PSD1_CANAL
ID PSD1_CANAL Reviewed; 590 AA.
AC Q5ABC5; A0A1D8PC92;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 26-APR-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Phosphatidylserine decarboxylase proenzyme 1, mitochondrial {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000303|PubMed:20132453};
DE EC=4.1.1.65 {ECO:0000255|HAMAP-Rule:MF_03208};
DE Contains:
DE RecName: Full=Phosphatidylserine decarboxylase 1 beta chain {ECO:0000255|HAMAP-Rule:MF_03208};
DE Contains:
DE RecName: Full=Phosphatidylserine decarboxylase 1 alpha chain {ECO:0000255|HAMAP-Rule:MF_03208};
DE Flags: Precursor;
GN Name=PSD1 {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000303|PubMed:20132453};
GN OrderedLocusNames=CAALFM_C100610WA;
GN ORFNames=CaO19.13466, CaO19.6045, orf19.6045;
OS Candida albicans (strain SC5314 / ATCC MYA-2876) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=237561;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=15123810; DOI=10.1073/pnas.0401648101;
RA Jones T., Federspiel N.A., Chibana H., Dungan J., Kalman S., Magee B.B.,
RA Newport G., Thorstenson Y.R., Agabian N., Magee P.T., Davis R.W.,
RA Scherer S.;
RT "The diploid genome sequence of Candida albicans.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:7329-7334(2004).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=17419877; DOI=10.1186/gb-2007-8-4-r52;
RA van het Hoog M., Rast T.J., Martchenko M., Grindle S., Dignard D.,
RA Hogues H., Cuomo C., Berriman M., Scherer S., Magee B.B., Whiteway M.,
RA Chibana H., Nantel A., Magee P.T.;
RT "Assembly of the Candida albicans genome into sixteen supercontigs aligned
RT on the eight chromosomes.";
RL Genome Biol. 8:RESEARCH52.1-RESEARCH52.12(2007).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=24025428; DOI=10.1186/gb-2013-14-9-r97;
RA Muzzey D., Schwartz K., Weissman J.S., Sherlock G.;
RT "Assembly of a phased diploid Candida albicans genome facilitates allele-
RT specific measurements and provides a simple model for repeat and indel
RT structure.";
RL Genome Biol. 14:RESEARCH97.1-RESEARCH97.14(2013).
RN [4]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=SC5314 / ATCC MYA-2876;
RX PubMed=20132453; DOI=10.1111/j.1365-2958.2009.07018.x;
RA Chen Y.L., Montedonico A.E., Kauffman S., Dunlap J.R., Menn F.M.,
RA Reynolds T.B.;
RT "Phosphatidylserine synthase and phosphatidylserine decarboxylase are
RT essential for cell wall integrity and virulence in Candida albicans.";
RL Mol. Microbiol. 75:1112-1132(2010).
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 (By similarity). Important for virulence (PubMed:20132453).
CC {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:20132453}.
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};
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}.
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}; Single-
CC pass membrane protein {ECO:0000255|HAMAP-Rule:MF_03208}; Intermembrane
CC side {ECO:0000255|HAMAP-Rule:MF_03208}.
CC -!- SUBCELLULAR LOCATION: [Phosphatidylserine decarboxylase 1 alpha chain]:
CC Mitochondrion inner membrane {ECO:0000255|HAMAP-Rule:MF_03208};
CC Peripheral membrane protein {ECO:0000255|HAMAP-Rule:MF_03208};
CC Intermembrane side {ECO:0000255|HAMAP-Rule:MF_03208}. Note=Anchored to
CC the mitochondrial inner membrane through its interaction with the
CC integral membrane beta 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 -!- DISRUPTION PHENOTYPE: A psd1 psd2 double mutant displays diminished
CC phosphatidylethanolamine levels. It exhibits defects in cell wall
CC integrity, mitochondrial function, filamentous growth and is less
CC virulent than the wild-type. {ECO:0000269|PubMed:20132453}.
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; CP017623; AOW25759.1; -; Genomic_DNA.
DR RefSeq; XP_719007.1; XM_713914.1.
DR AlphaFoldDB; Q5ABC5; -.
DR STRING; 237561.Q5ABC5; -.
DR PRIDE; Q5ABC5; -.
DR EnsemblFungi; KHC82852; KHC82852; W5Q_00055.
DR EnsemblFungi; KHC90152; KHC90152; I503_00055.
DR GeneID; 3639382; -.
DR KEGG; cal:CAALFM_C100610WA; -.
DR CGD; CAL0000188438; PSD1.
