PSD2_CANAL
ID PSD2_CANAL Reviewed; 1070 AA.
AC Q5AK66; A0A1D8PP10;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 10-MAY-2017, sequence version 2.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Phosphatidylserine decarboxylase proenzyme 2 {ECO:0000255|HAMAP-Rule:MF_03209, ECO:0000303|PubMed:20132453};
DE EC=4.1.1.65 {ECO:0000255|HAMAP-Rule:MF_03209};
DE Contains:
DE RecName: Full=Phosphatidylserine decarboxylase 2 beta chain {ECO:0000255|HAMAP-Rule:MF_03209};
DE Contains:
DE RecName: Full=Phosphatidylserine decarboxylase 2 alpha chain {ECO:0000255|HAMAP-Rule:MF_03209};
GN Name=PSD2 {ECO:0000255|HAMAP-Rule:MF_03209, ECO:0000303|PubMed:20132453};
GN OrderedLocusNames=CAALFM_C504680WA; ORFNames=CaO19.3954, orf19.3954;
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:0000250|UniProtKB:P53037, ECO:0000255|HAMAP-Rule:MF_03209,
CC 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_03209};
CC -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03209};
CC Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_03209};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step
CC 2/2. {ECO:0000255|HAMAP-Rule:MF_03209}.
CC -!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit and a
CC small pyruvoyl-containing alpha subunit. Interacts with pstB2. This
CC interaction may be a means to structurally tether the donor membrane
CC (ER) harboring PstB2 to acceptor membranes (Golgi/endosomes) harboring
CC PSD2 during PtdSer transport to the site of PtdEtn synthesis.
CC {ECO:0000255|HAMAP-Rule:MF_03209}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000255|HAMAP-
CC Rule:MF_03209}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_03209}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03209}.
CC Endosome membrane {ECO:0000255|HAMAP-Rule:MF_03209}; Peripheral
CC membrane protein {ECO:0000255|HAMAP-Rule:MF_03209}; Cytoplasmic side
CC {ECO:0000255|HAMAP-Rule:MF_03209}.
CC -!- DOMAIN: The C2 domains have an essential, but non-catalytic function.
CC They may facilitate interaction with PstB2 and are required for lipid
CC transport function. {ECO:0000255|HAMAP-Rule:MF_03209}.
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_03209}.
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 II sub-subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_03209}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP017627; AOW29874.1; -; Genomic_DNA.
DR RefSeq; XP_721863.2; XM_716770.2.
DR AlphaFoldDB; Q5AK66; -.
DR SMR; Q5AK66; -.
DR STRING; 237561.Q5AK66; -.
DR PRIDE; Q5AK66; -.
DR EnsemblFungi; KHC85551; KHC85551; I503_04484.
DR GeneID; 3636515; -.
DR KEGG; cal:CAALFM_C504680WA; -.
DR CGD; CAL0000195449; PSD2.
DR VEuPathDB; FungiDB:C5_04680W_A; -.
DR eggNOG; KOG2419; Eukaryota.
DR HOGENOM; CLU_002661_0_0_1; -.
DR InParanoid; Q5AK66; -.
DR OrthoDB; 707062at2759; -.
DR BRENDA; 4.1.1.65; 1096.
DR UniPathway; UPA00558; UER00616.
DR Proteomes; UP000000559; Chromosome 5.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004609; F:phosphatidylserine decarboxylase activity; IBA:GO_Central.
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:0036170; P:filamentous growth of a population of unicellular organisms in response to starvation; IMP:CGD.
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:0016540; P:protein autoprocessing; IEA:UniProtKB-UniRule.
DR Gene3D; 2.60.40.150; -; 2.
DR HAMAP; MF_00663; PS_decarb_PSD_B_type2; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR003817; PS_Dcarbxylase.
DR InterPro; IPR033177; PSD.
DR InterPro; IPR033179; PSD_type2_pro.
DR PANTHER; PTHR10067; PTHR10067; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF02666; PS_Dcarbxylase; 1.
DR SMART; SM00239; C2; 2.
DR SUPFAM; SSF49562; SSF49562; 2.
