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Database: UniProt
Entry: N1QNH3_SPHMS
LinkDB: N1QNH3_SPHMS
Original site: N1QNH3_SPHMS 
ID   N1QNH3_SPHMS            Unreviewed;      1163 AA.
AC   N1QNH3;
DT   26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT   26-JUN-2013, sequence version 1.
DT   24-JAN-2024, entry version 54.
DE   RecName: Full=Phosphatidylserine decarboxylase proenzyme 2 {ECO:0000256|HAMAP-Rule:MF_03209};
DE            EC=4.1.1.65 {ECO:0000256|HAMAP-Rule:MF_03209};
DE   Contains:
DE     RecName: Full=Phosphatidylserine decarboxylase 2 beta chain {ECO:0000256|HAMAP-Rule:MF_03209};
DE   Contains:
DE     RecName: Full=Phosphatidylserine decarboxylase 2 alpha chain {ECO:0000256|HAMAP-Rule:MF_03209};
GN   Name=PSD2 {ECO:0000256|HAMAP-Rule:MF_03209};
GN   ORFNames=SEPMUDRAFT_146718 {ECO:0000313|EMBL:EMF17758.1};
OS   Sphaerulina musiva (strain SO2202) (Poplar stem canker fungus) (Septoria
OS   musiva).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC   Dothideomycetidae; Mycosphaerellales; Mycosphaerellaceae; Sphaerulina.
OX   NCBI_TaxID=692275 {ECO:0000313|EMBL:EMF17758.1, ECO:0000313|Proteomes:UP000016931};
RN   [1] {ECO:0000313|EMBL:EMF17758.1, ECO:0000313|Proteomes:UP000016931}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SO2202 {ECO:0000313|EMBL:EMF17758.1,
RC   ECO:0000313|Proteomes:UP000016931};
RX   PubMed=23236275; DOI=10.1371/journal.ppat.1003037;
RA   Ohm R.A., Feau N., Henrissat B., Schoch C.L., Horwitz B.A., Barry K.W.,
RA   Condon B.J., Copeland A.C., Dhillon B., Glaser F., Hesse C.N., Kosti I.,
RA   LaButti K., Lindquist E.A., Lucas S., Salamov A.A., Bradshaw R.E.,
RA   Ciuffetti L., Hamelin R.C., Kema G.H.J., Lawrence C., Scott J.A.,
RA   Spatafora J.W., Turgeon B.G., de Wit P.J.G.M., Zhong S., Goodwin S.B.,
RA   Grigoriev I.V.;
RT   "Diverse lifestyles and strategies of plant pathogenesis encoded in the
RT   genomes of eighteen Dothideomycetes fungi.";
RL   PLoS Pathog. 8:E1003037-E1003037(2012).
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_03209}.
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_03209};
CC   -!- COFACTOR:
CC       Name=pyruvate; Xref=ChEBI:CHEBI:15361;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_03209};
CC       Note=Binds 1 pyruvoyl group covalently per subunit. {ECO:0000256|HAMAP-
CC       Rule:MF_03209};
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_03209}.
CC   -!- SUBUNIT: Heterodimer of a large membrane-associated beta subunit and a
CC       small pyruvoyl-containing alpha subunit. Interacts with pstB2. This
CC       interaction may be a means to structurally tether the donor membrane
CC       (ER) harboring PstB2 to acceptor membranes (Golgi/endosomes) harboring
CC       PSD2 during PtdSer transport to the site of PtdEtn synthesis.
CC       {ECO:0000256|HAMAP-Rule:MF_03209}.
CC   -!- SUBCELLULAR LOCATION: Golgi apparatus membrane {ECO:0000256|HAMAP-
CC       Rule:MF_03209}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_03209}; Cytoplasmic side {ECO:0000256|HAMAP-Rule:MF_03209}.
CC       Endosome membrane {ECO:0000256|HAMAP-Rule:MF_03209}; Peripheral
CC       membrane protein {ECO:0000256|HAMAP-Rule:MF_03209}; Cytoplasmic side
CC       {ECO:0000256|HAMAP-Rule:MF_03209}.
