ID G4U3D6_SERID Unreviewed; 1093 AA.
AC G4U3D6;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 63.
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 ORFNames=PIIN_01767 {ECO:0000313|EMBL:CCA78094.1};
OS Serendipita indica (strain DSM 11827) (Root endophyte fungus)
OS (Piriformospora indica).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Sebacinales; Serendipitaceae; Serendipita.
OX NCBI_TaxID=1109443 {ECO:0000313|EMBL:CCA78094.1, ECO:0000313|Proteomes:UP000007148};
RN [1] {ECO:0000313|EMBL:CCA78094.1, ECO:0000313|Proteomes:UP000007148}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 11827 {ECO:0000313|EMBL:CCA78094.1,
RC ECO:0000313|Proteomes:UP000007148};
RX PubMed=22022265; DOI=10.1371/journal.ppat.1002290;
RA Zuccaro A., Lahrmann U., Guldener U., Langen G., Pfiffi S., Biedenkopf D.,
RA Wong P., Samans B., Grimm C., Basiewicz M., Murat C., Martin F.,
RA Kogel K.H.;
RT "Endophytic Life Strategies Decoded by Genome and Transcriptome Analyses of
RT the Mutualistic Root Symbiont Piriformospora indica.";
RL PLoS Pathog. 7:e1002290-e1002290(2011).
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 {ECO:0000256|HAMAP-Rule:MF_03209}.
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:0000256|HAMAP-
CC 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. {ECO:0000256|HAMAP-
CC Rule:MF_03209};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step
CC 2/2. {ECO:0000256|HAMAP-Rule:MF_03209}.
CC -!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit and a
CC small pyruvoyl-containing alpha subunit. {ECO:0000256|HAMAP-
CC 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-Rule:MF_03209}.
CC Endosome membrane {ECO:0000256|HAMAP-Rule:MF_03209}; Peripheral
CC membrane protein {ECO:0000256|HAMAP-Rule:MF_03209}; Cytoplasmic side
CC {ECO:0000256|HAMAP-Rule:MF_03209}.
CC -!- DOMAIN: The C2 domains have an essential, but non-catalytic function.
CC They may facilitate interactions with other proteins and are required
CC for lipid transport function. {ECO:0000256|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:0000256|HAMAP-Rule:MF_03209}.
CC -!- SIMILARITY: Belongs to the phosphatidylserine decarboxylase family.
CC PSD-B subfamily. Eukaryotic type II sub-subfamily. {ECO:0000256|HAMAP-
CC Rule:MF_03209}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CCA78094.1}.
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DR EMBL; CAFZ01001883; CCA78094.1; -; Genomic_DNA.
DR AlphaFoldDB; G4U3D6; -.
DR STRING; 1109443.G4U3D6; -.
DR eggNOG; KOG2419; Eukaryota.
DR HOGENOM; CLU_002661_2_1_1; -.
DR InParanoid; G4U3D6; -.
DR OMA; TCASRDW; -.
DR OrthoDB; 51217at2759; -.
DR UniPathway; UPA00558; UER00616.
DR Proteomes; UP000007148; Unassembled WGS sequence.
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 CDD; cd00030; C2; 1.
DR CDD; cd04039; C2_PSD; 1.
DR Gene3D; 2.60.40.150; C2 domain; 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; IPR033179; PSD_type2_pro.
DR PANTHER; PTHR10067; PHOSPHATIDYLSERINE DECARBOXYLASE; 1.
DR PANTHER; PTHR10067:SF17; PHOSPHATIDYLSERINE DECARBOXYLASE PROENZYME 2; 1.
DR Pfam; PF00168; C2; 2.
DR Pfam; PF02666; PS_Dcarbxylase; 1.
DR SMART; SM00239; C2; 2.
DR SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR PROSITE; PS50004; C2; 2.
