ID A0A167YBF6_9HYPO Unreviewed; 1114 AA. AC A0A167YBF6; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 29-SEP-2021, entry version 30. 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=AAL_06849 {ECO:0000313|EMBL:KZZ91108.1}; OS Moelleriella libera RCEF 2490. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes; OC Hypocreomycetidae; Hypocreales; Clavicipitaceae; Moelleriella. OX NCBI_TaxID=1081109 {ECO:0000313|EMBL:KZZ91108.1, ECO:0000313|Proteomes:UP000078544}; RN [1] {ECO:0000313|EMBL:KZZ91108.1, ECO:0000313|Proteomes:UP000078544} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=RCEF 2490 {ECO:0000313|EMBL:KZZ91108.1, RC ECO:0000313|Proteomes:UP000078544}; RX PubMed=27071652; DOI=10.1093/gbe/evw082; RA Shang Y., Xiao G., Zheng P., Cen K., Zhan S., Wang C.; RT "Divergent and convergent evolution of fungal pathogenicity."; RL Genome Biol. Evol. 8:1374-1387(2016). 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:KZZ91108.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AZGY01000019; KZZ91108.1; -; Genomic_DNA. DR EnsemblFungi; KZZ91108; KZZ91108; AAL_06849. DR OrthoDB; 707062at2759; -. DR UniPathway; UPA00558; UER00616. DR Proteomes; UP000078544; 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 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; 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. DR InterPro; IPR033179; PSD_type2_pro. DR PANTHER; PTHR10067; PTHR10067; 2. DR Pfam; PF00168; C2; 2. DR Pfam; PF02666; PS_Dcarbxylase; 1. DR SMART; SM00239; C2; 2. DR SUPFAM; SSF47473; SSF47473; 1. DR SUPFAM; SSF49562; SSF49562; 2. DR TIGRFAMs; TIGR00163; PS_decarb; 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|PROSITE-ProRule:PRU00448}; 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|HAMAP-Rule:MF_03209}; KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_03209}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, 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:UP000078544}; KW Zymogen {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_5023449068" FT CHAIN 1008..1114 FT /note="Phosphatidylserine decarboxylase 2 alpha chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03209" FT /id="PRO_5023449067" FT DOMAIN 26..145 FT /note="C2" FT /evidence="ECO:0000259|PROSITE:PS50004" FT DOMAIN 265..386 FT /note="C2" FT /evidence="ECO:0000259|PROSITE:PS50004" FT DOMAIN 516..551 FT /note="EF-hand" FT /evidence="ECO:0000259|PROSITE:PS50222" FT CA_BIND 529..540 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00448" FT REGION 1..37 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 197..261 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 385..478 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 614..668 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1078..1114 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..29 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 197..216 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 223..241 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 408..466 FT /note="Polar 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 1114 AA; 124012 MW; 31C917395F7CA3D4 CRC64; MRIKPNRLLS SSSINSVNNH NTSPMRSNKT DYHGGPGTEA ATGLTLKLVI LKARNLAAKD RSGTSDPYLV ITCGDTRIVT HSVPKTLNPE WNAIEQFPIN SVQNLLLDVI CWDKDRFGKD YMGEFDLALE EVFQNERTEI EPRWFPLKSK RPGKKTGKVS GEVQLQFTLF DATHLGAPSR EILGKFHALI SAIPGSTPST TPLLTSSTTK SASSRLSGQD EHFDDDEDGL SEFDDDESED ASKPDTAEKA EKRRRRLRIK GLKKRRRDNP YAFNNSSSDV VGIIFLEISK ITDLPPESNL TRTSFDMDPF VVASLGKKTY RTRRVRHNLN PVYNEKMIFH VQSHEQSYSF SFTVIDHDKY SGNDFIAACS LPIHELVERA PQADPETGLY GLREPPDHVP SAARSRFKKL SVSRSSSTQS LTKLIRPQLS KNPSSTNVSP QGTTAELGQT HSANGSVTSD VQAPNAADNS DAVAEGDDGD FHEYVVPLKM KNLDKWESKH SPKIYLKAKY MPYPALRQQF WRAMLRQYDT DESGQISRVE LTTMLDTLGS TLRESTIDSF FHRFPHKAAD NEDGWDLTMD EAVICLEDQL AGKGKPKTVV DKVKSLVPDL RQLGISNKAP SADEPARPAA SGTSTPAVAE PKTAVDTTDG KGSGEEDSDE NGEREEEHVV EIRECPICHQ PRLNKRSDTD IITHIATCAS QDWRQVNTVL MGGFVTASQA QRKWYSKVIT KISYGGYKLG ANSANILVQD RITGQINEEK MSVYVRLGIR LLYKGLKSRD MENKRIRKML KNLSIKQGKK FDDPASRDEI EKFIAFHGLD MSEVLLPLEE FKNFNEFFYR ALKPEARPCS APDNPKIIVS PADCRSVVFD QISQATQIWV KGREFNLKRL LGDAYPQDAA RYEDGALGIF RLAPQDYHRF HIPVDGILGK PVTIAGEYYT VNPMAIRSSL DVYGENVRVV VPIDSVKHGR VMVICVGAMM VGSTVITRSA GEEVRRAEEL GYFKFGGSTV LLLFEPGKMQ FDDDLADNSS TALETLIRVG MSIGHSPDEG QWTPDMRKSE GDITEADKQE AMRRIQGNFA MEGSAHDSGS DDDGGPKRRM ARAPTMNTFA ASAM //