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:0000256|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:0000256|HAMAP-Rule:MF_03209}.
CC   -!- SIMILARITY: Belongs to the phosphatidylserine decarboxylase family.
CC       PSD-B subfamily. Eukaryotic type II sub-subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_03209}.
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DR   EMBL; KB456260; EMF17758.1; -; Genomic_DNA.
DR   RefSeq; XP_016765879.1; XM_016903818.1.
DR   AlphaFoldDB; N1QNH3; -.
DR   STRING; 692275.N1QNH3; -.
DR   GeneID; 27900955; -.
DR   eggNOG; KOG1032; Eukaryota.
DR   eggNOG; KOG2419; Eukaryota.
DR   HOGENOM; CLU_002661_0_0_1; -.
DR   OMA; FDEKMVF; -.
DR   OrthoDB; 51217at2759; -.
DR   UniPathway; UPA00558; UER00616.
DR   Proteomes; UP000016931; Unassembled WGS sequence.
DR   GO; GO:0010008; C:endosome membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0000139; C:Golgi membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005795; C:Golgi stack; IEA:UniProtKB-UniRule.
DR   GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
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   CDD; cd04039; C2_PSD; 1.
DR   Gene3D; 2.60.40.150; C2 domain; 2.
DR   Gene3D; 1.10.238.10; EF-hand; 1.
DR   HAMAP; MF_00663; PS_decarb_PSD_B_type2; 1.
DR   InterPro; IPR000008; C2_dom.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR011992; EF-hand-dom_pair.
DR   InterPro; IPR018247; EF_Hand_1_Ca_BS.
DR   InterPro; IPR002048; EF_hand_dom.
DR   InterPro; IPR003817; PS_Dcarbxylase.
DR   InterPro; IPR033177; PSD-B.
DR   InterPro; IPR033179; PSD_type2_pro.
DR   NCBIfam; TIGR00163; PS_decarb; 1.
DR   PANTHER; PTHR10067; PHOSPHATIDYLSERINE DECARBOXYLASE; 1.
DR   PANTHER; PTHR10067:SF17; PHOSPHATIDYLSERINE DECARBOXYLASE PROENZYME 2; 1.
DR   Pfam; PF00168; C2; 2.
DR   Pfam; PF02666; PS_Dcarbxylase; 1.
DR   SMART; SM00239; C2; 2.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 2.
DR   SUPFAM; SSF47473; EF-hand; 1.
DR   PROSITE; PS50004; C2; 2.
DR   PROSITE; PS00018; EF_HAND_1; 1.
DR   PROSITE; PS50222; EF_HAND_2; 1.
PE   3: Inferred from homology;
KW   Calcium {ECO:0000256|ARBA:ARBA00022837};
KW   Decarboxylase {ECO:0000256|ARBA:ARBA00022793, ECO:0000256|HAMAP-
KW   Rule:MF_03209}; Endosome {ECO:0000256|HAMAP-Rule:MF_03209};
KW   Golgi apparatus {ECO:0000256|HAMAP-Rule:MF_03209};
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW   Rule:MF_03209};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW   Rule:MF_03209};
KW   Lyase {ECO:0000256|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_03209};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_03209};
KW   Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209,
KW   ECO:0000256|HAMAP-Rule:MF_03209};
KW   Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264, ECO:0000256|HAMAP-
KW   Rule:MF_03209};
KW   Pyruvate {ECO:0000256|ARBA:ARBA00023317, ECO:0000256|HAMAP-Rule:MF_03209};
KW   Reference proteome {ECO:0000313|Proteomes:UP000016931};
KW   Zymogen {ECO:0000256|ARBA:ARBA00023145, ECO:0000256|HAMAP-Rule:MF_03209}.