PE 3: Inferred from homology;
KW Calcium {ECO:0000256|ARBA:ARBA00022837};
KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW Rule:MF_03209}; Endosome {ECO:0000256|HAMAP-Rule:MF_03209};
KW Golgi apparatus {ECO:0000256|HAMAP-Rule:MF_03209};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW Rule:MF_03209};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_03209};
KW Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_03209};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_03209};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209,
KW ECO:0000256|HAMAP-Rule:MF_03209};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264, ECO:0000256|HAMAP-
KW Rule:MF_03209};
KW Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000256|HAMAP-Rule:MF_03209};
KW Reference proteome {ECO:0000313|Proteomes:UP000007148};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145, ECO:0000256|HAMAP-Rule:MF_03209}.
FT CHAIN 1..1052
FT /note="Phosphatidylserine decarboxylase 2 beta chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT /id="PRO_5023399972"
FT CHAIN 1053..1093
FT /note="Phosphatidylserine decarboxylase 2 alpha chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT /id="PRO_5023399973"
FT DOMAIN 30..154
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 340..464
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT REGION 205..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 304..351
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 580..608
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..709
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 205..219
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 232..249
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 304..332
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 594..608
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 670..702
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 908
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT ACT_SITE 966
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT ACT_SITE 1053
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT ACT_SITE 1053
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid; for decarboxylase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT SITE 1052..1053
FT /note="Cleavage (non-hydrolytic); by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT MOD_RES 1053
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
SQ SEQUENCE 1093 AA; 120696 MW; 9F546F25FE31D4FB CRC64;
MAPTNSTTKK GIRIGSALKS GASKVIPGKR FARPIATVTT PAPGEQPVFI LKVQIVGCNG
LPGVDRSGKS DPYVTVRLLQ KQFQTPAITA NLDPEFPAAQ STFEFPVFAS LIEALGALEL
IVWDKNIVMK KEYLGEVAIP IGEWFAGTAL TFDDPNNTPI VRPLLSTKAS RPAMGSIRIK
LGLVPVNPQM PDVKQPYQEM VRRSQDAAVT LQSAPPTEGI GTVRSDDGHD LEDDGMTDDE
TEDEFDSDQP SAAEVIQAVA PVGAVSVAPA TPQVAVKAPE IVAPIPEPIS SRPGLLPRLF
STSSRRGLTQ PQQPAEESTS TSAPSSRPST PGKSKRPKFR RGRSDKGSTY NFGGEKDVLG
IVLLEVNKAE DLPKLKNMTR TGWDMDPFVV ISFSKKVFRT RVLRHNLNPV WDEKLLFHVR
RFEANYNIQL TVLDWDKLSG NDLIADTTLN VAELIQAAPK PDPTTGLYAD LQKDTEMMPF
SLTLNVNKEA VGDGSHKPTI SFKAKYQPYD LLRQRFWANY LKQYDTDDTG AFSHLEITAM
LDSLGSTLSR ETLNSWFTRS GRDPVREELT LAEVIQYLEE ETSRPDSQKK KLSGSQDESL
SAAPSGIATP SMLKSLQSEP LNFEKIDFTG EDFRRSPSRE DFPEANPNEP SGNTNVLGSM
PVPAGPQLKN KRNSLPTRAD IPSVVTTEAE TPSRQQSQSD EDDSGSGLED RVERVINVKT
CPLCHRPRLN NKGEMDIITH LAVCASQDWE KVDRITVGNF VTASQAQRKW YTKAIAKLST
GAYSIGANSA NVIVQNRMTG QLEEEKMQGF VRIGIRLLYK GARSRMEGAQ ARRLLKSMSI
KEGVKFNNPE SAKGIRAFIE FHNLNVDEIL DPIDSFPNFN EFFYRKLKPE ARPVSDPDDP
RTIVSSADCR LMAFESVGEA TRIWIKGREF TVGRLLGERY KDEIHKYEGG ALVIFRLAPQ
DYHRFHSPVD GKIGPMTYIS GEYYTVNPQA IRTQLDVYGE NARKIVPIDS PVFGRVFCAC
IGAMMVGTIV TTVNEGEEVK RGQEFGYFAF GGSTIVTIFP KGTAVWDQDL LDNSKAPLET
LVRVGMRIGR KAD
//
