PSD1_YEAST
ID PSD1_YEAST Reviewed; 500 AA.
AC P39006; D6W113;
DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1995, sequence version 1.
DT 03-AUG-2022, entry version 182.
DE RecName: Full=Phosphatidylserine decarboxylase proenzyme 1, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000305|PubMed:8227017};
DE EC=4.1.1.65 {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:6427211, ECO:0000305|PubMed:17976194};
DE Contains:
DE RecName: Full=Phosphatidylserine decarboxylase 1 beta chain {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000305|PubMed:18644857};
DE Contains:
DE RecName: Full=Phosphatidylserine decarboxylase 1 alpha chain {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000305|PubMed:18644857};
DE Flags: Precursor;
GN Name=PSD1 {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000303|PubMed:8227017};
GN OrderedLocusNames=YNL169C {ECO:0000312|SGD:S000005113}; ORFNames=N1692;
OS Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Saccharomycetaceae; Saccharomyces.
OX NCBI_TaxID=559292;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND FUNCTION.
RC STRAIN=ATCC 204510 / AB320;
RX PubMed=8227017; DOI=10.1016/s0021-9258(19)74506-2;
RA Clancey C.J., Chang S.-C., Dowhan W.;
RT "Cloning of a gene (PSD1) encoding phosphatidylserine decarboxylase from
RT Saccharomyces cerevisiae by complementation of an Escherichia coli
RT mutant.";
RL J. Biol. Chem. 268:24580-24590(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, AND PATHWAY.
RX PubMed=8407984; DOI=10.1016/s0021-9258(19)36940-6;
RA Trotter P.J., Pedretti J., Voelker D.R.;
RT "Phosphatidylserine decarboxylase from Saccharomyces cerevisiae. Isolation
RT of mutants, cloning of the gene, and creation of a null allele.";
RL J. Biol. Chem. 268:21416-21424(1993).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=9169873;
RA Philippsen P., Kleine K., Poehlmann R., Duesterhoeft A., Hamberg K.,
RA Hegemann J.H., Obermaier B., Urrestarazu L.A., Aert R., Albermann K.,
RA Altmann R., Andre B., Baladron V., Ballesta J.P.G., Becam A.-M.,
RA Beinhauer J.D., Boskovic J., Buitrago M.J., Bussereau F., Coster F.,
RA Crouzet M., D'Angelo M., Dal Pero F., De Antoni A., del Rey F., Doignon F.,
RA Domdey H., Dubois E., Fiedler T.A., Fleig U., Floeth M., Fritz C.,
RA Gaillardin C., Garcia-Cantalejo J.M., Glansdorff N., Goffeau A.,
RA Gueldener U., Herbert C.J., Heumann K., Heuss-Neitzel D., Hilbert H.,
RA Hinni K., Iraqui Houssaini I., Jacquet M., Jimenez A., Jonniaux J.-L.,
RA Karpfinger-Hartl L., Lanfranchi G., Lepingle A., Levesque H., Lyck R.,
RA Maftahi M., Mallet L., Maurer C.T.C., Messenguy F., Mewes H.-W., Moestl D.,
RA Nasr F., Nicaud J.-M., Niedenthal R.K., Pandolfo D., Pierard A.,
RA Piravandi E., Planta R.J., Pohl T.M., Purnelle B., Rebischung C.,
RA Remacha M.A., Revuelta J.L., Rinke M., Saiz J.E., Sartorello F.,
RA Scherens B., Sen-Gupta M., Soler-Mira A., Urbanus J.H.M., Valle G.,
RA Van Dyck L., Verhasselt P., Vierendeels F., Vissers S., Voet M.,
RA Volckaert G., Wach A., Wambutt R., Wedler H., Zollner A., Hani J.;
RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome XIV and its
RT evolutionary implications.";
RL Nature 387:93-98(1997).
RN [4]
RP GENOME REANNOTATION.
RC STRAIN=ATCC 204508 / S288c;
RX PubMed=24374639; DOI=10.1534/g3.113.008995;
RA Engel S.R., Dietrich F.S., Fisk D.G., Binkley G., Balakrishnan R.,
RA Costanzo M.C., Dwight S.S., Hitz B.C., Karra K., Nash R.S., Weng S.,
RA Wong E.D., Lloyd P., Skrzypek M.S., Miyasato S.R., Simison M., Cherry J.M.;
RT "The reference genome sequence of Saccharomyces cerevisiae: Then and now.";
RL G3 (Bethesda) 4:389-398(2014).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-174.
