ID A0A5M9MVJ4_9EURO Unreviewed; 1857 AA. AC A0A5M9MVJ4; DT 26-FEB-2020, integrated into UniProtKB/TrEMBL. DT 26-FEB-2020, sequence version 1. DT 27-NOV-2024, entry version 18. 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=ATNIH1004_007930 {ECO:0000313|EMBL:KAA8646497.1}; OS Aspergillus tanneri. OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes; OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus; OC Aspergillus subgen. Circumdati. OX NCBI_TaxID=1220188 {ECO:0000313|EMBL:KAA8646497.1, ECO:0000313|Proteomes:UP000324241}; RN [1] {ECO:0000313|EMBL:KAA8646497.1, ECO:0000313|Proteomes:UP000324241} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=NIH1004 {ECO:0000313|EMBL:KAA8646497.1, RC ECO:0000313|Proteomes:UP000324241}; RA Mounaud S., Singh I., Joardar V., Pakala S., Pakala S., Venepally P., RA Chung J.K., Losada L., Nierman W.C.; RT "The genome sequence of a newly discovered highly antifungal drug resistant RT Aspergillus species, Aspergillus tanneri NIH 1004."; RL Submitted (AUG-2019) 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}. 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:KAA8646497.1}. 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; QUQM01000007; KAA8646497.1; -; Genomic_DNA. DR VEuPathDB; FungiDB:EYZ11_003009; -. DR OrthoDB; 51217at2759; -. DR UniPathway; UPA00558; UER00616. DR Proteomes; UP000324241; 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:0000444; C:MIS12/MIND type complex; IEA:InterPro. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0004609; F:phosphatidylserine decarboxylase activity; IEA:UniProtKB-UniRule. DR GO; GO:0051301; P:cell division; IEA:InterPro. DR GO; GO:0007059; P:chromosome segregation; IEA:InterPro. 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 FunFam; 1.10.238.10:FF:000445; Phosphatidylserine decarboxylase proenzyme 2; 1. DR FunFam; 2.60.40.150:FF:000198; Phosphatidylserine decarboxylase proenzyme 2; 1. DR FunFam; 2.60.40.150:FF:000261; Phosphatidylserine decarboxylase proenzyme 2; 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; IPR013218; Dsn1/Mis13. 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; PF08202; MIS13; 1. 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|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 Zymogen {ECO:0000256|ARBA:ARBA00023145, ECO:0000256|HAMAP-Rule:MF_03209}. FT CHAIN 1..998 FT /note="Phosphatidylserine decarboxylase 2 beta chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03209" FT /id="PRO_5024518410" FT CHAIN 999..1857 FT /note="Phosphatidylserine decarboxylase 2 alpha chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03209" FT /id="PRO_5024518409" FT DOMAIN 22..139 FT /note="C2" FT /evidence="ECO:0000259|PROSITE:PS50004" FT DOMAIN 237..362 FT /note="C2" FT /evidence="ECO:0000259|PROSITE:PS50004" FT DOMAIN 507..542 FT /note="EF-hand" FT /evidence="ECO:0000259|PROSITE:PS50222" FT REGION 1..35 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 192..226 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 367..457 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1312..1542 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1626..1645 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1667..1716 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1738..1757 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 9..33 