PSD3_SCHPO
ID PSD3_SCHPO Reviewed; 967 AA.
AC O14111;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 18-APR-2012, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Phosphatidylserine decarboxylase proenzyme 3 {ECO:0000303|PubMed:19286980};
DE EC=4.1.1.65 {ECO:0000255|HAMAP-Rule:MF_03209};
DE Contains:
DE RecName: Full=Phosphatidylserine decarboxylase 3 beta chain {ECO:0000305};
DE Contains:
DE RecName: Full=Phosphatidylserine decarboxylase 3 alpha chain {ECO:0000305};
GN Name=psd3 {ECO:0000303|PubMed:19286980};
GN ORFNames=SPAC31G5.15 {ECO:0000312|PomBase:SPAC31G5.15};
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 REVISION OF GENE MODEL.
RX PubMed=21511999; DOI=10.1126/science.1203357;
RA Rhind N., Chen Z., Yassour M., Thompson D.A., Haas B.J., Habib N.,
RA Wapinski I., Roy S., Lin M.F., Heiman D.I., Young S.K., Furuya K., Guo Y.,
RA Pidoux A., Chen H.M., Robbertse B., Goldberg J.M., Aoki K., Bayne E.H.,
RA Berlin A.M., Desjardins C.A., Dobbs E., Dukaj L., Fan L., FitzGerald M.G.,
RA French C., Gujja S., Hansen K., Keifenheim D., Levin J.Z., Mosher R.A.,
RA Mueller C.A., Pfiffner J., Priest M., Russ C., Smialowska A., Swoboda P.,
RA Sykes S.M., Vaughn M., Vengrova S., Yoder R., Zeng Q., Allshire R.,
RA Baulcombe D., Birren B.W., Brown W., Ekwall K., Kellis M., Leatherwood J.,
RA Levin H., Margalit H., Martienssen R., Nieduszynski C.A., Spatafora J.W.,
RA Friedman N., Dalgaard J.Z., Baumann P., Niki H., Regev A., Nusbaum C.;
RT "Comparative functional genomics of the fission yeasts.";
RL Science 332:930-936(2011).
RN [3]
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 [4]
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 psd2, responsible for the
CC majority of phosphatidylethanolamine synthesis (PubMed:19286980).
CC {ECO:0000255|HAMAP-Rule:MF_03209, 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_03209};
CC -!- COFACTOR:
CC Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_03209};
CC Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000255|HAMAP-
CC Rule:MF_03209};
CC -!- COFACTOR:
CC Name=Ca(2+); Xref=ChEBI:CHEBI:29108;
CC Evidence={ECO:0000255|PROSITE-ProRule:PRU00041};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylethanolamine
CC biosynthesis; phosphatidylethanolamine from CDP-diacylglycerol: step
CC 2/2. {ECO:0000255|HAMAP-Rule:MF_03209}.
CC -!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit and a
CC small pyruvoyl-containing alpha subunit. {ECO:0000255|HAMAP-
CC Rule:MF_03209}.
CC -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000255|HAMAP-
CC Rule:MF_03209}; Peripheral membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_03209}; Cytoplasmic side {ECO:0000255|HAMAP-Rule:MF_03209}.
CC Endosome membrane {ECO:0000255|HAMAP-Rule:MF_03209}; Peripheral
CC membrane protein {ECO:0000255|HAMAP-Rule:MF_03209}; Cytoplasmic side
CC {ECO:0000255|HAMAP-Rule:MF_03209}. Cytoplasm
CC {ECO:0000269|PubMed:16823372}. Note=Localizes at the barrier septum.
CC {ECO:0000269|PubMed:16823372}.
CC -!- DOMAIN: The C2 domains have an essential, but non-catalytic function.
CC They may facilitate interactions with other proteins and are required
CC for lipid transport function. {ECO:0000255|HAMAP-Rule:MF_03209}.
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_03209}.
CC -!- SIMILARITY: Belongs to the phosphatidylserine decarboxylase family.
CC PSD-B subfamily. Eukaryotic type II sub-subfamily. {ECO:0000255|HAMAP-
CC Rule:MF_03209}.
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DR EMBL; CU329670; CAB11699.2; -; Genomic_DNA.
DR PIR; T38632; T38632.
DR RefSeq; NP_594016.2; NM_001019442.2.
DR AlphaFoldDB; O14111; -.
DR SMR; O14111; -.
DR BioGRID; 279608; 11.
DR STRING; 4896.SPAC31G5.15.1; -.
DR iPTMnet; O14111; -.
DR MaxQB; O14111; -.
DR PaxDb; O14111; -.
DR PRIDE; O14111; -.
DR EnsemblFungi; SPAC31G5.15.1; SPAC31G5.15.1:pep; SPAC31G5.15.
DR GeneID; 2543178; -.
DR KEGG; spo:SPAC31G5.15; -.
DR PomBase; SPAC31G5.15; psd3.
DR VEuPathDB; FungiDB:SPAC31G5.15; -.
DR eggNOG; KOG2419; Eukaryota.
DR HOGENOM; CLU_002661_0_0_1; -.
DR InParanoid; O14111; -.
DR OMA; NMTRTSF; -.
DR UniPathway; UPA00558; UER00616.
DR PRO; PR:O14111; -.