RC STRAIN=ATCC 96604 / S288c / FY1679;
RX PubMed=8686380;
RX DOI=10.1002/(sici)1097-0061(199602)12:2<169::aid-yea894>3.0.co;2-b;
RA Nasr F., Becam A.-M., Herbert C.J.;
RT "The sequence of 36.8 kb from the left arm of chromosome XIV reveals 24
RT complete open reading frames: 18 correspond to new genes, one of which
RT encodes a protein similar to the human myotonic dystrophy kinase.";
RL Yeast 12:169-175(1996).
RN [6]
RP CATALYTIC ACTIVITY.
RX PubMed=6427211; DOI=10.1016/s0021-9258(20)82136-x;
RA Carson M.A., Emala M., Hogsten P., Waechter C.J.;
RT "Coordinate regulation of phosphatidylserine decarboxylase activity and
RT phospholipid N-methylation in yeast.";
RL J. Biol. Chem. 259:6267-6273(1984).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=3005242; DOI=10.1128/jb.165.3.901-910.1986;
RA Kuchler K., Daum G., Paltauf F.;
RT "Subcellular and submitochondrial localization of phospholipid-synthesizing
RT enzymes in Saccharomyces cerevisiae.";
RL J. Bacteriol. 165:901-910(1986).
RN [8]
RP FUNCTION.
RX PubMed=8530379; DOI=10.1074/jbc.270.50.29836;
RA Achleitner G., Zweytick D., Trotter P.J., Voelker D.R., Daum G.;
RT "Synthesis and intracellular transport of aminoglycerophospholipids in
RT permeabilized cells of the yeast, Saccharomyces cerevisiae.";
RL J. Biol. Chem. 270:29836-29842(1995).
RN [9]
RP FUNCTION.
RX PubMed=11294902; DOI=10.1091/mbc.12.4.997;
RA Birner R., Buergermeister M., Schneiter R., Daum G.;
RT "Roles of phosphatidylethanolamine and of its several biosynthetic pathways
RT in Saccharomyces cerevisiae.";
RL Mol. Biol. Cell 12:997-1007(2001).
RN [10]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=14562095; DOI=10.1038/nature02026;
RA Huh W.-K., Falvo J.V., Gerke L.C., Carroll A.S., Howson R.W.,
RA Weissman J.S., O'Shea E.K.;
RT "Global analysis of protein localization in budding yeast.";
RL Nature 425:686-691(2003).
RN [11]
RP LEVEL OF PROTEIN EXPRESSION [LARGE SCALE ANALYSIS].
RX PubMed=14562106; DOI=10.1038/nature02046;
RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., Dephoure N.,
RA O'Shea E.K., Weissman J.S.;
RT "Global analysis of protein expression in yeast.";
RL Nature 425:737-741(2003).
RN [12]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 76625 / YPH499;
RX PubMed=14576278; DOI=10.1073/pnas.2135385100;
RA Sickmann A., Reinders J., Wagner Y., Joppich C., Zahedi R.P., Meyer H.E.,
RA Schoenfisch B., Perschil I., Chacinska A., Guiard B., Rehling P.,
RA Pfanner N., Meisinger C.;
RT "The proteome of Saccharomyces cerevisiae mitochondria.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:13207-13212(2003).
RN [13]
RP FUNCTION, CATALYTIC ACTIVITY, AND PROTEOLYTIC PROCESSING.
RX PubMed=17976194; DOI=10.1111/j.1742-4658.2007.06138.x;
RA Nebauer R., Schuiki I., Kulterer B., Trajanoski Z., Daum G.;
RT "The phosphatidylethanolamine level of yeast mitochondria is affected by
RT the mitochondrial components Oxa1p and Yme1p.";
RL FEBS J. 274:6180-6190(2007).
RN [14]
RP PROTEOLYTIC PROCESSING, AND MUTAGENESIS OF 461-LEU--SER-463.
RX PubMed=18644857; DOI=10.1128/mcb.00405-08;
RA Gulshan K., Schmidt J.A., Shahi P., Moye-Rowley W.S.;
RT "Evidence for the bifunctional nature of mitochondrial phosphatidylserine
RT decarboxylase: role in Pdr3-dependent retrograde regulation of PDR5
RT expression.";
RL Mol. Cell. Biol. 28:5851-5864(2008).
