ID M2SS51_COCSN Unreviewed; 1087 AA.
AC M2SS51;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 27-MAR-2024, entry version 58.
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=COCSADRAFT_116481 {ECO:0000313|EMBL:EMD65090.1};
OS Cochliobolus sativus (strain ND90Pr / ATCC 201652) (Common root rot and
OS spot blotch fungus) (Bipolaris sorokiniana).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae; Bipolaris.
OX NCBI_TaxID=665912 {ECO:0000313|EMBL:EMD65090.1, ECO:0000313|Proteomes:UP000016934};
RN [1] {ECO:0000313|EMBL:EMD65090.1, ECO:0000313|Proteomes:UP000016934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
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).
RN [2] {ECO:0000313|Proteomes:UP000016934}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ND90Pr / ATCC 201652 {ECO:0000313|Proteomes:UP000016934};
RX PubMed=23357949; DOI=10.1371/journal.pgen.1003233;
RA Condon B.J., Leng Y., Wu D., Bushley K.E., Ohm R.A., Otillar R., Martin J.,
RA Schackwitz W., Grimwood J., MohdZainudin N., Xue C., Wang R., Manning V.A.,
RA Dhillon B., Tu Z.J., Steffenson B.J., Salamov A., Sun H., Lowry S.,
RA LaButti K., Han J., Copeland A., Lindquist E., Barry K., Schmutz J.,
RA Baker S.E., Ciuffetti L.M., Grigoriev I.V., Zhong S., Turgeon B.G.;
RT "Comparative genome structure, secondary metabolite, and effector coding
RT capacity across Cochliobolus pathogens.";
RL PLoS Genet. 9:E1003233-E1003233(2013).
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; KB445642; EMD65090.1; -; Genomic_DNA.
DR RefSeq; XP_007699589.1; XM_007701399.1.
DR AlphaFoldDB; M2SS51; -.
DR STRING; 665912.M2SS51; -.
DR GeneID; 19130329; -.
DR KEGG; bsc:COCSADRAFT_116481; -.
DR eggNOG; KOG1012; Eukaryota.
DR eggNOG; KOG2419; Eukaryota.
DR HOGENOM; CLU_002661_0_0_1; -.
DR OMA; TCASRDW; -.
DR OrthoDB; 51217at2759; -.
DR UniPathway; UPA00558; UER00616.
DR Proteomes; UP000016934; 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 CDD; cd04024; C2A_Synaptotagmin-like; 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:UP000016934};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145, ECO:0000256|HAMAP-Rule:MF_03209}.
FT CHAIN 1..1003
FT /note="Phosphatidylserine decarboxylase 2 beta chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT /id="PRO_5023225603"
FT CHAIN 1004..1087
FT /note="Phosphatidylserine decarboxylase 2 alpha chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT /id="PRO_5023225602"
FT DOMAIN 45..163
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 265..387
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 523..558
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 1..57
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 212..255
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 378..483
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1043..1087
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 18..51
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 220..239
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 415..452
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..481
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1054..1069
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 859
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT ACT_SITE 917
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT ACT_SITE 1004
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT ACT_SITE 1004
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid; for decarboxylase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT SITE 1003..1004
FT /note="Cleavage (non-hydrolytic); by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT MOD_RES 1004
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
SQ SEQUENCE 1087 AA; 121247 MW; 56A411EE4B53B249 CRC64;
MPRPTFTTRL SLPHRLKRPT SCYNSSSTPN TQTPALSVPA SRNSSPRTRT RPMPEQPAPA
GLVLRVNVIK GRDLAAKDRS GTSDPYLVLT LGDAKVTTPA INKQLNPEWN ETLELPIVGE
QSLLLEAVCW DKDRFGKDYM GEFDVILEDH FQNGLTQQEP QWFPLESRRS GKKKSVVSGE
IQMQFTLIDP QNLSASPEQT LQKFFAIAGQ AHSPDEDDED LGGNSNSTDA EEDDDSSSDE
AQDESKKAEK REKRRKKLKL ARLKRKVKSQ AVYAYSSSGD VAGILFLEVQ RCSDLPPERN
VTRTTFDMDP FVITSLGKKT YRTKTVRHDL NPVFDEKLVF QVMRHETNYS VNFTVMDKDK
FSGNDYVGTV NFPLEKAIST APQEDPETGL YKLPEPSDSP GVSPDGGSKK SRFRIPMSRS
GSTHSLSRLG RPSLKKESST GSLSVQDANG TQPPSPGAPP SALTDSNGNL TPGSTLNLQP
SAVDDEDLKM YTLPLELKHQ ERWENKHNPT LYIRAKYLPY KALRQQFWRA MLKQYDADES
GLLDKVELTT MLDTLGSTLH EATIDSFFER FAYRHNGEHL LTFDEAVVCL EDQLEATEAK
NAKRDGSFAS GSQTPMTSGM LTPINQSSST TSIPVLETNT LGKEGEEGAD LQIDDLADEK
GEEHVIEIRE CPICHQPKLN KRSDANIITH IATCASQDWR QVNNIVMAGF VTSSQAQRKW
YSKVITKISY GGYKLGANSA NILVQDRLTG QINEERMSVY VRLGIRLLYK GLKANNMEKK
RIRKLLKSLS FKQGRKYDDP ASASEIEPFI NFHQLDMSEV LLPTDQFKNF NEFFYRALKP
GARPCSAPDD PRVIVSPSDC RTVVFNTIDT AQAIWVKGRD FTIERLLGDA YPQDVKRYYG
GSLGIFRLAP QDYHRFHIPV DGVLDEPKTI EGEYYTVNPM AIRSALDVYG ENVRVVVPID
SVAHGRVMVI CVGAMMVGST VITRKKGEQV KRAEELGYFK FGGSTLLLLF EPGQMRYDED
LVENSNAALE TLVRVGMSIG HSPNRPAYVP DMRKSNPTHE EKQDAKRRIE GSLAPAGVKG
PMPGAGM
//
