GenomeNet

Database: UniProt
Entry: A0A1X7R2F5_9SACH
LinkDB: A0A1X7R2F5_9SACH
Original site: A0A1X7R2F5_9SACH 
ID   A0A1X7R2F5_9SACH        Unreviewed;       529 AA.
AC   A0A1X7R2F5;
DT   05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT   05-JUL-2017, sequence version 1.
DT   24-JAN-2024, entry version 27.
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=KASA_0O04037G {ECO:0000313|EMBL:SMN19815.1};
OS   Kazachstania saulgeensis.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Saccharomycetaceae; Kazachstania.
OX   NCBI_TaxID=1789683 {ECO:0000313|EMBL:SMN19815.1, ECO:0000313|Proteomes:UP000196158};
RN   [1] {ECO:0000313|EMBL:SMN19815.1, ECO:0000313|Proteomes:UP000196158}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA   Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL   Submitted (APR-2017) 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_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; FXLY01000004; SMN19815.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1X7R2F5; -.
DR   STRING; 1789683.A0A1X7R2F5; -.
DR   OrthoDB; 1216391at2759; -.
DR   UniPathway; UPA00558; UER00616.
DR   Proteomes; UP000196158; 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, ECO:0000256|SAM:Phobius};
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:UP000196158};
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..496
FT                   /note="Phosphatidylserine decarboxylase 1 beta chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT                   /id="PRO_5023536790"
FT   CHAIN           497..529
FT                   /note="Phosphatidylserine decarboxylase 1 alpha chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT                   /id="PRO_5023536789"
FT   TOPO_DOM        1..83
FT                   /note="Mitochondrial matrix"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT   TRANSMEM        83..100
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TOPO_DOM        103..529
FT                   /note="Mitochondrial intermembrane"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT   ACT_SITE        230
FT                   /note="Charge relay system; for autoendoproteolytic
FT                   cleavage activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT   ACT_SITE        382
FT                   /note="Charge relay system; for autoendoproteolytic
FT                   cleavage activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT   ACT_SITE        497
FT                   /note="Charge relay system; for autoendoproteolytic
FT                   cleavage activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT   ACT_SITE        497
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid; for decarboxylase activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT   SITE            496..497
FT                   /note="Cleavage (non-hydrolytic); by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT   MOD_RES         497
FT                   /note="Pyruvic acid (Ser); by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
SQ   SEQUENCE   529 AA;  59939 MW;  0BE0CBFA6897F08E CRC64;
     MLKIVPMRSA LKQGHTMLKG RIAMVSGIST PMHLRNRTAV LFNRRFSRHF SRNELRKSTP
     SDIVKKAKNA VSTKSDKRLS MKWALLTGVT LVIGTMIIAS RNDRSGKLDV DDDDENDEKK
     LKNRYSSRGH FATYKGIKIF NNNWMFFCYS TLPLNAMSRL WGQVNSLTLP MWLRPIGFNF
     YTSLFGVNLD EMEDPNLYHY ANLSEFFYRT IRPETRPIAE GEGVIASPSD GQVLQIGIIN
     SDTGEIEQVK GLTYSIKEFL GTHDHPMMSK SESNLTLKQN THDGKLAKLL KLNESIDNID
     ANASKNIETR IPDDAPVIKF KDEGDTAVVK GKDISTSKKV KLLNELALNI PRYRSFKTDP
     SQNIQLYFAV IYLSPGDYHH YHAPVDWVCK QRRHFPGDLY SVAPYFQKNM PNLFVLNERV
     ALLGYWRYGF FSMTPVGATN VGSIKLNFDE KLVTNVKRRP HVEPHTCYEA TYKNASSLLG
     GMPLEKGEEM GGFKLGSTVV LCFEAPSDFK FNVKVGDKVK MGQNLGETK
//
DBGET integrated database retrieval system