RN [15]
RP MUTAGENESIS OF SER-463 AND 81-VAL--SER-100, SUBCELLULAR LOCATION, AND
RP TOPOLOGY.
RX PubMed=22984266; DOI=10.1074/jbc.m112.398107;
RA Horvath S.E., Boettinger L., Voegtle F.N., Wiedemann N., Meisinger C.,
RA Becker T., Daum G.;
RT "Processing and topology of the yeast mitochondrial phosphatidylserine
RT decarboxylase 1.";
RL J. Biol. Chem. 287:36744-36755(2012).
RN [16]
RP FUNCTION.
RX PubMed=23045528; DOI=10.1074/jbc.m112.399428;
RA Chan E.Y., McQuibban G.A.;
RT "Phosphatidylserine decarboxylase 1 (Psd1) promotes mitochondrial fusion by
RT regulating the biophysical properties of the mitochondrial membrane and
RT alternative topogenesis of mitochondrial genome maintenance protein 1
RT (Mgm1).";
RL J. Biol. Chem. 287:40131-40139(2012).
RN [17]
RP FUNCTION, CATALYTIC ACTIVITY, AND SUBCELLULAR LOCATION.
RX PubMed=23124206; DOI=10.1074/jbc.m112.390997;
RA Tamura Y., Onguka O., Itoh K., Endo T., Iijima M., Claypool S.M.,
RA Sesaki H.;
RT "Phosphatidylethanolamine biosynthesis in mitochondria: phosphatidylserine
RT (PS) trafficking is independent of a PS decarboxylase and intermembrane
RT space proteins UPS1P and UPS2P.";
RL J. Biol. Chem. 287:43961-43971(2012).
RN [18]
RP FUNCTION, AND MUTAGENESIS OF LEU-461; SER-463 AND THR-464.
RX PubMed=25829489; DOI=10.1074/jbc.m115.641118;
RA Onguka O., Calzada E., Ogunbona O.B., Claypool S.M.;
RT "Phosphatidylserine decarboxylase 1 autocatalysis and function does not
RT require a mitochondrial-specific factor.";
RL J. Biol. Chem. 290:12744-12752(2015).
RN [19]
RP PROTEOLYTIC CLEAVAGE, AND MUTAGENESIS OF ARG-358.
RX PubMed=30858161; DOI=10.26508/lsa.201900353;
RG Care4Rare Canada Consortium;
RA Zhao T., Goedhart C.M., Sam P.N., Sabouny R., Lingrell S., Cornish A.J.,
RA Lamont R.E., Bernier F.P., Sinasac D., Parboosingh J.S., Vance J.E.,
RA Claypool S.M., Innes A.M., Shutt T.E.;
RT "PISD is a mitochondrial disease gene causing skeletal dysplasia,
RT cataracts, and white matter changes.";
RL Life. Sci Alliance 2:0-0(2019).
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 (PubMed:8227017, PubMed:8407984, PubMed:17976194, PubMed:23124206,
CC PubMed:25829489). Phosphatidylethanolamine formed in the mitochondria
CC is exported to other membranes to fullfill their requirements for
CC PtdEtn (PubMed:8530379, PubMed:11294902). Required for normal
CC mitochondrial morphology and proper mitochondrial fusion during yeast
CC mating (PubMed:23045528). {ECO:0000255|HAMAP-Rule:MF_03208,
CC ECO:0000269|PubMed:11294902, ECO:0000269|PubMed:17976194,
CC ECO:0000269|PubMed:23045528, ECO:0000269|PubMed:23124206,
CC ECO:0000269|PubMed:25829489, ECO:0000269|PubMed:8227017,
CC ECO:0000269|PubMed:8407984, ECO:0000269|PubMed:8530379}.
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:23124206,
CC ECO:0000269|PubMed:6427211, ECO:0000305|PubMed:17976194};
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; phosphatidylethanolamine from CDP-diacylglycerol: step
CC 2/2. {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000305|PubMed:8407984}.
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}.