DR TIGRFAMs; TIGR00163; PS_decarb; 1.
DR PROSITE; PS50004; C2; 2.
PE 3: Inferred from homology;
KW Calcium; Decarboxylase; Endosome; Golgi apparatus; Lipid biosynthesis;
KW Lipid metabolism; Lyase; Membrane; Metal-binding;
KW Phospholipid biosynthesis; Phospholipid metabolism; Pyruvate;
KW Reference proteome; Repeat; Zymogen.
FT CHAIN 1..1070
FT /note="Phosphatidylserine decarboxylase proenzyme 2"
FT /id="PRO_0000435591"
FT CHAIN 1..955
FT /note="Phosphatidylserine decarboxylase 2 beta chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03209"
FT /id="PRO_0000435592"
FT CHAIN 956..1070
FT /note="Phosphatidylserine decarboxylase 2 alpha chain"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03209"
FT /id="PRO_0000435593"
FT DOMAIN 12..149
FT /note="C2 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT DOMAIN 315..439
FT /note="C2 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 1..23
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 432..468
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 814
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03209"
FT ACT_SITE 869
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03209"
FT ACT_SITE 956
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03209"
FT ACT_SITE 956
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid; for decarboxylase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03209"
FT BINDING 408
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 411
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 414
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT SITE 955..956
FT /note="Cleavage (non-hydrolytic); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03209"
FT MOD_RES 956
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03209"
SQ SEQUENCE 1070 AA; 121666 MW; 5A1D6E1047EF3C49 CRC64;
MRSSGYLNSN NGSSSSLEST NVNKSTDKNQ LYLKVVCNCA TDLVPQDTTG TGSESKKAYS
SSKSINPVLV VQLNNTIKST SKKLNTNQPS WNDELYMPLK NQDDSSLLIF SVWDKHTRYK
NYLGELRLNV KDIFVDNGNF VDKTELKWYH LNSNTKYHSF VTGSILAGFE LVIKNKKKRF
HSSYNDKFQQ LSIDSDVESA FKKWLSSLTK PTIYSVNNKI NPNDQGFYDD ELVNEFELES
VLTERSKKSH LNVPGGNGLL SVPGDDCHDA GSFSDASFLS DGGYASDASA NLFDQKETSS
DSKKSRIKSK MRLRRSKQEY ENFELASRQV LGVVFIEIVS CEDLPPYKNF TRTSFDMDPF
VVVSFGKKTF RTGWKRHTLN PVFNERLAFE LLPHESNFSI QFLVLDKDHF SFHDNVAHIS
LPLRTLTEYA TAKPTEGDSS DVNTSDSTSF SQTGNGFTTE DTEFPENDSV QIIENETPSN
KQSRKRYLSR KKVVGTQLDL KKFKAMSLSL QLHDQKYIGK YAPKLKIRVR FETYTELRKK
FWRVLLEESN STPENRDSCD YIELISLLDT LGCVNSDELV ELFYSNLGKS SWGGDLLTFD
EIIDQMETYV NQNVESGKVK IFEFEKCPIC NEKRVSKKQD LDIITHFAIC ASKDWSVVGK
LLSSSYVTPT QATKKWFTKA LIKLTYGKYK LGGNSANILV QDRMTGIIVE EKMSVYVRLG
IRLLYKGLDK ARSKRVRILL KNMSIKQGKK FDAPQSKSDI ASFIKFHKLD LDECEIDDPS
QFATFNDFFY RKLKPGAREI EDEKNSKIVT SPADCRSVVF ESIDKATQLW IKGAGFTIPK
LIHNDHSMRV SSYTLGIFRL APQDYHRFHS PVDGVIESIK HIDGEYYTVN PMAIRSELDV
FGENVRTIVT IKTKDFGNIY FIAVGAMMVG SIVLTKDTGY EISKGEELGY FKFGGSTVLL
LIESDKFKFD TDLVKNSSSG LETLLRVGQS IGHSPDVEEY KRDHISFDKL DKSKQLRLIR
VLTGGDLKDK HKLSNWEATK IDMEDFQEIE DEEVFDKDMP DEDASIKSED
