ID E3QG44_COLGM Unreviewed; 492 AA.
AC E3QG44;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE RecName: Full=CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase {ECO:0000256|RuleBase:RU365024};
DE EC=2.7.8.5 {ECO:0000256|RuleBase:RU365024};
GN ORFNames=GLRG_05023 {ECO:0000313|EMBL:EFQ29879.1};
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: Functions in the biosynthesis of the anionic phospholipids
CC phosphatidylglycerol and cardiolipin. {ECO:0000256|RuleBase:RU365024}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a CDP-1,2-diacyl-sn-glycerol + sn-glycerol 3-phosphate = 1,2-
CC diacyl-sn-glycero-3-phospho-(1'-sn-glycero-3'-phosphate) + CMP +
CC H(+); Xref=Rhea:RHEA:12593, ChEBI:CHEBI:15378, ChEBI:CHEBI:57597,
CC ChEBI:CHEBI:58332, ChEBI:CHEBI:60110, ChEBI:CHEBI:60377; EC=2.7.8.5;
CC Evidence={ECO:0000256|ARBA:ARBA00001566,
CC ECO:0000256|RuleBase:RU365024};
CC -!- PATHWAY: Phospholipid metabolism; phosphatidylglycerol biosynthesis;
CC phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
CC {ECO:0000256|ARBA:ARBA00005042, ECO:0000256|RuleBase:RU365024}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|RuleBase:RU365024}.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-II
CC family. {ECO:0000256|ARBA:ARBA00010682, ECO:0000256|RuleBase:RU365024}.
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DR EMBL; GG697346; EFQ29879.1; -; Genomic_DNA.
DR RefSeq; XP_008093899.1; XM_008095708.1.
DR AlphaFoldDB; E3QG44; -.
DR STRING; 645133.E3QG44; -.
DR EnsemblFungi; EFQ29879; EFQ29879; GLRG_05023.
DR GeneID; 24410388; -.
DR VEuPathDB; FungiDB:GLRG_05023; -.
DR eggNOG; KOG3964; Eukaryota.
DR HOGENOM; CLU_030471_1_1_1; -.
DR OrthoDB; 179003at2759; -.
DR UniPathway; UPA00084; UER00503.
DR Proteomes; UP000008782; Unassembled WGS sequence.
DR GO; GO:0031966; C:mitochondrial membrane; IEA:EnsemblFungi.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008444; F:CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; IEA:EnsemblFungi.
DR CDD; cd09135; PLDc_PGS1_euk_1; 1.
DR CDD; cd09137; PLDc_PGS1_euk_2; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR InterPro; IPR016270; PGS1.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR PANTHER; PTHR12586:SF1; CDP-DIACYLGLYCEROL--GLYCEROL-3-PHOSPHATE 3-PHOSPHATIDYLTRANSFERASE, MITOCHONDRIAL; 1.
DR PANTHER; PTHR12586; CDP-DIACYLGLYCEROL--SERINE O-PHOSPHATIDYLTRANSFERASE; 1.
DR PIRSF; PIRSF000850; Phospholipase_D_PSS; 2.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50035; PLD; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|RuleBase:RU365024};
KW Lipid biosynthesis {ECO:0000256|RuleBase:RU365024};
KW Lipid metabolism {ECO:0000256|RuleBase:RU365024};
KW Mitochondrion {ECO:0000256|RuleBase:RU365024};
KW Nucleotide-binding {ECO:0000256|RuleBase:RU365024};
KW Phospholipid biosynthesis {ECO:0000256|RuleBase:RU365024};
KW Phospholipid metabolism {ECO:0000256|RuleBase:RU365024};
KW Reference proteome {ECO:0000313|Proteomes:UP000008782};
KW Transferase {ECO:0000256|RuleBase:RU365024}.
FT DOMAIN 153..179
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
SQ SEQUENCE 492 AA; 54388 MW; 3371AA8F6D9A3B44 CRC64;
MPSAGTPSAS NSGSAAGMLA PFANELDKIA PSFSVNGSQI QIIRTPADFY ETLKERIRNA
KRRVFLSTLY IGKTEKELVA TLQEALRNNP ELKLSILTDA LRGTREEPNP SCASLLAPLV
FEFGADRVEI RMYHTPNLTG VRKKYIPKRI NEGWGLQHMK LYGIDDEIIL SGANLSSDYF
TNRQDRYHLF SSKDVTDYFW NIHHGVSSFS FLVEPSKEAA GFTLTWPKSN PAPSPLEEPK
QFIGTTTPTL DALISPKQSA SADAGKDTKV YMLAQLSQLM KPDTSTELPA ITHVLSTLSK
PEYSGSSWTF TAGYFNPAPS LTKLLLSTAS RNNVVITASQ QANGFYQSPG VSGLLPGAYT
LLARRFIRAV HERGLDDSIV LKEWRKGTVG EPGGWTYHAK GLWITLPGDQ NPSISIVGSS
NYTKRSYSHD LEAGAMILTK DEDLKKRLGQ EQTWLQEHAE RVTREDFSKN ERRVGLQVRL
AMWIAQAVGG AL
//
