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Database: UniProt
Entry: C1GHD8_PARBD
LinkDB: C1GHD8_PARBD
Original site: C1GHD8_PARBD 
ID   C1GHD8_PARBD            Unreviewed;       544 AA.
AC   C1GHD8;
DT   26-MAY-2009, integrated into UniProtKB/TrEMBL.
DT   26-MAY-2009, sequence version 1.
DT   24-JAN-2024, entry version 64.
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=PADG_06674 {ECO:0000313|EMBL:EEH50595.1};
OS   Paracoccidioides brasiliensis (strain Pb18).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenales incertae sedis; Paracoccidioides.
OX   NCBI_TaxID=502780 {ECO:0000313|EMBL:EEH50595.1, ECO:0000313|Proteomes:UP000001628};
RN   [1] {ECO:0000313|EMBL:EEH50595.1, ECO:0000313|Proteomes:UP000001628}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Pb18 {ECO:0000313|EMBL:EEH50595.1,
RC   ECO:0000313|Proteomes:UP000001628};
RX   PubMed=22046142; DOI=10.1371/journal.pgen.1002345;
RA   Desjardins C.A., Champion M.D., Holder J.W., Muszewska A., Goldberg J.,
RA   Bailao A.M., Brigido M.M., Ferreira M.E., Garcia A.M., Grynberg M.,
RA   Gujja S., Heiman D.I., Henn M.R., Kodira C.D., Leon-Narvaez H.,
RA   Longo L.V.G., Ma L.-J., Malavazi I., Matsuo A.L., Morais F.V., Pereira M.,
RA   Rodriguez-Brito S., Sakthikumar S., Salem-Izacc S.M., Sykes S.M.,
RA   Teixeira M.M., Vallejo M.C., Walter M.E., Yandava C., Young S., Zeng Q.,
RA   Zucker J., Felipe M.S., Goldman G.H., Haas B.J., McEwen J.G., Nino-Vega G.,
RA   Puccia R., San-Blas G., Soares C.M., Birren B.W., Cuomo C.A.;
RT   "Comparative genomic analysis of human fungal pathogens causing
RT   paracoccidioidomycosis.";
RL   PLoS Genet. 7:E1002345-E1002345(2011).
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}.
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DR   EMBL; KN275965; EEH50595.1; -; Genomic_DNA.
DR   RefSeq; XP_010762191.1; XM_010763889.1.
DR   AlphaFoldDB; C1GHD8; -.
DR   STRING; 502780.C1GHD8; -.
DR   GeneID; 22585345; -.
DR   KEGG; pbn:PADG_06674; -.
DR   VEuPathDB; FungiDB:PADG_06674; -.
DR   eggNOG; KOG2420; Eukaryota.
DR   HOGENOM; CLU_029061_1_1_1; -.
DR   InParanoid; C1GHD8; -.
DR   OMA; RLWGKFN; -.
DR   OrthoDB; 1216391at2759; -.
DR   UniPathway; UPA00558; UER00616.
DR   Proteomes; UP000001628; Unassembled WGS sequence.
DR   GO; GO:0005743; C:mitochondrial inner membrane; IEA:UniProtKB-SubCell.
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-B.
DR   InterPro; IPR033661; PSD_type1_euk.
DR   NCBIfam; TIGR00163; PS_decarb; 1.
DR   PANTHER; PTHR10067; PHOSPHATIDYLSERINE DECARBOXYLASE; 1.
DR   PANTHER; PTHR10067:SF6; PHOSPHATIDYLSERINE DECARBOXYLASE PROENZYME, MITOCHONDRIAL; 1.
DR   Pfam; PF02666; PS_Dcarbxylase; 2.
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:UP000001628};
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..492
FT                   /note="Phosphatidylserine decarboxylase 1 beta chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT                   /id="PRO_5023543368"
FT   CHAIN           493..544
FT                   /note="Phosphatidylserine decarboxylase 1 alpha chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT                   /id="PRO_5023543369"
FT   TOPO_DOM        1..77
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT   TOPO_DOM        97..544
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT   REGION          99..127
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          254..282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          300..324
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        99..123
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        261..282
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        219
FT                   /note="Charge relay system; for autoendoproteolytic
FT                   cleavage activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT   ACT_SITE        365
FT                   /note="Charge relay system; for autoendoproteolytic
FT                   cleavage activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT   ACT_SITE        493
FT                   /note="Charge relay system; for autoendoproteolytic
FT                   cleavage activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT   ACT_SITE        493
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid; for decarboxylase activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT   SITE            492..493
FT                   /note="Cleavage (non-hydrolytic); by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT   MOD_RES         493
FT                   /note="Pyruvic acid (Ser); by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
SQ   SEQUENCE   544 AA;  61429 MW;  630C1CB274B6A82F CRC64;
     MLVGRAFVYR NPAQFLRAWD VVAAEVIPCK PSRRITLPRR QFSSSSRRWQ QDGNGKESFH
     SRLRTALRNT KVEWYPIPVG VGIAFLGFVQ FFRSKNAEKE QEEREEREER ETSEKDGYQE
     VSSRRKVRPS GPWQVQVMST LPLKAMSRLW GRFNELVIPY YLRVPGFKLY SWIFGVNLDE
     IAEPDLHTYP NLASFFYREL KPGVRPLDPN PLSILSPSDG RIFQFGMIEN GEVEQVKGMT
     YSLDALLGHE MMSPSHEAVH PTKSPVHHSE HSSNKDPDNV TADENFAKMN GITYTLPTLL
     SGTGKAPDRD KSMDASMHSS SSSEAKVRAD LAKGQTAWYM PKPTSNRALF YVVIYLAPGD
     YHRFHSPVSW VVESRRHFAG ELFSVSPYLQ RTLPGLFTLN ERIVLLGRWR WGFFSMTPVG
     ATNVGSIKIN FDSELRTNSL TTDTAADRVA AAAAKRGEIY SGFSEATYRH ASKTLAGHAL
     QRGEEMGGFQ LGSSIVLVFE APLGDRPSFD LGWMGEHREG GWKWSIEKGQ YVKYGQPLGA
     VEDV
//
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