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Database: UniProt
Entry: M1AV34_SOLTU
LinkDB: M1AV34_SOLTU
Original site: M1AV34_SOLTU 
ID   M1AV34_SOLTU            Unreviewed;       445 AA.
AC   M1AV34;
DT   03-APR-2013, integrated into UniProtKB/TrEMBL.
DT   03-APR-2013, sequence version 1.
DT   24-JAN-2024, entry version 57.
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};
OS   Solanum tuberosum (Potato).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   asterids; lamiids; Solanales; Solanaceae; Solanoideae; Solaneae; Solanum.
OX   NCBI_TaxID=4113 {ECO:0000313|EnsemblPlants:PGSC0003DMT400031012, ECO:0000313|Proteomes:UP000011115};
RN   [1] {ECO:0000313|Proteomes:UP000011115}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. DM1-3 516 R44 {ECO:0000313|Proteomes:UP000011115};
RX   PubMed=21743474; DOI=10.1038/nature10158;
RG   The Potato Genome Sequencing Consortium;
RT   "Genome sequence and analysis of the tuber crop potato.";
RL   Nature 475:189-195(2011).
RN   [2] {ECO:0000313|EnsemblPlants:PGSC0003DMT400031012}
RP   IDENTIFICATION.
RC   STRAIN=DM1-3 516 R44 {ECO:0000313|EnsemblPlants:PGSC0003DMT400031012};
RG   EnsemblPlants;
RL   Submitted (JUN-2015) 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 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   AlphaFoldDB; M1AV34; -.
DR   STRING; 4113.M1AV34; -.
DR   PaxDb; 4113-PGSC0003DMT400031012; -.
DR   EnsemblPlants; PGSC0003DMT400031012; PGSC0003DMT400031012; PGSC0003DMG402011882.
DR   Gramene; PGSC0003DMT400031012; PGSC0003DMT400031012; PGSC0003DMG402011882.
DR   eggNOG; KOG2420; Eukaryota.
DR   HOGENOM; CLU_029061_3_0_1; -.
DR   InParanoid; M1AV34; -.
DR   OMA; RLWGKFN; -.
DR   UniPathway; UPA00558; UER00616.
DR   Proteomes; UP000011115; Unassembled WGS sequence.
DR   ExpressionAtlas; M1AV34; baseline.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
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-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   Reference proteome {ECO:0000313|Proteomes:UP000011115};
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..399
FT                   /note="Phosphatidylserine decarboxylase 1 beta chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT                   /id="PRO_5023474830"
FT   CHAIN           400..445
FT                   /note="Phosphatidylserine decarboxylase 1 alpha chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT                   /id="PRO_5023474831"
FT   TOPO_DOM        1..63
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT   TOPO_DOM        83..445
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT   ACT_SITE        187
FT                   /note="Charge relay system; for autoendoproteolytic
FT                   cleavage activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT   ACT_SITE        288
FT                   /note="Charge relay system; for autoendoproteolytic
FT                   cleavage activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT   ACT_SITE        400
FT                   /note="Charge relay system; for autoendoproteolytic
FT                   cleavage activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT   ACT_SITE        400
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid; for decarboxylase activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT   SITE            399..400
FT                   /note="Cleavage (non-hydrolytic); by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT   MOD_RES         400
FT                   /note="Pyruvic acid (Ser); by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
SQ   SEQUENCE   445 AA;  50098 MW;  03779D971D15543D CRC64;
     MKFRASQRIP CFTYNGRFSH THAQRFHFTT FLRKVQATEA RASLNRGGSS SNSSSQGNTL
     LLPGATVATI VMLGLLHARR LYDDQKIEDA REKGILEFQP DVKATFMRLL PLRSISRFWG
     TLTSVELPMW LRPSVYKGWA RAFHSNLEEV ALPLEEYASL REFFVRRLKE GTRPIDPDPC
     CLISPVDGTV LQFGELKEVG AMIEQVKGFS YSVSSLLGAS SLLPMSVVDD NTNQDGGQEG
     SMDDTNQKSW WRVSLASPKV RDPAPARPMK GLFYCVIYLS PGDYHRIHSP ADWNVFGRRH
     FSGRLFPMNE RATRTIRNLY VENERVVLEG KWQEGFMAMA AVGATNIGSI ELFIEPTLRT
     NRPWKKLLHP EPPEEQVYEP RGTGVLLKKG DELAAFNMGS TVVLVFQAPI LQPSADKSSS
     AEFSFCIKKG DRVHMGEALG RWHDP
//
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