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Database: UniProt
Entry: A0A0H1B414_9EURO
LinkDB: A0A0H1B414_9EURO
Original site: A0A0H1B414_9EURO 
ID   A0A0H1B414_9EURO        Unreviewed;      1071 AA.
AC   A0A0H1B414;
DT   16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT   16-SEP-2015, sequence version 1.
DT   24-JAN-2024, entry version 42.
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=EMPG_10467 {ECO:0000313|EMBL:KLJ06130.1};
OS   Blastomyces silverae.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Ajellomycetaceae; Blastomyces.
OX   NCBI_TaxID=2060906 {ECO:0000313|EMBL:KLJ06130.1, ECO:0000313|Proteomes:UP000053573};
RN   [1] {ECO:0000313|Proteomes:UP000053573}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=UAMH 139 {ECO:0000313|Proteomes:UP000053573};
RX   PubMed=26439490; DOI=10.1371/journal.pgen.1005493;
RA   Munoz J.F., Gauthier G.M., Desjardins C.A., Gallo J.E., Holder J.,
RA   Sullivan T.D., Marty A.J., Carmen J.C., Chen Z., Ding L., Gujja S.,
RA   Magrini V., Misas E., Mitreva M., Priest M., Saif S., Whiston E.A.,
RA   Young S., Zeng Q., Goldman W.E., Mardis E.R., Taylor J.W., McEwen J.G.,
RA   Clay O.K., Klein B.S., Cuomo C.A.;
RT   "The dynamic genome and transcriptome of the human fungal pathogen
RT   Blastomyces and close relative Emmonsia.";
RL   PLoS Genet. 11:E1005493-E1005493(2015).
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}.
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:KLJ06130.1}.
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DR   EMBL; LDEV01003291; KLJ06130.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0H1B414; -.
DR   STRING; 2060906.A0A0H1B414; -.
DR   OrthoDB; 51217at2759; -.
DR   UniPathway; UPA00558; UER00616.
DR   Proteomes; UP000053573; 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; 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; PS50222; EF_HAND_2; 1.
PE   3: Inferred from homology;
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:UP000053573};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145, ECO:0000256|HAMAP-Rule:MF_03209}.
FT   CHAIN           1..993
FT                   /note="Phosphatidylserine decarboxylase 2 beta chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT                   /id="PRO_5023297801"
FT   CHAIN           994..1071
FT                   /note="Phosphatidylserine decarboxylase 2 alpha chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT                   /id="PRO_5023297800"
FT   DOMAIN          23..140
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          240..362
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          495..530
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   REGION          1..37
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          195..222
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          364..452
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          579..650
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1032..1054
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..31
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        195..212
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        378..445
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        591..621
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        623..650
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1036..1054
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        849
FT                   /note="Charge relay system; for autoendoproteolytic
FT                   cleavage activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT   ACT_SITE        907
FT                   /note="Charge relay system; for autoendoproteolytic
FT                   cleavage activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT   ACT_SITE        994
FT                   /note="Charge relay system; for autoendoproteolytic
FT                   cleavage activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT   ACT_SITE        994
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid; for decarboxylase activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT   SITE            993..994
FT                   /note="Cleavage (non-hydrolytic); by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT   MOD_RES         994
FT                   /note="Pyruvic acid (Ser); by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
SQ   SEQUENCE   1071 AA;  118983 MW;  037F24899A8B9E8E CRC64;
     MVRISLTRRV GSHMSTKSNA MPSSGDLSPA LTPSGPDTKP LILKATVISG RNLAPKDRNG
     LSDPYLVVSL GEARQSTPTI SKTLNPEWNV CFDLPILGVP LLECICWDKD RFGKDYMGEF
     DIPLEDIFSA GTIQPQPQWY TLHSGRKAGK KRGDVSGEIQ MQFTLFDPTN PSAEPPEILQ
     RFKALVSSDD EDEIVPVISP DTDDLEKEDE TTDGTDDPTK PDVVEKRRRK LRLARLKRKS
     IAARAYEFSG SKDGVSGIVF MEIVKILDLP PERNMTRTSF DMDPFVVTSL GKKTLRTRVI
     RHNLNPVFEE KMVFQVMKHE QSYSISFTVI DRDKLSGNDF VASSSFPLQT LALAAPVADL
     ETGLYNLPGP PSESSPTPPA TKSRFRLNLS RSSSATSLTK LTKPTLRTKS SATSLSSQSG
     QEQQSTTPPN VPSETSSQLN LPTSGSMVEE PEVPADEYGL KTYIIPLVLK NKERWEDKHF
     PELHVKAKYM PYPALRQQFW RAMLKQYDAD DSARISKVEL TTMLDTLGST LKESTIDGFF
     KRFATENEPS ETVDLTFDQA VICLEDTLQS LQKKSLGDKM GDHIPLHSGK ESPESANQSS
     SEDNVPGISL TLASNTDPER PAVPTISRDE RSSSGDSEYN LHPDDLGEDG GEEHVVEVRE
     CPICHQPRLG KRSDADIITH IATCVSQDWR QVDNLVMGGF VTSSQAQRKW YSKVITKISY
     GGYKLGANSA NILVQDRITG QINEERMSVY VRLGIRLLYR GLKSREMEKK RIRKMLKSLS
     IKQGKKYDDP ASAAQIVPFI NFHQLDMSEV LLPLNEFKSF NEFFYRALKP GARPCSAPNN
     PKIVVSPADC RSVVYDRMDE ATKIWVKGRE FSVERLLGKA YPEDAKRYKN GALGIFRLAP
     QDYHRFHIPV DGVMGTPKTI EGEYYTVNPM AIRSALDVYG ENVRIIVPID SVEHGRVMVI
     CVGAMMVGST VITAKGGQKV ARGDELGYFK FGGSTLLVLF EPGKVAFDSD LVGNSLGALE
     TLVRVGMSIG HHPDEPQYTP DMRKSEESIT AQDRAEAMRR IEGSLNAPSD E
//
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