PSD2_SCHPO
ID PSD2_SCHPO Reviewed; 516 AA.
AC Q9UTB5;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 121.
DE RecName: Full=Phosphatidylserine decarboxylase proenzyme 2, mitochondrial {ECO:0000303|PubMed:19286980};
DE EC=4.1.1.65 {ECO:0000255|HAMAP-Rule:MF_03208};
DE Contains:
DE RecName: Full=Phosphatidylserine decarboxylase 2 beta chain {ECO:0000305};
DE Contains:
DE RecName: Full=Phosphatidylserine decarboxylase 2 alpha chain {ECO:0000305};
DE Flags: Precursor;
GN Name=psd2 {ECO:0000303|PubMed:19286980};
GN ORFNames=SPAC25B8.03 {ECO:0000312|PomBase:SPAC25B8.03};
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [3]
RP FUNCTION.
RX PubMed=19286980; DOI=10.1128/ec.00029-09;
RA Luo J., Matsuo Y., Gulis G., Hinz H., Patton-Vogt J., Marcus S.;
RT "Phosphatidylethanolamine is required for normal cell morphology and
RT cytokinesis in the fission yeast Schizosaccharomyces pombe.";
RL Eukaryot. Cell 8:790-799(2009).
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 (By similarity). Together with psd1 and psd3, responsible for the
CC majority of phosphatidylethanolamine synthesis (PubMed:19286980).
CC {ECO:0000255|HAMAP-Rule:MF_03208, ECO:0000269|PubMed:19286980}.
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:0000255|HAMAP-
CC Rule:MF_03208};
CC -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03208};
CC Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_03208};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step
CC 2/2. {ECO:0000255|HAMAP-Rule:MF_03208}.
CC -!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit and a
CC small pyruvoyl-containing alpha subunit. {ECO:0000255|HAMAP-
CC Rule:MF_03208}.
CC -!- SUBCELLULAR LOCATION: [Phosphatidylserine decarboxylase 2 beta chain]:
CC Mitochondrion {ECO:0000305|PubMed:16823372}. Mitochondrion inner
CC membrane {ECO:0000255|HAMAP-Rule:MF_03208}; Single-pass membrane
CC protein {ECO:0000255|HAMAP-Rule:MF_03208}; Intermembrane side
CC {ECO:0000255|HAMAP-Rule:MF_03208}. Nucleus envelope
CC {ECO:0000269|PubMed:16823372}.
CC -!- SUBCELLULAR LOCATION: [Phosphatidylserine decarboxylase 2 alpha chain]:
CC Mitochondrion {ECO:0000305|PubMed:16823372}. Mitochondrion inner
CC membrane {ECO:0000255|HAMAP-Rule:MF_03208}; Peripheral membrane protein
CC {ECO:0000255|HAMAP-Rule:MF_03208}; Intermembrane side
CC {ECO:0000255|HAMAP-Rule:MF_03208}. Nucleus envelope
CC {ECO:0000269|PubMed:16823372}. Note=Anchored to the mitochondrial inner
CC membrane through its interaction with the integral membrane beta chain.
CC {ECO:0000255|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:0000255|HAMAP-Rule:MF_03208}.
CC -!- SIMILARITY: Belongs to the phosphatidylserine decarboxylase family.
CC PSD-B subfamily. Eukaryotic type I sub-subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_03208}.
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DR EMBL; CU329670; CAB61769.1; -; Genomic_DNA.
DR PIR; T50190; T50190.
DR RefSeq; NP_594463.1; NM_001019892.2.
DR AlphaFoldDB; Q9UTB5; -.
DR STRING; 4896.SPAC25B8.03.1; -.
DR iPTMnet; Q9UTB5; -.
DR MaxQB; Q9UTB5; -.
DR PaxDb; Q9UTB5; -.
DR PRIDE; Q9UTB5; -.
DR EnsemblFungi; SPAC25B8.03.1; SPAC25B8.03.1:pep; SPAC25B8.03.
DR GeneID; 2541447; -.
