(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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