DR VEuPathDB; FungiDB:C1_00610W_A; -.
DR eggNOG; KOG2420; Eukaryota.
DR HOGENOM; CLU_029061_1_0_1; -.
DR InParanoid; Q5ABC5; -.
DR OMA; RLWGKFN; -.
DR OrthoDB; 1226492at2759; -.
DR BRENDA; 4.1.1.65; 1096.
DR UniPathway; UPA00558; UER00616.
DR PRO; PR:Q5ABC5; -.
DR Proteomes; UP000000559; Chromosome 1.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0042393; F:histone binding; IEA:EnsemblFungi.
DR GO; GO:0004609; F:phosphatidylserine decarboxylase activity; IBA:GO_Central.
DR GO; GO:0036244; P:cellular response to neutral pH; IMP:CGD.
DR GO; GO:0009267; P:cellular response to starvation; IMP:CGD.
DR GO; GO:0030447; P:filamentous growth; IMP:CGD.
DR GO; GO:0036180; P:filamentous growth of a population of unicellular organisms in response to biotic stimulus; IMP:CGD.
DR GO; GO:0036171; P:filamentous growth of a population of unicellular organisms in response to chemical stimulus; IMP:CGD.
DR GO; GO:0036178; P:filamentous growth of a population of unicellular organisms in response to neutral pH; IMP:CGD.
DR GO; GO:0036170; P:filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
DR GO; GO:0006122; P:mitochondrial electron transport, ubiquinol to cytochrome c; IEA:EnsemblFungi.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; IEA:EnsemblFungi.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IMP:CGD.
DR GO; GO:0006659; P:phosphatidylserine biosynthetic process; IMP:CGD.
DR GO; GO:0010636; P:positive regulation of mitochondrial fusion; IEA:EnsemblFungi.
DR GO; GO:0010954; P:positive regulation of protein processing; IEA:EnsemblFungi.
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.
DR InterPro; IPR033661; PSD_type1_euk.
DR PANTHER; PTHR10067; PTHR10067; 1.
DR Pfam; PF02666; PS_Dcarbxylase; 2.
DR TIGRFAMs; TIGR00163; PS_decarb; 1.
PE 3: Inferred from homology;
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..59
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT CHAIN 60..590
FT /note="Phosphatidylserine decarboxylase proenzyme 1,
FT mitochondrial"
FT /id="PRO_0000435588"
FT CHAIN 60..557
FT /note="Phosphatidylserine decarboxylase 1 beta chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT /id="PRO_0000435589"
FT CHAIN 558..590
FT /note="Phosphatidylserine decarboxylase 1 alpha chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT /id="PRO_0000435590"
FT TOPO_DOM 60..140
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT TRANSMEM 141..159
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT TOPO_DOM 160..590
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT ACT_SITE 260
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT ACT_SITE 403
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT ACT_SITE 558
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT ACT_SITE 558
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid; for decarboxylase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT SITE 557..558
FT /note="Cleavage (non-hydrolytic); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT MOD_RES 558
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
SQ SEQUENCE 590 AA; 67506 MW; EC071ACC82198A78 CRC64;
MPLKPISFRW SKTSVRSVPN PFMYGPDNLN KPLSRASQMA ERVHQQTPSS TNYQQRRYFS
YYYYQFPKIP RPKRNMLYYS TWSRNPVTNA SNANKPSKRH MLPFGSFKIS KRSFANANQK
LKTKLKKLKM GKERRRFIRW WTVTSLTIVL GGVYAKIKYE RGDHEENPYK IRPQSWHLYA
YSALPLKTIS RLWGQVNSIN LPVWIRSPSY RVYSAIFGVN LDEMENPDLS SYKNLSEFFY
RDIKPDARPI ADGDLVSPAD GKVLKFGVVE NGEIEQVKGM TYSIDALLGI DTGKLAAPTH
SLNFDYNSDD ETIVKRDEEF AKINGISYSM DDLVGGNSKS TYHMNELTYK DEHDGTAAGE
RASFSKELRV AEELTPNPVE YFRKKNLYFA VIYLAPGDYH HFHSPTSWVT TLRRHFIGEL
FSVAPFFQKT LQGLFVLNER VALLGYWKYG FFSMVPVGAT NVGSIVVNFD KDLKTNDIYE
HEVYSSASSV NESTPLLDQK DYSANDILTI TNSEYEDKKR KKLRKNTVYE ATYTNASRLL
GGYPLSKGQD IGGFKLGSTV VLVFEAPENF KFNLKVGEKV KVGQSLGGFV
