ID E3QBL4_COLGM Unreviewed; 1124 AA.
AC E3QBL4;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 65.
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=GLRG_03497 {ECO:0000313|EMBL:EFQ28353.1};
OS Colletotrichum graminicola (strain M1.001 / M2 / FGSC 10212) (Maize
OS anthracnose fungus) (Glomerella graminicola).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum graminicola species complex.
OX NCBI_TaxID=645133 {ECO:0000313|Proteomes:UP000008782};
RN [1] {ECO:0000313|Proteomes:UP000008782}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=M1.001 / M2 / FGSC 10212 {ECO:0000313|Proteomes:UP000008782};
RX PubMed=22885923; DOI=10.1038/ng.2372;
RA O'Connell R.J., Thon M.R., Hacquard S., Amyotte S.G., Kleemann J.,
RA Torres M.F., Damm U., Buiate E.A., Epstein L., Alkan N., Altmueller J.,
RA Alvarado-Balderrama L., Bauser C.A., Becker C., Birren B.W., Chen Z.,
RA Choi J., Crouch J.A., Duvick J.P., Farman M.A., Gan P., Heiman D.,
RA Henrissat B., Howard R.J., Kabbage M., Koch C., Kracher B., Kubo Y.,
RA Law A.D., Lebrun M.-H., Lee Y.-H., Miyara I., Moore N., Neumann U.,
RA Nordstroem K., Panaccione D.G., Panstruga R., Place M., Proctor R.H.,
RA Prusky D., Rech G., Reinhardt R., Rollins J.A., Rounsley S., Schardl C.L.,
RA Schwartz D.C., Shenoy N., Shirasu K., Sikhakolli U.R., Stueber K.,
RA Sukno S.A., Sweigard J.A., Takano Y., Takahara H., Trail F.,
RA van der Does H.C., Voll L.M., Will I., Young S., Zeng Q., Zhang J.,
RA Zhou S., Dickman M.B., Schulze-Lefert P., Ver Loren van Themaat E.,
RA Ma L.-J., Vaillancourt L.J.;
RT "Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered
RT by genome and transcriptome analyses.";
RL Nat. Genet. 44:1060-1065(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; GG697340; EFQ28353.1; -; Genomic_DNA.
DR RefSeq; XP_008092373.1; XM_008094182.1.
DR AlphaFoldDB; E3QBL4; -.
DR STRING; 645133.E3QBL4; -.
DR EnsemblFungi; EFQ28353; EFQ28353; GLRG_03497.
DR GeneID; 24408862; -.
DR VEuPathDB; FungiDB:GLRG_03497; -.
DR eggNOG; KOG2419; Eukaryota.
DR HOGENOM; CLU_002661_0_0_1; -.
DR OrthoDB; 51217at2759; -.
DR UniPathway; UPA00558; UER00616.
DR Proteomes; UP000008782; 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; 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:UP000008782};
KW Zymogen {ECO:0000256|ARBA:ARBA00023145, ECO:0000256|HAMAP-Rule:MF_03209}.
FT CHAIN 1..1026
FT /note="Phosphatidylserine decarboxylase 2 beta chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT /id="PRO_5023236837"
FT CHAIN 1027..1124
FT /note="Phosphatidylserine decarboxylase 2 alpha chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT /id="PRO_5023236838"
FT DOMAIN 28..148
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 278..400
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 533..568
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 217..271
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 421..471
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 633..674
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1062..1124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..41
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 217..233
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 236..258
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 422..471
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 634..663
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1071..1096
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 882
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT ACT_SITE 940
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT ACT_SITE 1027
FT /note="Charge relay system; for autoendoproteolytic
FT cleavage activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT ACT_SITE 1027
FT /note="Schiff-base intermediate with substrate; via pyruvic
FT acid; for decarboxylase activity"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT SITE 1026..1027
FT /note="Cleavage (non-hydrolytic); by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT MOD_RES 1027
FT /note="Pyruvic acid (Ser); by autocatalysis"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
SQ SEQUENCE 1124 AA; 125075 MW; CD394F55889CC33D CRC64;
MVRIIPGRLK SSSSLRNSRS SSPTRNSSNG SSTTSKMGDL SPKENGLTLK VVILKARNLA
AKDRSGTSDP YLVVTLGDAK VTTHEVPKTL NPDWNVIEEL PVNSTQCLLL DVICWDKDRF
GKDYLGEFDL ALEEIFADEQ NEQPPKWYPL RSKRPGKKTS VVSGEVMLQF TLFDQSNTAA
TREQIFEKFY ALVSQLPAGS RQITPTMTPL IQPVRNMSVH SGTDSSPPSS RNQTDADQEE
EEDDDLDIED DTPEDEDPSK PEVAEKRRRR LRIKGLKKKK RDQAYAFNNS GGDVVGIIYL
EVLNITDLPP EPNSTRLTFD MDPFVVASLG KKTYRTKRVR HNLNPVFNEK MIFQVQGHEQ
TYSFSFTVMD HDKYSGNDFI ADCTLPIREL IDKAPKADPE TGLYDVPEPH EYVPPQQRRF
KKLAMSRTSS SQSLSKARPV LSKNASSAST TTAAPSGTLT PTPAVQGSTL NPEFLSPEQA
LAGAGAQTAE LEAEDADFNE FSIALKMKDA KKWEDKHNPV LYIRAKYVPY PALRQQFWRS
MLKQYDTDES GRISKIELTT MLDTLGSTLH ESTIDSFFQR FPHRAQGEDM SDLTFDEAVI
CLEDQLEAKS RPQLTVGDRV KGMLPDAERV KNLLSGHDNN NSGSNGLSTE ASSSDSTINV
PELSTPGEEG DLLDRDDLAE DRSGEEHVVE IRECPICHQP RLNKRKDTDI ITHIATCASQ
DWRQVNNLVM GGFVTASQAQ RKWYSKVITK ISYGGYKLGA NSANILVQDR ITGQINEEKM
SVYVRLGIRL LYKGLKSSNM ETKRIRKMLK SMSVKQGKKF DDPASKAEIP KFIEFHRLDM
SEVLLPVEEF KSFNEFFYRA LKPGARPCSA PDRPDVVVSP ADCRSVVFNS VTQATKVWVK
GREFSIKRLL GDAYPDDVKR FENGALGIFR LAPQDYHRFH IPVDGVLDKP KTIAGEYYTV
NPMAIRSALD VYGENVRVLC PIDSPVHGRV MVICVGAMMV GSTVITAKEG TQVNRADELG
YFKFGGSTIV LLFEPGKMKF DDDLVDNSNG ALETLIRAGM SVGHAPDQPQ WGPDMRKDAK
DVTDAEKKDA KRRIGGNIGG EESSSGEETS DTHADLGTHA ASAM
//
