ID A0A0C9LUU3_9FUNG Unreviewed; 466 AA.
AC A0A0C9LUU3;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 43.
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=MAM1_0097c05097 {ECO:0000313|EMBL:GAN05625.1};
OS Mucor ambiguus.
OC Eukaryota; Fungi; Fungi incertae sedis; Mucoromycota; Mucoromycotina;
OC Mucoromycetes; Mucorales; Mucorineae; Mucoraceae; Mucor.
OX NCBI_TaxID=91626 {ECO:0000313|EMBL:GAN05625.1};
RN [1] {ECO:0000313|EMBL:GAN05625.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=NBRC 6742 {ECO:0000313|EMBL:GAN05625.1};
RA Takeda I., Yamane N., Morita T., Tamano K., Machida M., Baker S., Koike H.;
RT "Draft genome sequence of an oleaginous Mucoromycotina fungus Mucor
RT ambiguus NBRC6742.";
RL Submitted (SEP-2014) 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}.
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DR EMBL; DF836386; GAN05625.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0C9LUU3; -.
DR STRING; 91626.A0A0C9LUU3; -.
DR OrthoDB; 1216391at2759; -.
DR UniPathway; UPA00558; UER00616.
DR Proteomes; UP000053815; 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:UP000053815};
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..433
FT /note="Phosphatidylserine decarboxylase 1 beta chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT /id="PRO_5023366464"
FT CHAIN 434..466
FT /note="Phosphatidylserine decarboxylase 1 alpha chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT /id="PRO_5023366465"
FT TOPO_DOM 1..59
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT TOPO_DOM 79..466
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT ACT_SITE 184
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT ACT_SITE 321
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT ACT_SITE 434
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT ACT_SITE 434
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid; for decarboxylase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT SITE 433..434
FT /note="Cleavage (non-hydrolytic); by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
FT MOD_RES 434
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03208"
SQ SEQUENCE 466 AA; 52226 MW; 5A359D14C2E48BBC CRC64;
MVIRLLSKPS LSAVRYSTRF APKSKPFHTS AIRQQQQQQQ QQKPLLGRLV DSWNNTETKW
YPIPVALGLG VIGFIQYRRV IQREEDRSEH PKKYVASGPW QVHVAAALPL RSMSRLWGAF
NSLTIPEPLR PLGYKLYSWI FGCNLDEMKN PNLYDYPNLS AFFYRELKEG ARPIADATLV
SPSDGKVLHF GVVKGQDIEQ IKGVTYKLHA LLGNDEESTS PVGNAILGNT PEIVDEEEFA
NVNGIEYSLD DMMSEGHSIK TESAVGPDGL ARSEKNDPQD ERALVKLADV TPDITEHKVK
PGHAMFFCVV YLAPGDYHRF HSPTNWIVQT RRHFAGELFS VSPYFVNLLQ NLFVLNERVA
LLGKWKYGFF SMIPVGATNV GSIKINFDEA LKTNQKEDIP LGTYTEVTYK SASKILGGKA
LRYGDEMGGF YLGSTVVLVF EAPQSFEFKI TAGQKVKMGQ VLGQVE
//
