(data stored in SCRATCH zone)

SWISSPROT: C5DCE7_LACTC

ID   C5DCE7_LACTC            Unreviewed;      1048 AA.
AC   C5DCE7;
DT   28-JUL-2009, integrated into UniProtKB/TrEMBL.
DT   28-JUL-2009, sequence version 1.
DT   08-MAY-2019, entry version 62.
DE   RecName: Full=Phosphatidylserine decarboxylase proenzyme 2 {ECO:0000256|HAMAP-Rule:MF_03209};
DE            EC=4.1.1.65 {ECO:0000256|HAMAP-Rule:MF_03209};
DE   Contains:
DE     RecName: Full=Phosphatidylserine decarboxylase 2 beta chain {ECO:0000256|HAMAP-Rule:MF_03209};
DE   Contains:
DE     RecName: Full=Phosphatidylserine decarboxylase 2 alpha chain {ECO:0000256|HAMAP-Rule:MF_03209};
GN   Name=PSD2 {ECO:0000256|HAMAP-Rule:MF_03209};
GN   OrderedLocusNames=KLTH0B02442g {ECO:0000313|EMBL:CAR21458.1};
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:CAR21458.1, ECO:0000313|Proteomes:UP000002036};
RN   [1] {ECO:0000313|EMBL:CAR21458.1, 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_03209}.
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_03209};
CC   -!- COFACTOR:
CC       Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03209};
CC       Note=Binds 1 pyruvoyl group covalently per subunit.
CC       {ECO:0000256|HAMAP-Rule:MF_03209};
CC   -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC       biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol:
CC       step 2/2. {ECO:0000256|HAMAP-Rule:MF_03209}.
CC   -!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit
CC       and a small pyruvoyl-containing alpha subunit. Interacts with
CC       pstB2. This interaction may be a means to structurally tether the
CC       donor membrane (ER) harboring PstB2 to acceptor membranes
CC       (Golgi/endosomes) harboring PSD2 during PtdSer transport to the
CC       site of PtdEtn synthesis. {ECO:0000256|HAMAP-Rule:MF_03209}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000256|HAMAP-
CC       Rule:MF_03209}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_03209}; Cytoplasmic side {ECO:0000256|HAMAP-
CC       Rule:MF_03209}. Endosome membrane {ECO:0000256|HAMAP-
CC       Rule:MF_03209}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_03209}; Cytoplasmic side {ECO:0000256|HAMAP-
CC       Rule:MF_03209}.
CC   -!- DOMAIN: The C2 domains have an essential, but non-catalytic
CC       function. They may facilitate interaction with PstB2 and are
CC       required for lipid transport function. {ECO:0000256|HAMAP-
CC       Rule:MF_03209}.
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_03209}.
CC   -!- SIMILARITY: Belongs to the phosphatidylserine decarboxylase
CC       family. PSD-B subfamily. Eukaryotic type II sub-subfamily.
CC       {ECO:0000256|HAMAP-Rule:MF_03209}.
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DR   EMBL; CU928166; CAR21458.1; -; Genomic_DNA.
DR   RefSeq; XP_002551896.1; XM_002551850.1.
DR   STRING; 381046.XP_002551896.1; -.
DR   EnsemblFungi; CAR21458; CAR21458; KLTH0B02442g.
DR   GeneID; 8290726; -.
DR   KEGG; lth:KLTH0B02442g; -.
DR   HOGENOM; HOG000199289; -.
DR   InParanoid; C5DCE7; -.
DR   KO; K01613; -.
DR   OMA; KTSWRKH; -.
DR   OrthoDB; 707062at2759; -.
DR   UniPathway; UPA00558; UER00616.
DR   Proteomes; UP000002036; Chromosome B.
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: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   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   TIGRFAMs; TIGR00163; PS_decarb; 1.
DR   PROSITE; PS50004; C2; 1.