CC -!- SUBCELLULAR LOCATION: [Phosphatidylserine decarboxylase 1 beta chain]:
CC Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208,
CC ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:22984266,
CC ECO:0000269|PubMed:23124206, ECO:0000269|PubMed:3005242}; Single-pass
CC membrane protein {ECO:0000255|HAMAP-Rule:MF_03208,
CC ECO:0000305|PubMed:22984266}; Intermembrane side {ECO:0000255|HAMAP-
CC Rule:MF_03208, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:22984266,
CC ECO:0000269|PubMed:23124206}.
CC -!- SUBCELLULAR LOCATION: [Phosphatidylserine decarboxylase 1 alpha chain]:
CC Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208,
CC ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:22984266,
CC ECO:0000269|PubMed:23124206, ECO:0000269|PubMed:3005242}; Peripheral
CC membrane protein {ECO:0000255|HAMAP-Rule:MF_03208,
CC ECO:0000269|PubMed:22984266}; Intermembrane side {ECO:0000255|HAMAP-
CC Rule:MF_03208, ECO:0000269|PubMed:14562095,
CC ECO:0000269|PubMed:14576278, ECO:0000269|PubMed:22984266,
CC ECO:0000269|PubMed:23124206}. Note=Anchored to the mitochondrial inner
CC membrane through its interaction with the integral membrane beta chain.
CC {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:22984266}.
CC -!- PTM: The precursor is imported via the TOM complex into mitochondria,
CC where the N-terminal presequence is cleaved by the matrix-located
CC proteases MPP (MAS1-MAS2) and OCT1. {ECO:0000269|PubMed:22984266,
CC ECO:0000305|PubMed:17976194}.
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 (PubMed:25829489,
CC PubMed:30858161). The autoendoproteolytic cleavage occurs by a
CC canonical serine protease mechanism, in which the side chain hydroxyl
CC group of the serine supplies its oxygen atom to form the C-terminus of
CC the beta chain, while the remainder of the serine residue undergoes an
CC oxidative deamination to produce ammonia and the pyruvoyl prosthetic
CC group on the alpha chain. During this reaction, the Ser that is part of
CC the protease active site of the proenzyme becomes the pyruvoyl
CC prosthetic group, which constitutes an essential element of the active
CC site of the mature decarboxylase (By similarity). {ECO:0000255|HAMAP-
CC Rule:MF_03208, ECO:0000305|PubMed:18644857,
CC ECO:0000305|PubMed:30858161}.
CC -!- MISCELLANEOUS: Present with 1080 molecules/cell in log phase SD medium.
CC {ECO:0000269|PubMed:14562106}.
CC -!- SIMILARITY: Belongs to the phosphatidylserine decarboxylase family.
CC PSD-B subfamily. Eukaryotic type I sub-subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_03208}.
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DR EMBL; L20973; AAA34918.1; -; Genomic_DNA.
DR EMBL; Z71444; CAA96056.1; -; Genomic_DNA.
DR EMBL; Z71448; CAA96063.1; -; Genomic_DNA.
DR EMBL; X92517; CAA63270.1; -; Genomic_DNA.
DR EMBL; BK006947; DAA10379.1; -; Genomic_DNA.
DR PIR; A48053; A48053.
DR RefSeq; NP_014230.1; NM_001183007.1.
DR AlphaFoldDB; P39006; -.
DR SMR; P39006; -.
DR BioGRID; 35659; 558.
DR DIP; DIP-4599N; -.
DR IntAct; P39006; 6.
DR MINT; P39006; -.
DR STRING; 4932.YNL169C; -.
DR iPTMnet; P39006; -.
DR MaxQB; P39006; -.
DR PaxDb; P39006; -.
DR PRIDE; P39006; -.
DR EnsemblFungi; YNL169C_mRNA; YNL169C; YNL169C.
DR GeneID; 855552; -.
DR KEGG; sce:YNL169C; -.
DR SGD; S000005113; PSD1.
DR VEuPathDB; FungiDB:YNL169C; -.
DR eggNOG; KOG2420; Eukaryota.
DR GeneTree; ENSGT00390000013484; -.
DR HOGENOM; CLU_029061_1_0_1; -.
DR InParanoid; P39006; -.
DR OMA; RLWGKFN; -.
DR BioCyc; YEAST:YNL169C-MON; -.
DR BRENDA; 4.1.1.65; 984.
DR UniPathway; UPA00558; UER00616.
DR PRO; PR:P39006; -.
DR Proteomes; UP000002311; Chromosome XIV.
