ID A0A0D2BYN6_9EURO Unreviewed; 1091 AA.
AC A0A0D2BYN6;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 48.
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=PV06_06101 {ECO:0000313|EMBL:KIW42562.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW42562.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW42562.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW42562.1,
RC ECO:0000313|Proteomes:UP000053342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL Submitted (JAN-2015) to the EMBL/GenBank/DDBJ databases.
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: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
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. 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: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-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}.
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DR EMBL; KN847336; KIW42562.1; -; Genomic_DNA.
DR RefSeq; XP_016262778.1; XM_016407174.1.
DR AlphaFoldDB; A0A0D2BYN6; -.
DR STRING; 215243.A0A0D2BYN6; -.
DR GeneID; 27358175; -.
DR VEuPathDB; FungiDB:PV06_06101; -.
DR HOGENOM; CLU_002661_0_0_1; -.
DR OrthoDB; 51217at2759; -.
DR UniPathway; UPA00558; UER00616.
DR Proteomes; UP000053342; 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:0005509; F:calcium ion binding; IEA:InterPro.
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; cd04039; C2_PSD; 1.
DR CDD; cd04024; C2A_Synaptotagmin-like; 1.
DR Gene3D; 2.60.40.150; C2 domain; 2.
DR Gene3D; 1.10.238.10; EF-hand; 1.
DR HAMAP; MF_00663; PS_decarb_PSD_B_type2; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR011992; EF-hand-dom_pair.
DR InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR InterPro; IPR002048; EF_hand_dom.
DR InterPro; IPR003817; PS_Dcarbxylase.
DR InterPro; IPR033177; PSD-B.
DR InterPro; IPR033179; PSD_type2_pro.
DR NCBIfam; TIGR00163; PS_decarb; 1.
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 SUPFAM; SSF47473; EF-hand; 1.
DR PROSITE; PS50004; C2; 2.
DR PROSITE; PS00018; EF_HAND_1; 1.
DR PROSITE; PS50222; EF_HAND_2; 1.
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:UP000053342};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145, ECO:0000256|HAMAP-Rule:MF_03209}.
FT CHAIN 1..1007
FT /note="Phosphatidylserine decarboxylase 2 beta chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT /id="PRO_5023417464"
FT CHAIN 1008..1091
FT /note="Phosphatidylserine decarboxylase 2 alpha chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT /id="PRO_5023417465"
FT DOMAIN 42..157
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 261..386
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 525..560
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 382..401
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 411..491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1045..1091
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..53
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 411..429
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 436..476
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1050..1075
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 863
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT ACT_SITE 921
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT ACT_SITE 1008
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT ACT_SITE 1008
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid; for decarboxylase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT SITE 1007..1008
FT /note="Cleavage (non-hydrolytic); by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT MOD_RES 1008
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
SQ SEQUENCE 1091 AA; 121619 MW; 5903ACE4E2BB062E CRC64;
MVHISLPRSL HNLGKSKDQA SSSSTNNNNN NNNGGQRPEP PRNGSSNYSL TSSDSKPLIL
KVYVVKARNL AAKDRSGTSD PYLVVTLGNS KQSTPSISKN LNPEWKICFD MPLTGVPLLE
CMCWDKDRFG KDYMGEFDIA IEDIFANGKV QQEPKWYKLK SRRVGSKKES TVSGEVLMQF
SIIDSANPSA SPDEIRKKFL AYIGSEEEDD ELSRVSTNVD AGDEDVDDID EDVEESVTET
EAGPKGAIAD KKEKKRRLAR LRRKSIAARA YNFLGADNDV NGVLFTEIVK ITDLPPERNM
TRTSFDMDPF VVTALGRKIL RTKVVRHNLN PVYNEKMVFQ IMKHETGYSL TFTVIDRDKL
SGNDFVASTS FPIQKMIEAA PEEDPETGLY DLPEPPEFSA AMATNQNGKS RFRLPLSRSS
SQSSLSKLAR PNFKRDDSSV SVSSSLSTSI SNESRPPAPT SAPVDSSAST LKVPGTADVA
SPQPPEDPTM KSYVLPLELK NKEQWEAKHR PELYIRGRYL PYKALRQQFW RAMFKQYDAD
DSKRISKIEF TTMLDTLGST LKESTIDGFY TRFATENEET GEVDLSFDQA VMCLEEQLQK
GSDKKTTSEK IKAAIPTTSK PQDDPNIVQS HVLSGEVPAI EQKEIGTAGE EGQLLDDDLE
DMGDSEEHVI EIRECPICHQ PKLNRRTEAD IITHIATCAS SDWRQVNNLV MGGFVTQSQA
QRKWYSKVIT KISYGGYKLG ANSANILVQD RITGQINEER MSVYVRIGIR LLYKALGARE
MEKRRIKKML KSLSIKQGKK YDDPASASQI EGFIDFHRLN MSEVLLSTDQ FKNFNEFFYR
ALKPGARPCS APDRPEVIVS PADCRSVVFN TIDDATKIWV KGRDYSLEKL FGDAYPLEAK
RYKGGSMGIF RLAPQDYHRF HVPVDGTIGT PKTIEGEYYT VNPMAIRSAL DVYGENVRVL
VPIDSVAHGR VMYVCIGAMM VGSTAITRKP GEKVKRAEEL GYFKFGGSTV LLFFEPGKMV
YDDDLIDNSN GALETLVRVG MSIGHSPHVE SHTPDMKKDE SKITAEERAD AKRRIEGSLA
PNNGGEPTPA A
//
