(data stored in ACNUC8465 zone)

SWISSPROT: C5DCY4_LACTC

ID   C5DCY4_LACTC            Unreviewed;       512 AA.
AC   C5DCY4;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   08-MAY-2019, entry version 55.
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:0000256|HAMAP-Rule:MF_03208};
GN   OrderedLocusNames=KLTH0B06798g {ECO:0000313|EMBL:CAR21645.1};
OS   Lachancea thermotolerans (strain ATCC 56472 / CBS 6340 / NRRL Y-8284)
OS   (Yeast) (Kluyveromyces thermotolerans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina;
OC   Saccharomycetes; Saccharomycetales; Saccharomycetaceae; Lachancea.
OX   NCBI_TaxID=559295 {ECO:0000313|EMBL:CAR21645.1, ECO:0000313|Proteomes:UP000002036};
RN   [1] {ECO:0000313|EMBL:CAR21645.1, ECO:0000313|Proteomes:UP000002036}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 56472 / CBS 6340 / NRRL Y-8284
RC   {ECO:0000313|Proteomes:UP000002036};
RX   PubMed=19525356; DOI=10.1101/gr.091546.109;
RG   The Genolevures Consortium;
RA   Souciet J.-L., Dujon B., Gaillardin C., Johnston M., Baret P.V.,
RA   Cliften P., Sherman D.J., Weissenbach J., Westhof E., Wincker P.,
RA   Jubin C., Poulain J., Barbe V., Segurens B., Artiguenave F.,
RA   Anthouard V., Vacherie B., Val M.-E., Fulton R.S., Minx P., Wilson R.,
RA   Durrens P., Jean G., Marck C., Martin T., Nikolski M., Rolland T.,
RA   Seret M.-L., Casaregola S., Despons L., Fairhead C., Fischer G.,
RA   Lafontaine I., Leh V., Lemaire M., de Montigny J., Neuveglise C.,
RA   Thierry A., Blanc-Lenfle I., Bleykasten C., Diffels J., Fritsch E.,
RA   Frangeul L., Goeffon A., Jauniaux N., Kachouri-Lafond R., Payen C.,
RA   Potier S., Pribylova L., Ozanne C., Richard G.-F., Sacerdot C.,
RA   Straub M.-L., Talla E.;
RT   "Comparative genomics of protoploid Saccharomycetaceae.";
RL   Genome Res. 19:1696-1709(2009).
CC   -!- FUNCTION: Catalyzes the formation of phosphatidylethanolamine
CC       (PtdEtn) from phosphatidylserine (PtdSer). Plays a central role in
CC       phospholipid metabolism and in the interorganelle trafficking of
CC       phosphatidylserine. {ECO:0000256|HAMAP-Rule:MF_03208}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=1,2-diacyl-sn-glycero-3-phospho-L-serine + H(+) = a 1,2-
CC         diacyl-sn-glycero-3-phosphoethanolamine + CO2;
CC         Xref=Rhea:RHEA:20828, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC         ChEBI:CHEBI:57262, ChEBI:CHEBI:64612; EC=4.1.1.65;
CC         Evidence={ECO:0000256|HAMAP-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.
CC       {ECO:0000256|HAMAP-Rule:MF_03208};
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC       biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol:
CC       step 2/2. {ECO:0000256|HAMAP-Rule:MF_03208}.
CC   -!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit
CC       and a small pyruvoyl-containing alpha subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_03208}.
CC   -!- SUBCELLULAR LOCATION: Phosphatidylserine decarboxylase 1 alpha
CC       chain: Mitochondrion inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_03208}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_03208}; Intermembrane side {ECO:0000256|HAMAP-
CC       Rule:MF_03208}. Note=Anchored to the mitochondrial inner membrane
CC       through its interaction with the integral membrane beta chain.
CC       {ECO:0000256|HAMAP-Rule:MF_03208}.
CC   -!- SUBCELLULAR LOCATION: Phosphatidylserine decarboxylase 1 beta
CC       chain: Mitochondrion inner membrane {ECO:0000256|HAMAP-
CC       Rule:MF_03208}; Single-pass membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_03208}; Intermembrane side {ECO:0000256|HAMAP-
CC       Rule:MF_03208}.
CC   -!- PTM: Is synthesized initially as an inactive proenzyme. Formation
CC       of the active enzyme involves a self-maturation process in which
CC       the active site pyruvoyl group is generated from an internal
CC       serine residue via an autocatalytic post-translational
CC       modification. Two non-identical subunits are generated from the
CC       proenzyme in this reaction, and the pyruvate is formed at the N-
CC       terminus of the alpha chain, which is derived from the carboxyl
CC       end of the proenzyme. The autoendoproteolytic cleavage occurs by a