DR KEGG; spo:SPAC25B8.03; -.
DR PomBase; SPAC25B8.03; psd2.
DR VEuPathDB; FungiDB:SPAC25B8.03; -.
DR eggNOG; KOG2420; Eukaryota.
DR HOGENOM; CLU_029061_1_1_1; -.
DR InParanoid; Q9UTB5; -.
DR OMA; HNLFVLN; -.
DR PhylomeDB; Q9UTB5; -.
DR UniPathway; UPA00558; UER00616.
DR PRO; PR:Q9UTB5; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0031305; C:integral component of mitochondrial inner membrane; IEA:UniProtKB-UniRule.
DR GO; GO:0005739; C:mitochondrion; HDA:PomBase.
DR GO; GO:0005635; C:nuclear envelope; HDA:PomBase.
DR GO; GO:0004609; F:phosphatidylserine decarboxylase activity; IMP:PomBase.
DR GO; GO:0006656; P:phosphatidylcholine biosynthetic process; ISS:PomBase.
DR GO; GO:0006646; P:phosphatidylethanolamine biosynthetic process; IMP:PomBase.
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; 1.
DR TIGRFAMs; TIGR00163; PS_decarb; 1.
PE 3: Inferred from homology;
KW Decarboxylase; Lipid biosynthesis; Lipid metabolism; Lyase; Membrane;
KW Mitochondrion; Mitochondrion inner membrane; Nucleus;
KW Phospholipid biosynthesis; Phospholipid metabolism; Pyruvate;
KW Reference proteome; Transit peptide; Transmembrane; Transmembrane helix;
KW Zymogen.
FT TRANSIT 1..21
FT /note="Mitochondrion"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT CHAIN 22..516
FT /note="Phosphatidylserine decarboxylase proenzyme 2,
FT mitochondrial"
FT /id="PRO_0000316032"
FT CHAIN 22..487
FT /note="Phosphatidylserine decarboxylase 2 beta chain"
FT /evidence="ECO:0000305"
FT /id="PRO_0000316033"
FT CHAIN 488..516
FT /note="Phosphatidylserine decarboxylase 2 alpha chain"
FT /evidence="ECO:0000305"
FT /id="PRO_0000316034"
FT TOPO_DOM 22..33
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT TRANSMEM 34..52
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT TOPO_DOM 53..516
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT ACT_SITE 159
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT ACT_SITE 373
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT ACT_SITE 488
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT ACT_SITE 488
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid; for decarboxylase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT SITE 487..488
FT /note="Cleavage (non-hydrolytic); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
FT MOD_RES 488
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03208"
SQ SEQUENCE 516 AA; 58464 MW; FFE4579558985FB9 CRC64;
MRPRQRFRRF HPRWSKVNLR GFGGVGALKG VKALNGMNVR VSMRLKWISN RIHRIRRSRR
LGRLSISVRP NGSWQVYLLS SLPLRSLSRV WGQFNRAHLP TFLRTPGFKL YAWVFGCNLS
ELKDPDLTHY RNFQDFFCRE LRPETRPVDP VSPVVSPVDG RIVCQGVVDN NRIQHVKGLS
YSLEALLGGI SSSNPLVVNF EDEITPDLIQ KHEQFAEQHS ISLNSNNRYR KADASAAVVD
EHSDEEALLC AFTDHPHFYL NDSRNSLNYF CPFSAFEDIS NSVRSSCGKR LSPSSNFDLN
NLGGDDDLRS ESSSDFESAP ASILEHEPTN WDDWVQEADV TDIDSLPWHN IRPGNKLFYS
VIYLAPGDYH RFHSPADWVI ESRRHFSGEL FSVSPFLARR LHNLFVLNER VALLGRYEHG
FMSMIPVGAT NVGSIVINCD PTLSTNRLVL RKKSLGTFQE AVYKNASPVL DGMPVSRGEQ
VGGFQLGSTV VLVFEAPADF EFSTYQGQYV RVGEAL