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 374..457 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1312..1339 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1340..1374 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1449..1472 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1678..1704 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1740..1757 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 854 FT /note="Charge relay system; for autoendoproteolytic FT cleavage activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03209" FT ACT_SITE 912 FT /note="Charge relay system; for autoendoproteolytic FT cleavage activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03209" FT ACT_SITE 999 FT /note="Charge relay system; for autoendoproteolytic FT cleavage activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03209" FT ACT_SITE 999 FT /note="Schiff-base intermediate with substrate; via pyruvic FT acid; for decarboxylase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03209" FT SITE 998..999 FT /note="Cleavage (non-hydrolytic); by autocatalysis" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03209" FT MOD_RES 999 FT /note="Pyruvic acid (Ser); by autocatalysis" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03209" SQ SEQUENCE 1857 AA; 206855 MW; 341E4C4BFE082EE6 CRC64; MVRLPIPQRL TSHLSTRSNA STPGQSRSTS PMRLPESKPL VLKVSVLRGR NLAPKDRNGR SDPYLIVTLG DARQSTPMIP KTLNPEWNVT FEMPVVGVPL LECICWDHDR FGKDYMGEFD IPLEEIFSPG EVYQQPQWYT LTSKRKTIKK KDSTVSGEIL LQFSLIDTSN PTASPTDTYN KYKNLVCAGE EEDDFPQIPP LGLDGVDRDE ETSDETDDPS KPEVVEKRRR RLRLARLKRK SIAARAYQFS GAGNGVQGIV FMEIVKVTDL PPERNVTRTS FDMDPFVVTS LGRKTLRTPV IRHNLNPVYN EKMVFQVMKH EQSYTIGFTV MDRDKFSGND FVASAGFPLQ TLVQAAPDAD PETGLYKFLD STLDPTGSEH SGSDNTAGIK IDISPSPSHN SLSNMSNKVR SRSSTASISA QSVQSAHSGQ ELSTSSPPAI VTEEGSSDSI SNAPTMTNNG NYVASSLDSD GLQAYRIPLT LKNKERWEDK HSPLLVVKAK YMPYRALRQQ FWRLMLRQYD ADDSGRIDKV ELTTMLDTLG STLKESTIDS FFERFSVENE PCETMDLTFD QAVICLEDTL QALQIANRAG PKNHALTSSA ISQESEDPSS CDEDIETSAA IPPTTAPQAL AVPILASDQL AMDEELEPDD LGDERGEEHV IEIRECPLCH QPRLSKRSDA DIITHIATCA SRDWRQVDNL VMGGFVTSSQ AQRKWYTKVI TKISYGGYKL GANSANILVQ DRITGQINEE RMSVYVRLGI RLLYRGLKSR EMEKKRIRKI LKSMSVKQGK KYDDPASASQ IQDFINFHQL DLSEVLLPLD KFKNFNEFFY RQLKPGARPC SAPNEPRIVV SPADCRSVVF DRMNEATGIW VKGREFSIDR LLGDAYPEDV QRYRNGALGI FRLAPQDYHR FHIPVDGVLG TPKTIGGEYY TVNPMAIRSA LDVYGENVRV LVPIDSVAHG RVMVVCVGAM MVGSTVITRQ GGEKVSRGDE LGYFKFGGST LLLLFEEGTI KFDSDLVGNS KGPLETLIRV GMSVGHSPDI PQFEPDMPKK PESLTSEDIQ AARRRIEGSL APLADGRFRN SQRSLAPHPT RHYQNNRVLR RLARANPRQP DAGLYALLRK ERFSIPQTVY ESDLIVSSGR CQLRLVVESA PRTLRHVASP PPFFVTGLAD RPSSQLRPRE IRAPTTNSSE RISTAQNSRL VESFLVVLCF GEVKFVKGYL KKRAAGSSQL LEQRGHSSQY HDCCLETSKE KSAKRLFPTF RQLFELLLLL LPTTPPLSLG PDMIVTVLAT TTTKTERRQP LRQIDMVTSQ AQARFVSSSS GKHDRIGTRA STRLSLTSQE KEENASRTKR KSSFDEDVDD FQFTRIKPKK AKPTVDAIPE VPQPLPEKSA PQQSPKRGRP PKKRQEPKPD SSGEVQNTIE SKPKRQTRGA AKAALVEPET QPASATRSTR KGDHVEPVPK EKKRRKGRPS KSNDEPQQQN GFVSPEPPKA GTATIALPIA DTPVMQRNKE MRGQTKSGKG NRRSSLGMRG RRASSLIDSG ASNALPHKEV DTADFYKHIA SDGLPEPRRM RQLLTWCATR ALGEKPSGSS TEDASERLAA RVIQEELLKD FSTNSELSNW FAREEVDSPS VVVKKPNPKN VQNTEKIKEL EEQIQKLQKQ KQALNALLRP PPSPSIKPAS KQLDTAQNGQ SGPPPSQAES NTNKRARSPE PDPIDLSLLE PSQQQLYALI DPNAATRHPD TELQKAQSSW EPNSLSTVTP STISTRLSRI AAGLVPTLDS FAAGVHDIEL YRAMSDSVSS RVLRICAERL DERDARNSLR RLAIEEEEGD HQNISIRQRP REDLGMILGA LSRVERR //