ID A0A167YBF6_9HYPO Unreviewed; 1114 AA. AC A0A167YBF6; DT 06-JUL-2016, integrated into UniProtKB/TrEMBL. DT 06-JUL-2016, sequence version 1. DT 27-SEP-2017, entry version 11. 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 alpha chain {ECO:0000256|HAMAP-Rule:MF_03209}; DE Contains: DE RecName: Full=Phosphatidylserine decarboxylase 2 beta 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 Aschersonia aleyrodis RCEF 2490. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; OC Sordariomycetes; Hypocreomycetidae; Hypocreales; Clavicipitaceae; OC 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 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: Phosphatidyl-L-serine = CC phosphatidylethanolamine + CO(2). {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. 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 interactions with other proteins and CC are 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}. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. {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 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; 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; 1. 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 Complete proteome {ECO:0000313|Proteomes:UP000078544}; 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:UP000078544}; KW Zymogen {ECO:0000256|HAMAP-Rule:MF_03209}. FT DOMAIN 45 126 C2. {ECO:0000259|PROSITE:PS50004}. FT DOMAIN 269 370 C2. {ECO:0000259|PROSITE:PS50004}. FT DOMAIN 516 551 EF-hand. {ECO:0000259|PROSITE:PS50222}. FT CA_BIND 529 540 {ECO:0000256|PROSITE-ProRule:PRU00448}. FT ACT_SITE 863 863 Charge relay system; for FT autoendoproteolytic cleavage activity. FT {ECO:0000256|HAMAP-Rule:MF_03209}. FT ACT_SITE 921 921 Charge relay system; for FT autoendoproteolytic cleavage activity. FT {ECO:0000256|HAMAP-Rule:MF_03209}. FT ACT_SITE 1008 1008 Charge relay system; for FT autoendoproteolytic cleavage activity. FT {ECO:0000256|HAMAP-Rule:MF_03209}. FT ACT_SITE 1008 1008 Schiff-base intermediate with substrate; FT via pyruvic acid; for decarboxylase FT activity. {ECO:0000256|HAMAP-Rule: FT MF_03209}. FT SITE 1007 1008 Cleavage (non-hydrolytic); by FT autocatalysis. {ECO:0000256|HAMAP-Rule: FT MF_03209}. FT MOD_RES 1008 1008 Pyruvic acid (Ser); by autocatalysis. FT {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 //