENCE   496 AA;  57166 MW;  1F3038E5E946959D CRC64;
     FSKAVNLKPN PRQWSTRWTI VQRSIYGTRQ LQQQPNSSSS TNHQQHHQQH HQHHQHHQQQ
     QQQFHHQSTT GKSRSKVYRK WSWKAGAGWT ILSVLDWWLL AAGGWLTWRG VFLRWTPIGI
     CMVVAAKWHL HNRELDKKGL PRTAAKWQAK MYCSLPLRLM SRCWGWMADR RVPKPVRPML
     YGLYSSTFGV KMEEAAANNF KEYRSLGEFF TRPLKEDARP IDPKTSFVSP CDGRILHFGA
     ANSNLIEQVK GVSYSLEAFL GPPTWTKKDD PEMVEKVKHN PSPDSVLYQC VIYLAPGDYH
     RFHSPALWKP ELRRHFSGEL LSVSPKIAGW IPGLFCLNER AVYIGKWKHG FFSYTAVGAT
     NVGSVEIFMD EKLKTNKWVG LACGSHKHNE YDELEMPADK YLEKGELVGQ FRMGSTIVLI
     FEAPKDFKFN LFPGQRVKVG ERLGTFESTE ESPEDPEEVK RVIKSLDELE PVSVRKKHRS
     GRTGERARFV CVVSQD
//
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