CC       canonical serine protease mechanism, in which the side chain
CC       hydroxyl group of the serine supplies its oxygen atom to form the
CC       C-terminus of the beta chain, while the remainder of the serine
CC       residue undergoes an oxidative deamination to produce ammonia and
CC       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
CC       an essential element of the active site of the mature
CC       decarboxylase. {ECO:0000256|HAMAP-Rule:MF_03208}.
CC   -!- SIMILARITY: Belongs to the phosphatidylserine decarboxylase
CC       family. PSD-B subfamily. Eukaryotic type I sub-subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_03208}.
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DR   EMBL; CU928166; CAR21645.1; -; Genomic_DNA.
DR   RefSeq; XP_002552083.1; XM_002552037.1.
DR   STRING; 381046.XP_002552083.1; -.
DR   EnsemblFungi; CAR21645; CAR21645; KLTH0B06798g.
DR   GeneID; 8290922; -.
DR   KEGG; lth:KLTH0B06798g; -.
DR   HOGENOM; HOG000282409; -.
DR   InParanoid; C5DCY4; -.
DR   KO; K01613; -.
DR   OMA; LLGYWKY; -.
DR   OrthoDB; 1226492at2759; -.
DR   UniPathway; UPA00558; UER00616.
DR   Proteomes; UP000002036; Chromosome B.
DR   GO; GO:0031305; C:integral component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
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   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   3: Inferred from homology;
DR   PRODOM; C5DCY4.
DR   SWISS-2DPAGE; C5DCY4.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002036};
KW   Decarboxylase {ECO:0000256|HAMAP-Rule:MF_03208};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03208};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_03208};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_03208};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_03208, ECO:0000256|SAM:Phobius};
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:UP000002036};
KW   Transmembrane {ECO:0000256|HAMAP-Rule:MF_03208,
KW   ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_03208,
KW   ECO:0000256|SAM:Phobius}; Zymogen {ECO:0000256|HAMAP-Rule:MF_03208}.
FT   TOPO_DOM      1     66       Mitochondrial matrix. {ECO:0000256|HAMAP-
FT                                Rule:MF_03208}.
FT   TRANSMEM     62     81       Helical. {ECO:0000256|SAM:Phobius}.
FT   TOPO_DOM     86    512       Mitochondrial intermembrane.
FT                                {ECO:0000256|HAMAP-Rule:MF_03208}.
FT   ACT_SITE    204    204       Charge relay system; for
FT                                autoendoproteolytic cleavage activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_03208}.
FT   ACT_SITE    353    353       Charge relay system; for
FT                                autoendoproteolytic cleavage activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_03208}.
FT   ACT_SITE    468    468       Charge relay system; for
FT                                autoendoproteolytic cleavage activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_03208}.
FT   ACT_SITE    468    468       Schiff-base intermediate with substrate;
FT                                via pyruvic acid; for decarboxylase
FT                                activity. {ECO:0000256|HAMAP-Rule:
FT                                MF_03208}.
FT   SITE        467    468       Cleavage (non-hydrolytic); by
FT                                autocatalysis. {ECO:0000256|HAMAP-Rule:
FT                                MF_03208}.
FT   MOD_RES     468    468       Pyruvic acid (Ser); by autocatalysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_03208}.
SQ   SEQUENCE   512 AA;  57658 MW;  F21FF2CA8DD21403 CRC64;
     MMNVKLGIMK GGTGMKSRLG MYKLGGAAGT RIRNRTASLW NRRFYSSRAN HMLRISGYDR
     QVVVKLVVVT GVTLVLGSLL LNFAEREPEA DEGHEGDEVD ENGARKRGPK IKIFNNNWLF
     FWYSTLPLNA MSRLWGQVNS LTLPVWMRPW SFKLYAAMFG ANLDEMEDPV LEHYQNLSEF
     FYRGIRPETR PVAPGDDVVV CPSDGKVLQL GVIDAHTGDI EQVKGMTYSV REFLGTHAHP
     QMTRSESHDS IKNSATADKD HIEFARINNI PYTFNDMIGE TPGEDSSHLQ KIKYTSEGDK
     SLPDASPSRP KIMKLLSQLS THYISKMSDM KPENNKLFFA VIYLAPGDYH HYHSPVNWVC
     KLRRHFPGEL FSVAPYFQRN FPNLFILNER VALLGHWKYG FFSMTPVGAT NVGSIKLNFD
     KELVTNEKRN RRTKPHTCYE ATYENTSSIL GGVPLVKGEE MGGFMLGSTV VLCFEAPSDF
     NFDIKVGQAV KMGQPLGKTS QTAQESLGDG QE
//

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