PE   3: Inferred from homology;
DR   PRODOM; C5DCE7.
DR   SWISS-2DPAGE; C5DCE7.
KW   Complete proteome {ECO:0000313|Proteomes:UP000002036};
KW   Decarboxylase {ECO:0000256|HAMAP-Rule:MF_03209};
KW   Endosome {ECO:0000256|HAMAP-Rule:MF_03209};
KW   Golgi apparatus {ECO:0000256|HAMAP-Rule:MF_03209};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03209};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_03209};
KW   Lyase {ECO:0000256|HAMAP-Rule:MF_03209};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_03209};
KW   Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03209};
KW   Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_03209};
KW   Pyruvate {ECO:0000256|HAMAP-Rule:MF_03209};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002036};
KW   Zymogen {ECO:0000256|HAMAP-Rule:MF_03209}.
FT   DOMAIN      366    469       C2. {ECO:0000259|PROSITE:PS50004}.
FT   ACT_SITE    787    787       Charge relay system; for
FT                                autoendoproteolytic cleavage activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_03209}.
FT   ACT_SITE    844    844       Charge relay system; for
FT                                autoendoproteolytic cleavage activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_03209}.
FT   ACT_SITE    931    931       Charge relay system; for
FT                                autoendoproteolytic cleavage activity.
FT                                {ECO:0000256|HAMAP-Rule:MF_03209}.
FT   ACT_SITE    931    931       Schiff-base intermediate with substrate;
FT                                via pyruvic acid; for decarboxylase
FT                                activity. {ECO:0000256|HAMAP-Rule:
FT                                MF_03209}.
FT   SITE        930    931       Cleavage (non-hydrolytic); by
FT                                autocatalysis. {ECO:0000256|HAMAP-Rule:
FT                                MF_03209}.
FT   MOD_RES     931    931       Pyruvic acid (Ser); by autocatalysis.
FT                                {ECO:0000256|HAMAP-Rule:MF_03209}.
SQ   SEQUENCE   1048 AA;  118650 MW;  4CE408114961DC08 CRC64;
     MGIIRRRSRR ARLTLRVHAI QAHDVTMQNS GCNPVCLVTS NGVFSRTAKL KNTTSPHWDQ
     MLKLKLPERP TSEYLRVVVY DALASTVDES AVDEFHTRSA GLNDLDSSAK YLYLGETQLS
     LRDLFRRKDQ PTSYKFSRDA AWYPLYNKNA LRFEHTDMQN APAAMAVGEI QLALSLSCTK
     GQSLFKAFNS WQSAFSEPRS SSSMSSSISA AAKSGSDGPS SSAAGSGIFD DFDEETNFDL
     ITQDPSMDEL EPTENDLEGL QFIYSKLEDE DGVEDISSSS DELEPGAQLN FTKVATALDE
     YDVAISRSDF DPSSGNSRVS TPPLISEDDL IDEDNASSSD SKESRYVRMI QTRKRRPRRP
     RKGNASAKFE LSKRGHAAGV AYVDIDSIND LPTLKNKFSK KYMMDPFIII TFGRRVFKTS
     WRKHSLNPVY NERLAFEVYE NEMNFSLHFR IIDKDNFSYH NNVAKGDVSL TDLINRQQKS
     EAGEEWVAMH IPLQFNKTID SSISPPILNL KAKFVSYTDL KKHFWEKALD LLTKQETFDV
     IDINLLMEKL GSFSDEEIED FFYFFGKSPW AHDKLSRDEV ISYLQQSKNS SGFKKLKKCP
     LCSGWCKSTR NVVKSKLILE NDLVTHLSIC SSNSEKKKML KASYVSSDFA SKRWFSKFLI
     KLTYGKYALG SNNANILVQD RDTGIVLEEK ISAHVKVGIR IIYNARGTES KKFKTLLRNL
     SIKQGRKFDN PSSVRQIDSF IRFHSLDTSE CEETEYKTFN EFFYRKLKPG SRSPEVENPE
     ILLSPADCRC TVFSNIKASK EIWIKGKTFT ITKLTNSYHP EIYNDASCSI GIFRLAPQDY
     HRFHCPCDGV IGKPQEISGE YYTVNPMAVR TELDVFGENV RVVVPIHSKE FGTILYIAVG
     AMMVGSIILT CKEGETVERG QELGYFKFGG STILLVVPSQ NVMFDTDLLN NSNERIETLV
     KVGMSIGHTP AVKEHKREKR VLYSKEDIDR IKRTISVSDE TVEKADNAPW EYHSLRKLAP
     HHHSAETTVS SDPTETAREL DLLSIFSD
//

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