ID A0A1C7MRJ9_GRIFR Unreviewed; 803 AA.
AC A0A1C7MRJ9;
DT 30-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 30-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
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};
GN Name=psd1 {ECO:0000313|EMBL:OBZ79493.1};
GN Synonyms=PSD1 {ECO:0000256|HAMAP-Rule:MF_03208};
GN ORFNames=A0H81_00240 {ECO:0000313|EMBL:OBZ79493.1};
OS Grifola frondosa (Maitake) (Polyporus frondosus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Polyporales; Grifolaceae; Grifola.
OX NCBI_TaxID=5627 {ECO:0000313|EMBL:OBZ79493.1, ECO:0000313|Proteomes:UP000092993};
RN [1] {ECO:0000313|EMBL:OBZ79493.1, ECO:0000313|Proteomes:UP000092993}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=9006-11 {ECO:0000313|EMBL:OBZ79493.1,
RC ECO:0000313|Proteomes:UP000092993};
RA Min B., Park H., Kim J.-G., Cho H., Oh Y.-L., Kong W.-S., Choi I.-G.;
RT "Whole genome sequencing of Grifola frondosa 9006-11.";
RL Submitted (MAR-2016) to the EMBL/GenBank/DDBJ databases.
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}.
CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_03208}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:OBZ79493.1}.
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DR EMBL; LUGG01000001; OBZ79493.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C7MRJ9; -.
DR STRING; 5627.A0A1C7MRJ9; -.
DR OrthoDB; 1216391at2759; -.
DR UniPathway; UPA00558; UER00616.
DR Proteomes; UP000092993; 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 CDD; cd16653; RING-like_Rtf2; 1.
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 InterPro; IPR027799; Rtf2_RING-finger.
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; 2.
DR Pfam; PF04641; Rtf2; 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:UP000092993};
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..771
FT /note="Phosphatidylserine decarboxylase 1 beta chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT /id="PRO_5023279832"
FT CHAIN 772..803
FT /note="Phosphatidylserine decarboxylase 1 alpha chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT /id="PRO_5023279833"
FT TOPO_DOM 1..382
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT TOPO_DOM 402..803
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT REGION 1..26
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 216..256
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 582..601
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 9..26
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 216..241
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 582..600
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 508
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT ACT_SITE 673
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
SQ SEQUENCE 803 AA; 88263 MW; 0068E38147ED255D CRC64;
MGNDGGSIPD RRDLVRSKPK AEQADRANQT RARWFFCALS KRPLQEPIVS CALGKLYNKD
SILEFLLDRT AFGDGEEICG HIRSLKDVKT LKLTLNASRM SAASDTATDV AAFVCPLNFK
EMNGSQPFVY LSTCGCVFSQ AGLRAVSGGT TPPNDSAVVD LDGKGKVQVL GDSTKQLDVC
PQCAIKYDRT TDVLVLNPPS ELESKMRIAM ELRRASEPVK TKGKKRKAVA DVGDGDRPLS
KRKVPSPTPS TNPSIAAASR AVANSLAQEE VKRKAGMSDA IKSLYRSKEG TATKETFMTM
GTFTRSLSAS SALQDWIWSA NEAIRSPAIF QACQSPAGGI PDKKPSLYSA PVESYCHAPS
RLLIVYGPER LANAWKETPT NWYPLPIAVG ALLLVVLRYQ HKRAEKEVHV DEHGHEVVRL
KGPWHVHVLG ALPLRNLSRL WGYLNSLELP VWFRPLGIRI YARIFGCDLE EIDPDDLTQY
ASLGEFFYRK LKDGARPTAD SILVSPADGK VIHFGVIKNG LVEQVKGSTY SLDALLGIEH
RNNAPATSVE FVLREGEEVN HRHFAEINGI EYTLSDFLGS STPTSSVSSG TTTPSDTRSE
SHARIYGDQI DASVSPDISL PEVVAHDASV AAEMGIKHSL ERKTSFRSVI GKPGRELFFI
VIYLAPGDYH RFHSPTAWVV EKRRHFVGDL FSVSPWMAKR LANLFVLNER VALLGRWRHG
FFSMVPVGAT NVGSIKVKFD QALRTNVGSR RSTPAGSFTE AVYSAASPIL GGNHSRKLKR
WADFVWEALL SSSSRRQMPL SLL
//