DR Proteomes; UP000002485; Chromosome I.
DR GO; GO:0032153; C:cell division site; HDA:PomBase.
DR GO; GO:0005829; C:cytosol; HDA:PomBase.
DR GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0000329; C:fungal-type vacuole membrane; ISS:PomBase.
DR GO; GO:0000139; C:Golgi membrane; ISS:PomBase.
DR GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-UniRule.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004609; F:phosphatidylserine decarboxylase activity; IMP:PomBase.
DR GO; GO:0005543; F:phospholipid binding; ISM: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 Gene3D; 2.60.40.150; -; 1.
DR HAMAP; MF_00663; PS_decarb_PSD_B_type2; 1.
DR InterPro; IPR000008; C2_dom.
DR InterPro; IPR035892; C2_domain_sf.
DR InterPro; IPR003817; PS_Dcarbxylase.
DR InterPro; IPR033177; PSD.
DR InterPro; IPR033179; PSD_type2_pro.
DR PANTHER; PTHR10067; PTHR10067; 1.
DR Pfam; PF00168; C2; 1.
DR Pfam; PF02666; PS_Dcarbxylase; 1.
DR SMART; SM00239; C2; 1.
DR SUPFAM; SSF49562; SSF49562; 1.
DR TIGRFAMs; TIGR00163; PS_decarb; 1.
DR PROSITE; PS50004; C2; 1.
PE 3: Inferred from homology;
KW Calcium; Cytoplasm; Decarboxylase; Endosome; Golgi apparatus;
KW Lipid biosynthesis; Lipid metabolism; Lyase; Membrane; Metal-binding;
KW Phospholipid biosynthesis; Phospholipid metabolism; Pyruvate;
KW Reference proteome; Zymogen.
FT CHAIN 1..967
FT /note="Phosphatidylserine decarboxylase proenzyme 3"
FT /id="PRO_0000303954"
FT CHAIN 1..911
FT /note="Phosphatidylserine decarboxylase 3 beta chain"
FT /evidence="ECO:0000305"
FT /id="PRO_0000416837"
FT CHAIN 912..967
FT /note="Phosphatidylserine decarboxylase 3 alpha chain"
FT /evidence="ECO:0000305"
FT /id="PRO_0000416838"
FT DOMAIN 250..373
FT /note="C2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT REGION 217..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 532..566
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 947..967
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..255
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 532..559
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 769
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03209"
FT ACT_SITE 825
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03209"
FT ACT_SITE 912
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03209"
FT ACT_SITE 912
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid; for decarboxylase activity"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03209"
FT BINDING 343
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 346
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT BINDING 349
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00041"
FT SITE 911..912
FT /note="Cleavage (non-hydrolytic); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03209"
FT MOD_RES 912
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_03209"
SQ SEQUENCE 967 AA; 108213 MW; 5B2115FB91FA42BC CRC64;
MPFTKSCRSA NTLRKGIKNG KLILKIIVND IDNVESCLSG DESNDSKKSS ASFYMKLKYG
SYRALADNIL STDENRKEDI AVFDVPLPNG LQIDTFTLCL YRKSKWKKQI VGEAYIGIQA
LLLSTNPDET CKYPVISPPS GRNKENQSPS HQICNLSLKW IIYDPEDADA DSKTLAKAWL
QQIKMNQTSI DPMSNISKSL KELEVDNVES DLEDSSFIAE PDSSIPPSES SVSISTDTGK
ETPPSKSKKS SNQPYVSIGE GNSDLLGFVF LEIISVSNLP PLKNVFRTGF DMDPFVITAF
SKNIFRTKWL RHNLNPVYNE KFLFEVGAFE SNYDLVFKVV DHDKMSLNDS IAVGSFNVQS
IINSSAQVDP ETGLYSFNIE TSSPSQDTSS KAEDSPTVQK IADDFSSAVG KDLRTDIIEQ
IIPLTLCCKH DFSTPRDVKL SFKAMFFPIA ALRQKFWRVM LAQYGDIEDG HIGKLGMYAV
LDTLGSNIPN SMVDDIYTEL SSKNHDDTSD SITVDEAVIC LERLVDLVCH QDQQATQTPQ
SPSSNEESGP GTPTQTSDQY EDSEDSRNFP SKLYLVYLSN CPLCLKFKLS KVNQQKATVH
LATCASHDWK RVDRLMMTSY VSLNQAQRRW FSKAFAKVVY GSSKVGSTSA TTLVQNRQTG
QIQEEKMNAY VRIGIRLLYR GIRNRRIEGS KVKKILRSLT LKQGMKYDSP ISVKEIKPFI
RFFDLNMNEV DMPVGGFKTF NEFFYRKLKP GSRPCAFPDN PDILVSPADS RIVAYECIEK
ATTYWIKGTE FTVERLLGYS NEAQRFVGGS ICISRLAPQD YHRFHSPVNG CIGPITKIEG
QYYTVNPMAI RSYLDVFGEN VRVLIPIDSN EFGKVMLVAV GAMMVGSTVL TVDEGKIVQR
SDELGYFKFG GSTVITLFEP NVTSFDEDLL RNSKTKIETL VKMGERIGQK IDPNKPTDAE
DHSKSDS
