ID T0KYV5_COLGC Unreviewed; 1124 AA.
AC T0KYV5;
DT 16-OCT-2013, integrated into UniProtKB/TrEMBL.
DT 16-OCT-2013, sequence version 1.
DT 27-MAR-2024, entry version 55.
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=CGLO_02056 {ECO:0000313|EMBL:EQB57783.1};
OS Colletotrichum gloeosporioides (strain Cg-14) (Anthracnose fungus)
OS (Glomerella cingulata).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum gloeosporioides species complex.
OX NCBI_TaxID=1237896 {ECO:0000313|EMBL:EQB57783.1, ECO:0000313|Proteomes:UP000015530};
RN [1] {ECO:0000313|Proteomes:UP000015530}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Cg-14 {ECO:0000313|Proteomes:UP000015530};
RX PubMed=23902260; DOI=10.1094/MPMI-03-13-0080-R;
RA Alkan N., Meng X., Friedlander G., Reuveni E., Sukno S., Sherman A.,
RA Thon M., Fluhr R., Prusky D.;
RT "Global aspects of pacC regulation of pathogenicity genes in Colletotrichum
RT gloeosporioides as revealed by transcriptome analysis.";
RL Mol. Plant Microbe Interact. 26:1345-1358(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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EQB57783.1}.
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DR EMBL; AMYD01000422; EQB57783.1; -; Genomic_DNA.
DR AlphaFoldDB; T0KYV5; -.
DR STRING; 1237896.T0KYV5; -.
DR eggNOG; KOG2419; Eukaryota.
DR HOGENOM; CLU_002661_0_0_1; -.
DR OMA; TCASRDW; -.
DR OrthoDB; 51217at2759; -.
DR UniPathway; UPA00558; UER00616.
DR Proteomes; UP000015530; 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:UP000015530};
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_5023469890"
FT CHAIN 1027..1124
FT /note="Phosphatidylserine decarboxylase 2 alpha chain"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_03209"
FT /id="PRO_5023469891"
FT DOMAIN 30..149
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 279..400
FT /note="C2"
FT /evidence="ECO:0000259|PROSITE:PS50004"
FT DOMAIN 536..571
FT /note="EF-hand"
FT /evidence="ECO:0000259|PROSITE:PS50222"
FT REGION 1..44
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 204..273
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 423..478
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..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 11..40
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 204..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 423..467
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 644..661
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1073..1096
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1098..1124
FT /note="Polar 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; 125123 MW; E28EEC1ED891FA46 CRC64;
MVRIIPGRLK SSSSLRHSRS SSPTRNNSNS STSSNGKMGE LSPKDNGLTL KVVIMKARNL
AAKDRSGTSD PFLVVTLGDA KVTTHEVPKT LNPEWNVIEE LPVNNTQSLI LDVICWDKDR
FGKDYLGEFD LALEEIFADE QNEQPPRWYP LKSKKPGKKT SVVSGEVMLQ FTLFDQSNTA
ATREQVFEKF YSLVSQVPAG SRQITPTMTP LIQPIKNMRV RSGTTPSPPL SRNATDDQEE
EDDDDLDIED DTPEDEDPSK PEAAEKRKRR LRIKGLKKKR RDHAYEFNNS GSDVVGIIYL
EVLNITDLPP EPNSTRTTFD MDPFVVASLG KKTYRTKRVR HNLNPVFNEK MIFQVQGHEQ
QYSFAFTVMD HDKYSGNDFI ADCNLAVREL IDKAPKADPE TGLYDVPEPA EFVAPQQRRF
KKLAMSRTSS SQSLSKVVRP SLSKNPSSTS GAPGGSQSGT VTPTPAAQPG GLNPEFLSPE
QALAGAGAQT AEAQQSEEVD FHDFSIPLKM KDAKKWEDKH NPVLYIRAKY VPYPALRQQF
WRSMLKQYDT DESGRISKIE LTTMLDTLGS TLHESTIDGF FKRFPHREEG EEVGDLTMDE
AVLCLEDQLE AKSKPVTVTQ KMKGMLPDAD KVKNLLSGPG HAQPGLSTEA SSSSDGTLNV
PELSTPGEEG DLLDKDDLAE DRSGEEHVVE IRECPICHQP RLNKRKDTDI ITHIATCASQ
DWRQVNNLVM GGFVTASQAQ RKWYSKVITK ISYGGYKLGA NSANILVQDR ITGQINEEKM
SVYVRLGIRL LYKGLKSSNM ETKRIRKMLK SMSIKQGKKF DDPASKAEIP KFIEFHRLDM
SEVLLPLEEF KNFNEFFYRA LKPDARPCSG AERPDVTVSP ADCRSVVFNS VNQATNVWIK
GREFSIKRLL GDAYPEDVKR FENGALGIFR LAPQDYHRFH IPVDGILDKP KTIAGEYYTV
NPMAIRSALD VYGENVRVLC PIDSPVHGRV MVICVGAMMV GSTVITRKEG EQVKRAEELG
YFKFGGSTIV LLFEPGKMVF DDDLVDNSNT ALETLVRAGM SVGHAPGTPQ WAPDMRKDEK
DITEADKKDA KRRIGGSLTG EESSSGDETP GNGTDINTHA ASAM
//
