ID K5X1K0_AGABU Unreviewed; 594 AA. AC K5X1K0; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 23-MAY-2018, entry version 31. DE RecName: Full=Phosphatidylserine decarboxylase proenzyme 1, mitochondrial {ECO:0000256|HAMAP-Rule:MF_03208}; DE EC=4.1.1.65 {ECO:0000256|HAMAP-Rule:MF_03208}; DE Contains: DE RecName: Full=Phosphatidylserine decarboxylase 1 beta chain {ECO:0000256|HAMAP-Rule:MF_03208}; DE Contains: DE RecName: Full=Phosphatidylserine decarboxylase 1 alpha chain {ECO:0000256|HAMAP-Rule:MF_03208}; GN Name=PSD1 {ECO:0000256|HAMAP-Rule:MF_03208}; GN ORFNames=AGABI1DRAFT_108406 {ECO:0000313|EMBL:EKM77018.1}; OS Agaricus bisporus var. burnettii (strain JB137-S8 / ATCC MYA-4627 / OS FGSC 10392) (White button mushroom). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; OC Agaricomycetes; Agaricomycetidae; Agaricales; Agaricaceae; Agaricus. OX NCBI_TaxID=597362 {ECO:0000313|EMBL:EKM77018.1, ECO:0000313|Proteomes:UP000008493}; RN [1] {ECO:0000313|Proteomes:UP000008493} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=JB137-S8 / ATCC MYA-4627 / FGSC 10392 RC {ECO:0000313|Proteomes:UP000008493}; RX PubMed=23045686; DOI=10.1073/pnas.1206847109; RA Morin E., Kohler A., Baker A.R., Foulongne-Oriol M., Lombard V., RA Nagy L.G., Ohm R.A., Patyshakuliyeva A., Brun A., Aerts A.L., RA Bailey A.M., Billette C., Coutinho P.M., Deakin G., Doddapaneni H., RA Floudas D., Grimwood J., Hilden K., Kuees U., LaButti K.M., RA Lapidus A., Lindquist E.A., Lucas S.M., Murat C., Riley R.W., RA Salamov A.A., Schmutz J., Subramanian V., Woesten H.A.B., Xu J., RA Eastwood D.C., Foster G.D., Sonnenberg A.S., Cullen D., de Vries R.P., RA Lundell T., Hibbett D.S., Henrissat B., Burton K.S., Kerrigan R.W., RA Challen M.P., Grigoriev I.V., Martin F.; RT "Genome sequence of the button mushroom Agaricus bisporus reveals RT mechanisms governing adaptation to a humic-rich ecological niche."; RL Proc. Natl. Acad. Sci. U.S.A. 109:17501-17506(2012). 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_03208}. CC -!- CATALYTIC ACTIVITY: Phosphatidyl-L-serine = CC phosphatidylethanolamine + CO(2). {ECO:0000256|HAMAP- CC Rule:MF_03208}. CC -!- COFACTOR: CC Name=pyruvate; Xref=ChEBI:CHEBI:15361; CC Evidence={ECO:0000256|HAMAP-Rule:MF_03208}; CC Note=Binds 1 pyruvoyl group covalently per subunit. CC {ECO:0000256|HAMAP-Rule:MF_03208}; CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine CC biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: CC step 2/2. {ECO:0000256|HAMAP-Rule:MF_03208}. CC -!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit CC and a small pyruvoyl-containing alpha subunit. {ECO:0000256|HAMAP- CC Rule:MF_03208}. CC -!- SUBCELLULAR LOCATION: Phosphatidylserine decarboxylase 1 alpha CC chain: Mitochondrion inner membrane {ECO:0000256|HAMAP- CC Rule:MF_03208}; Peripheral membrane protein {ECO:0000256|HAMAP- CC Rule:MF_03208}; Intermembrane side {ECO:0000256|HAMAP- CC Rule:MF_03208}. Note=Anchored to the mitochondrial inner membrane CC through its interaction with the integral membrane beta chain. CC {ECO:0000256|HAMAP-Rule:MF_03208}. CC -!- SUBCELLULAR LOCATION: Phosphatidylserine decarboxylase 1 beta CC chain: Mitochondrion inner membrane {ECO:0000256|HAMAP- CC Rule:MF_03208}; Single-pass membrane protein {ECO:0000256|HAMAP- CC Rule:MF_03208}; Intermembrane side {ECO:0000256|HAMAP- CC Rule:MF_03208}. 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_03208}. CC -!