ID K5X1K0_AGABU Unreviewed; 594 AA. AC K5X1K0; DT 09-JAN-2013, integrated into UniProtKB/TrEMBL. DT 09-JAN-2013, sequence version 1. DT 29-SEP-2021, entry version 48. 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 / FGSC OS 10392) (White button mushroom). OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes; OC 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., Nagy L.G., RA Ohm R.A., Patyshakuliyeva A., Brun A., Aerts A.L., Bailey A.M., RA Billette C., Coutinho P.M., Deakin G., Doddapaneni H., Floudas D., RA Grimwood J., Hilden K., Kuees U., LaButti K.M., Lapidus A., Lindquist E.A., RA Lucas S.M., Murat C., Riley R.W., Salamov A.A., Schmutz J., Subramanian V., RA Woesten H.A.B., Xu J., Eastwood D.C., Foster G.D., Sonnenberg A.S., RA Cullen D., de Vries R.P., Lundell T., Hibbett D.S., Henrissat B., RA Burton K.S., Kerrigan R.W., 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 (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_03208}. 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_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. {ECO:0000256|HAMAP- CC Rule:MF_03208}; 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_03208}. CC -!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit and a CC small pyruvoyl-containing alpha subunit. {ECO:0000256|HAMAP- CC Rule:MF_03208}. CC -!- SUBCELLULAR LOCATION: [Phosphatidylserine decarboxylase 1 alpha chain]: CC Mitochondrion inner membrane {ECO:0000256|HAMAP-Rule:MF_03208}; CC Peripheral membrane protein {ECO:0000256|HAMAP-Rule:MF_03208}; CC Intermembrane side {ECO:0000256|HAMAP-Rule:MF_03208}. Note=Anchored to CC the mitochondrial inner membrane through its interaction with the CC integral membrane beta chain. {ECO:0000256|HAMAP-Rule:MF_03208}. CC -!- SUBCELLULAR LOCATION: [Phosphatidylserine decarboxylase 1 beta chain]: CC Mitochondrion inner membrane {ECO:0000256|HAMAP-Rule:MF_03208}; Single- CC pass membrane protein {ECO:0000256|HAMAP-Rule:MF_03208}; Intermembrane CC side {ECO:0000256|HAMAP-Rule:MF_03208}. 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_03208}. CC -!- SIMILARITY: Belongs to the phosphatidylserine decarboxylase family. CC PSD-B subfamily. Eukaryotic type I sub-subfamily. {ECO:0000256|HAMAP- CC 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 STRING; 5341.XP_007332318.1; -. DR EnsemblFungi; EKM77018; EKM77018; AGABI1DRAFT_108406. DR GeneID; 18822560; -. DR KEGG; abp:AGABI1DRAFT108406; -. DR eggNOG; KOG2420; Eukaryota. DR HOGENOM; CLU_029061_1_1_1; -. DR InParanoid; K5X1K0; -. DR OMA; PTKWYPL; -. DR OrthoDB; 1226492at2759; -. 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; 1. DR Pfam; PF02666; PS_Dcarbxylase; 2. DR TIGRFAMs; TIGR00163; PS_decarb; 1. PE 3: Inferred from homology; KW Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP- KW Rule:MF_03208}; Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_03208}; KW Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_03208}; KW Lyase {ECO:0000256|ARBA:ARBA00023239, 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|ARBA:ARBA00022692, ECO:0000256|HAMAP- KW Rule:MF_03208}; KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP- KW Rule:MF_03208}; Zymogen {ECO:0000256|HAMAP-Rule:MF_03208}. FT CHAIN 1..536 FT /note="Phosphatidylserine decarboxylase 1 beta chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208" FT /id="PRO_5023364781" FT CHAIN 537..594 FT /note="Phosphatidylserine decarboxylase 1 alpha chain" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208" FT /id="PRO_5023364780" FT TOPO_DOM 1..101 FT /note="Mitochondrial matrix" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208" FT TOPO_DOM 121..594 FT /note="Mitochondrial intermembrane" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208" FT REGION 308..328 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 362..384 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 308..324 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 229 FT /note="Charge relay system; for autoendoproteolytic FT cleavage activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208" FT ACT_SITE 408 FT /note="Charge relay system; for autoendoproteolytic FT cleavage activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208" FT ACT_SITE 537 FT /note="Charge relay system; for autoendoproteolytic FT cleavage activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208" FT ACT_SITE 537 FT /note="Schiff-base intermediate with substrate; via pyruvic FT acid; for decarboxylase activity" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208" FT SITE 536..537 FT /note="Cleavage (non-hydrolytic); by autocatalysis" FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208" FT MOD_RES 537 FT /note="Pyruvic acid (Ser); by autocatalysis" FT /evidence="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 //