FT   CHAIN           1..1081
FT                   /note="Phosphatidylserine decarboxylase 2 beta chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT                   /id="PRO_5023496003"
FT   CHAIN           1082..1163
FT                   /note="Phosphatidylserine decarboxylase 2 alpha chain"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT                   /id="PRO_5023496002"
FT   DOMAIN          57..175
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          292..416
FT                   /note="C2"
FT                   /evidence="ECO:0000259|PROSITE:PS50004"
FT   DOMAIN          571..606
FT                   /note="EF-hand"
FT                   /evidence="ECO:0000259|PROSITE:PS50222"
FT   REGION          1..68
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          242..296
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          409..522
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          648..725
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1121..1145
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        12..55
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        249..264
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        282..296
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        444..522
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        649..681
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        937
FT                   /note="Charge relay system; for autoendoproteolytic
FT                   cleavage activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT   ACT_SITE        995
FT                   /note="Charge relay system; for autoendoproteolytic
FT                   cleavage activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT   ACT_SITE        1082
FT                   /note="Charge relay system; for autoendoproteolytic
FT                   cleavage activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT   ACT_SITE        1082
FT                   /note="Schiff-base intermediate with substrate; via pyruvic
FT                   acid; for decarboxylase activity"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT   SITE            1081..1082
FT                   /note="Cleavage (non-hydrolytic); by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT   MOD_RES         1082
FT                   /note="Pyruvic acid (Ser); by autocatalysis"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
SQ   SEQUENCE   1163 AA;  130539 MW;  84F50356052FAB8E CRC64;
     MPRPHLPSAL SLKRVKSSSN TSSSNANNNI NNNNNTSAPT TPLATRSSSP GYLMSNASRP
     PAKPMEGDHM GMGLLLHVQV LKARNLAAKD KSGFSDPFLV LTLGESKEAT SVVGKSLNPE
     WNQTFEFPVT SPDSALLEAV CWDKDRFRKD YMGEFDVVLE DIFAAGNLHP EPKWFKLEGR
     RNGRRKQKKD SNISGDVLIR FKLSDPIHTA ATPQQILQRF SGLVSDPEQD DDEDDDEELL
     RRMNSSNLDD LDEEDDDDEK EPSDETDDGA RTPVGTSSEE KQRHKRRRKL RRLRRKKKTS
     AYEFGATSDV AGVLYLEVNK VTDLPPEKNM TKTTFDMDPF VVTSLGRKTY RTRVVRHDLN
     PVYDEKLVFQ VQKNEQNFSL YFAVVDRDKF SGNDFVGTAN FPLERARELA PEADPDTGLY
     RLPDPEAVES EYQKRKRFRN PLSRSSSRND LPKLNSKANS STNLNKLAKS SSSSNLTTLT
     SLPQNEASRP SLQQRTSEVS IGDRTTRPPA VRMSSSGALT SHDDQNALDL ADEAGLHAFE
     LPLELKNIQR WEGKHHPVLY IRAKYLPYRA LRQQFWRVLL RQYDADESGK IDKIELVTML
     DTLGSTLHNK TIDGFFERWA DVNGEEYLTL DQAVICLEEQ LMKSRDSLPY ASHRSSANAD
     PSTSTARFTT VTNSPSSPEH SPAVGTPYLD ASDPLNYRPR QTSIPALEVS DLGDSGEMGD
     YMDGLEEELG GDPDSKEEHV VEISECPICH QPRISKGRKT TDADIITHIA TCASSDWRAV
     NNLVMAGFVT SSQAQRKWYS KIITKVSYGG YKLGANSANI LVQDRLTGQI NEERMSIYVR
     LGIRLLYKGL KSREMEKKRV RKLLRSMSFK QGRKYDDPAS ASQITGFINF HQLDMNEVKL
     PTEQFKTFNE FFYRELKPGA RPCSAPDDPN VIVSPADCRS VVFNRLEDAQ RIWVKGREFS
     IERLLGDAYP QDAKRYQNGS LGIFRLAPQD YHRFHIPVDG VMGEPKLIEG EYYTVNPMAI
     RSALDVYGEN VRVVVPIDSA CHGRVMVICV GAMMVGSTVI TRKAGEKVRR AEELGYFKFG
     GSTLLLLFEP GKMRFDEDLV TNASGALETL VRVGMAIGRT TGHSAHMPDQ PKANPTEEEK
     QRAKQRIEGS LAPSLRHHVS TAM
//
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