- SIMILARITY: Belongs to the phosphatidylserine decarboxylase CC family. PSD-B subfamily. Eukaryotic type I sub-subfamily. CC {ECO:0000256|HAMAP-Rule:MF_03208}. 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; JH971398; EKM77018.1; -; Genomic_DNA. DR RefSeq; XP_007332318.1; XM_007332256.1. DR EnsemblFungi; EKM77018; EKM77018; AGABI1DRAFT_108406. DR GeneID; 18822560; -. DR KEGG; abp:AGABI1DRAFT108406; -. DR InParanoid; K5X1K0; -. DR KO; K01613; -. DR OrthoDB; EOG092C3BRF; -. DR UniPathway; UPA00558; UER00616. DR Proteomes; UP000008493; Unassembled WGS sequence. DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IEA:UniProtKB-UniRule. 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 HAMAP; MF_03208; PS_decarb_PSD_B_type1_euk; 1. DR InterPro; IPR003817; PS_Dcarbxylase. DR InterPro; IPR033177; PSD. DR InterPro; IPR033661; PSD_type1_euk. DR PANTHER; PTHR10067; PTHR10067; 2. DR Pfam; PF02666; PS_Dcarbxylase; 2. DR TIGRFAMs; TIGR00163; PS_decarb; 1. PE 3: Inferred from homology; KW Complete proteome {ECO:0000313|Proteomes:UP000008493}; KW Decarboxylase {ECO:0000256|HAMAP-Rule:MF_03208}; KW Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03208}; KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_03208}; KW Lyase {ECO:0000256|HAMAP-Rule:MF_03208}; KW Membrane {ECO:0000256|HAMAP-Rule:MF_03208}; KW Mitochondrion {ECO:0000256|HAMAP-Rule:MF_03208}; KW Mitochondrion inner membrane {ECO:0000256|HAMAP-Rule:MF_03208}; KW Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03208}; KW Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_03208}; KW Pyruvate {ECO:0000256|HAMAP-Rule:MF_03208}; KW Reference proteome {ECO:0000313|Proteomes:UP000008493}; KW Transmembrane {ECO:0000256|HAMAP-Rule:MF_03208}; KW Transmembrane helix {ECO:0000256|HAMAP-Rule:MF_03208}; KW Zymogen {ECO:0000256|HAMAP-Rule:MF_03208}. FT TOPO_DOM 1 101 Mitochondrial matrix. {ECO:0000256|HAMAP- FT Rule:MF_03208}. FT TOPO_DOM 121 594 Mitochondrial intermembrane. FT {ECO:0000256|HAMAP-Rule:MF_03208}. FT ACT_SITE 229 229 Charge relay system; for FT autoendoproteolytic cleavage activity. FT {ECO:0000256|HAMAP-Rule:MF_03208}. FT ACT_SITE 408 408 Charge relay system; for FT autoendoproteolytic cleavage activity. FT {ECO:0000256|HAMAP-Rule:MF_03208}. FT ACT_SITE 537 537 Charge relay system; for FT autoendoproteolytic cleavage activity. FT {ECO:0000256|HAMAP-Rule:MF_03208}. FT ACT_SITE 537 537 Schiff-base intermediate with substrate; FT via pyruvic acid; for decarboxylase FT activity. {ECO:0000256|HAMAP-Rule: FT MF_03208}. FT SITE 536 537 Cleavage (non-hydrolytic); by FT autocatalysis. {ECO:0000256|HAMAP-Rule: FT MF_03208}. FT MOD_RES 537 537 Pyruvic acid (Ser); by autocatalysis. FT {ECO:0000256|HAMAP-Rule:MF_03208}. SQ SEQUENCE 594 AA; 65270 MW; A9DBB2D3EA0420AF CRC64; MYFSRKTILT KGKKPLYAAS RVLNASSASA SNAFSRCWFH STTKTSALLS TVKSRGLRRV YYTTKHGADG ASSSAGSGGP EVAVPLYSKL VKAWTDTPTK WYPLPIAVGA LLLVAIQYRR KSRRMATDVE LDENGQEVIK LTGPWQVHVL GALPLRNMSR LWGYVSSIEL PIWARPYSFK LYALAFGCNL DEIEPSDLRA YASLGDFFYR KLKDGTRPVA NATLVSPADG TVLHFGRVDA NGDPSLGPVR VEQVKGITYS LDALLGVERP DSPKGIVVHF HNPDEELVHH QEFANVNGIE YSLEQLLGSS SSSGTSTPSD EQTPLLNERP KKYGSQMDAS VISPHQDPLR TLQHDTQIAQ EIQTPPSTPP PSSSSPSSSS PSIKSLRPGH SLFFSVIYLA PGDYHRFHSP TAWVVEKRRH FIGELFSVSP YVVKRLKNVF VLNERVALLG RWKYGFFGMV PVGATNVGSI KINFDKELRT NEVYRRHSDS SSSNGKTKRR LPPVGTYSEA VYNLASPLLH GQPLEPAQEM GGFCLGSTIV LVFEAPDEFE FVVGAGEKVK VGQRLGDVKE RLEELGVREL GGLRGGDTSL VFFG //