PISD_CRIGR
ID PISD_CRIGR Reviewed; 409 AA.
AC P27465; Q64402;
DT 01-AUG-1992, integrated into UniProtKB/Swiss-Prot.
DT 16-AUG-2004, sequence version 2.
DT 25-MAY-2022, entry version 104.
DE RecName: Full=Phosphatidylserine decarboxylase proenzyme, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03208};
DE EC=4.1.1.65 {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:2007589};
DE Contains:
DE RecName: Full=Phosphatidylserine decarboxylase beta chain {ECO:0000255|HAMAP-Rule:MF_03208};
DE Contains:
DE RecName: Full=Phosphatidylserine decarboxylase alpha chain {ECO:0000255|HAMAP-Rule:MF_03208};
DE Flags: Precursor;
GN Name=Pisd {ECO:0000255|HAMAP-Rule:MF_03208}; Synonyms=PSSC;
OS Cricetulus griseus (Chinese hamster) (Cricetulus barabensis griseus).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea;
OC Cricetidae; Cricetinae; Cricetulus.
OX NCBI_TaxID=10029;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 40-409, FUNCTION, CATALYTIC ACTIVITY, AND
RP PATHWAY.
RX PubMed=2007589; DOI=10.1016/s0021-9258(18)38127-4;
RA Kuge O., Nishijima M., Akamatsu Y.;
RT "A cloned gene encoding phosphatidylserine decarboxylase complements the
RT phosphatidylserine biosynthetic defect of a Chinese hamster ovary cell
RT mutant.";
RL J. Biol. Chem. 266:6370-6376(1991).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-99, SUBCELLULAR LOCATION, MUTAGENESIS OF
RP SER-378, AND SUBUNIT.
RC STRAIN=CHO-K1;
RX PubMed=8870646; DOI=10.1042/bj3190033;
RA Kuge O., Saito K., Kojima M., Akamatsu Y., Nishijima M.;
RT "Post-translational processing of the phosphatidylserine decarboxylase gene
RT product in Chinese hamster ovary cells.";
RL Biochem. J. 319:33-38(1996).
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:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:2007589}.
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:0000255|HAMAP-
CC Rule:MF_03208, ECO:0000269|PubMed:2007589};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:20829;
CC Evidence={ECO:0000305|PubMed:2007589};
CC -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03208};
CC Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_03208};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis. {ECO:0000305|PubMed:2007589}.
CC -!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit and a
CC small pyruvoyl-containing alpha subunit. {ECO:0000255|HAMAP-
CC Rule:MF_03208, ECO:0000305|PubMed:8870646}.
CC -!- SUBCELLULAR LOCATION: [Phosphatidylserine decarboxylase beta chain]:
CC Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208,
CC ECO:0000305|PubMed:8870646}; Single-pass membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03208}; Intermembrane side
CC {ECO:0000255|HAMAP-Rule:MF_03208}.
CC -!- SUBCELLULAR LOCATION: [Phosphatidylserine decarboxylase alpha chain]:
CC Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208,
CC ECO:0000305|PubMed:8870646}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03208}; Intermembrane side
CC {ECO:0000255|HAMAP-Rule:MF_03208}. Note=Anchored to the mitochondrial
CC inner membrane through its interaction with the integral membrane beta
CC chain. {ECO:0000255|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:0000255|HAMAP-Rule:MF_03208}.
CC -!- SIMILARITY: Belongs to the phosphatidylserine decarboxylase family.
CC PSD-B subfamily. Eukaryotic type I sub-subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_03208}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAA56630.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; M62722; AAA37015.1; -; mRNA.
DR EMBL; X80455; CAA56630.1; ALT_INIT; mRNA.
DR PIR; S72438; S72438.
DR RefSeq; XP_003504168.1; XM_003504120.3.
DR RefSeq; XP_007620920.1; XM_007622730.2.
DR AlphaFoldDB; P27465; -.
DR SMR; P27465; -.