DR RNAct; P39006; protein.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IDA:SGD.
DR GO; GO:0005739; C:mitochondrion; HDA:SGD.
DR GO; GO:0042393; F:histone binding; IDA:SGD.
DR GO; GO:0004609; F:phosphatidylserine decarboxylase activity; IMP:SGD.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IMP:SGD.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IDA:SGD.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IBA:GO_Central.
DR GO; GO:0010636; P:positive regulation of mitochondrial fusion; IMP:SGD.
DR GO; GO:0010954; P:positive regulation of protein processing; IMP:SGD.
DR GO; GO:0016540; P:protein autoprocessing; IDA:SGD.
DR GO; GO:0009268; P:response to pH; IDA:SGD.
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; Reference proteome; Transit peptide;
KW Transmembrane; Transmembrane helix; Zymogen.
FT TRANSIT 1..44
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT CHAIN 45..500
FT /note="Phosphatidylserine decarboxylase proenzyme 1,
FT mitochondrial"
FT /id="PRO_0000029843"
FT CHAIN 45..462
FT /note="Phosphatidylserine decarboxylase 1 beta chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT /id="PRO_0000029844"
FT CHAIN 463..500
FT /note="Phosphatidylserine decarboxylase 1 alpha chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT /id="PRO_0000029845"
FT TOPO_DOM 45..79
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208,
FT ECO:0000305|PubMed:22984266"
FT TRANSMEM 80..98
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT TOPO_DOM 99..500
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208,
FT ECO:0000305|PubMed:22984266"
FT ACT_SITE 210
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT ACT_SITE 348
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT ACT_SITE 463
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT ACT_SITE 463
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid; for decarboxylase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT SITE 462..463
FT /note="Cleavage (non-hydrolytic); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT MOD_RES 463
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT MUTAGEN 81..100
FT /note="Missing: In PSD1deltaIM; Mislocalizes to the
FT mitochondrial matrix."
FT /evidence="ECO:0000269|PubMed:22984266"
FT MUTAGEN 358
FT /note="R->Q: Changed autocatalytic proteolysis."
FT /evidence="ECO:0000269|PubMed:30858161"
FT MUTAGEN 461..463
FT /note="LGS->AAA: No processing of the proenzyme, complete
FT loss of activity."
FT /evidence="ECO:0000269|PubMed:18644857"
FT MUTAGEN 461
FT /note="L->A: No effect."
FT /evidence="ECO:0000269|PubMed:25829489"
FT MUTAGEN 462
FT /note="G->A: Significantly impairs processing of the
FT proenzyme, retains some activity."
FT /evidence="ECO:0000269|PubMed:25829489"
FT MUTAGEN 463
FT /note="S->A: No processing of the proenzyme, complete loss
FT of activity."
FT /evidence="ECO:0000269|PubMed:22984266,
FT ECO:0000269|PubMed:25829489"
FT MUTAGEN 464
FT /note="T->I: No effect."
FT /evidence="ECO:0000269|PubMed:25829489"
SQ SEQUENCE 500 AA; 56595 MW; D57047C5AD11777A CRC64;
MSIMPVKNAL AQGRTLLMGR MPAVKFSTRM QLRNRTAVLW NRKFSTRLFV QQRRSSGEIV
DRAKAAAANS GRKQVSMKWV VLTSFTIVLG TILLVSRNDS TEEDATEGKK GRRTRKIKIF
NNNWLFFCYS TLPLNAMSRL WGQVNSLTLP IWVRPWGYRL YSFLFGVNLD EMEDPDLTHY
ANLSEFFYRN IKPGTRPVAQ GEDVIASPSD GKILQVGIIN SETGEIEQVK GMTYSIKEFL
GTHSHPLMSK SASSLDLTSD EEKHREFARV NRIQLAGSED TEQPLLNFKN EGDQSVREFK
PSVSKNIHLL SQLSLNYFSN GFSCSEPHDT ELFFAVIYLA PGDYHHFHSP VDWVCKVRRH
FPGDLFSVAP YFQRNFPNLF VLNERVALLG SWKYGFFSMT PVGATNVGSI KLNFDQEFVT
NSKSDKHLEP HTCYQAVYEN ASKILGGMPL VKGEEMGGFE LGSTVVLCFE APTEFKFDVR
VGDKVKMGQK LGIIGKNDLK