DR STRING; 10029.XP_007620919.1; -.
DR PRIDE; P27465; -.
DR Ensembl; ENSCGRT00001031548; ENSCGRP00001027301; ENSCGRG00001024345.
DR GeneID; 100689093; -.
DR KEGG; cge:100689093; -.
DR CTD; 23761; -.
DR eggNOG; KOG2420; Eukaryota.
DR GeneTree; ENSGT00390000013484; -.
DR OrthoDB; 1226492at2759; -.
DR UniPathway; UPA00558; -.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005739; C:mitochondrion; ISS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:Ensembl.
DR GO; GO:0004609; F:phosphatidylserine decarboxylase activity; ISS:UniProtKB.
DR GO; GO:0035694; P:mitochondrial protein catabolic process; ISS:UniProtKB.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; ISS:UniProtKB.
DR GO; GO:0016540; P:protein autoprocessing; IEA:UniProtKB-UniRule.
DR GO; GO:0010821; P:regulation of mitochondrion organization; ISS:UniProtKB.
DR HAMAP; MF_03208; PS_decarb_PSD_B_type1_euk; 1.
DR InterPro; IPR003817; PS_Dcarbxylase.
DR InterPro; IPR033177; PSD.
DR InterPro; IPR033661; PSD_type1_euk.
DR PANTHER; PTHR10067; PTHR10067; 1.
DR Pfam; PF02666; PS_Dcarbxylase; 1.
DR TIGRFAMs; TIGR00163; PS_decarb; 1.
PE 1: Evidence at protein level;
KW Decarboxylase; Lipid biosynthesis; Lipid metabolism; Lyase; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Phospholipid biosynthesis;
KW Phospholipid metabolism; Pyruvate; Transit peptide; Transmembrane;
KW Transmembrane helix; Zymogen.
FT TRANSIT 1..52
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT CHAIN 53..409
FT /note="Phosphatidylserine decarboxylase proenzyme,
FT mitochondrial"
FT /id="PRO_0000435570"
FT CHAIN 53..377
FT /note="Phosphatidylserine decarboxylase beta chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT /id="PRO_0000029833"
FT CHAIN 378..409
FT /note="Phosphatidylserine decarboxylase alpha chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT /id="PRO_0000029834"
FT TOPO_DOM 53..63
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT TRANSMEM 64..82
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT TOPO_DOM 83..409
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT ACT_SITE 191
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT ACT_SITE 267
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT ACT_SITE 378
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT ACT_SITE 378
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid; for decarboxylase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT SITE 377..378
FT /note="Cleavage (non-hydrolytic); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208,
FT ECO:0000305|PubMed:8870646"
FT MOD_RES 378
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT MUTAGEN 378
FT /note="S->A: Blocks the formation of alpha chain."
FT /evidence="ECO:0000269|PubMed:8870646"
SQ SEQUENCE 409 AA; 46758 MW; F034559B714EE6F5 CRC64;
MAASVCRPYV RSLPGVMPWR SSSCHYEYTA MHHFLGSFQK LPFEPFNTGA RKIHTAPVRS
LFLLRPVPIL LATGGGYAGY RQYEKYRDQK LEKLGLEIPP KLASHWEVAL YKSVPTRLLS
RAWGRLNQVE LPYWLRRPVY SLYIWTFGVN MTEAAVEDLH HYRNLSEFFR RKLKPQARPV
CGLHSVISPS DGKILTFGQV KNCEVEQVKG VTYSLESFLG PRTYTEDLSF PPASSRDSFR
NQLVTREGNE LYHCVIYLAP GDYHCFHSPT DWTVSHRRHF PGSLMSVNPG MARWIKELFC
HNERVVLSGD WKHGFFSLTA VGATNVGSIR IYFDQDLHTN SPRYSKGSYN DLSFVTHANK
EGIPMRKGEH LGEFNLGSTI VLIFEAPKDF NFRLKAGQKI RFGEALGSL
