ID PGPS1_DICDI Reviewed; 581 AA.
AC Q7KWX2; Q550R0;
DT 01-JUL-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 27-MAR-2024, entry version 98.
DE RecName: Full=Probable CDP-diacylglycerol--glycerol-3-phosphate 3-phosphatidyltransferase;
DE EC=2.7.8.5;
DE AltName: Full=Phosphatidylglycerophosphate synthase 1;
DE Short=PGP synthase 1;
GN Name=pgs1; ORFNames=DDB_G0277037;
OS Dictyostelium discoideum (Social amoeba).
OC Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC Dictyosteliaceae; Dictyostelium.
OX NCBI_TaxID=44689;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=12097910; DOI=10.1038/nature00847;
RA Gloeckner G., Eichinger L., Szafranski K., Pachebat J.A., Bankier A.T.,
RA Dear P.H., Lehmann R., Baumgart C., Parra G., Abril J.F., Guigo R.,
RA Kumpf K., Tunggal B., Cox E.C., Quail M.A., Platzer M., Rosenthal A.,
RA Noegel A.A.;
RT "Sequence and analysis of chromosome 2 of Dictyostelium discoideum.";
RL Nature 418:79-85(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AX4;
RX PubMed=15875012; DOI=10.1038/nature03481;
RA Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT "The genome of the social amoeba Dictyostelium discoideum.";
RL Nature 435:43-57(2005).
CC -!- FUNCTION: Functions in the biosynthesis of the anionic phospholipids
CC phosphatidylglycerol and cardiolipin. {ECO:0000250}.
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 -!- PATHWAY: Phospholipid metabolism; phosphatidylglycerol biosynthesis;
CC phosphatidylglycerol from CDP-diacylglycerol: step 1/2.
CC -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-II
CC family. {ECO:0000305}.
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DR EMBL; AAFI02000019; EAL69020.2; -; Genomic_DNA.
DR RefSeq; XP_642872.2; XM_637780.2.
DR AlphaFoldDB; Q7KWX2; -.
DR SMR; Q7KWX2; -.
DR STRING; 44689.Q7KWX2; -.
DR PaxDb; 44689-DDB0237934; -.
DR EnsemblProtists; EAL69020; EAL69020; DDB_G0277037.
DR GeneID; 8620738; -.
DR KEGG; ddi:DDB_G0277037; -.
DR dictyBase; DDB_G0277037; pgs1.
DR eggNOG; KOG3964; Eukaryota.
DR HOGENOM; CLU_030471_1_1_1; -.
DR InParanoid; Q7KWX2; -.
DR OMA; HKCLAQC; -.
DR PhylomeDB; Q7KWX2; -.
DR UniPathway; UPA00084; UER00503.
DR PRO; PR:Q7KWX2; -.
DR Proteomes; UP000002195; Chromosome 2.
DR GO; GO:0005739; C:mitochondrion; ISS:dictyBase.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0008444; F:CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity; ISS:dictyBase.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; IBA:GO_Central.
DR GO; GO:0008654; P:phospholipid biosynthetic process; ISS:dictyBase.
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; IPR025202; PLD-like_dom.
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 Pfam; PF13091; PLDc_2; 1.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 1.
DR PROSITE; PS50035; PLD; 1.
PE 3: Inferred from homology;
KW ATP-binding; Lipid biosynthesis; Lipid metabolism; Nucleotide-binding;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome;
KW Repeat; Transferase.
FT CHAIN 1..581
FT /note="Probable CDP-diacylglycerol--glycerol-3-phosphate 3-
FT phosphatidyltransferase"
FT /id="PRO_0000342201"
FT DOMAIN 248..274
FT /note="PLD phosphodiesterase 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT DOMAIN 487..520
FT /note="PLD phosphodiesterase 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT REGION 27..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 253
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 255
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT ACT_SITE 260
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00153"
FT BINDING 160..167
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
SQ SEQUENCE 581 AA; 65509 MW; E27C824B4B4C6542 CRC64;
MIKRALAPIV QPQRLFAALM VIGGGGRSAT TTTTTTTKAC GNGSSQSPPS TPLLSSKSST
ITSNKKSAIP SSHLYIPKKS TLDSRQIGNY SREYSTSSSS SSKKSIFNDT YLNDLFWQLS
SQGPAFEVNP NNIDFIQEPI DFYNHLIDGV KRSKKRITMA SLYLGTSKQE IELVKEMKLA
MERNKELKIH ILLDGLRGTR IGLDKESSAT ILGELLSLYS DRVTISMYHT PDLNGILKKV
LPPRINETIG VQHIKTYIFD DDLLLSGANL SKDYFTNRQD RYVLIRSTST VSNYFNEIVE
IIGSLSLHVD KDNRNQLLLS SGSIDPVTQS NEFKNLAYTK LSTLLKSHSY YPSNSNSNSS
VDSPFDCNNI NNGETTWIFP TIQMGPFNIR QDEVVTSHIF ESVPNDSKFF ITSPYFNLTE
NYLNLILTGK PKLDIITCSP QANGFYGSKG LSSAVPDCYA IIEKRFLQRV QDTDNGDRIS
VQEYIRDKWT YHAKGLWIQV KNQQHPSITL IGSPNFGSRS VEKDLEAQII LITQNKQLQQ
KMENEKNYLW TDTQNANLEL FEKRKVSLMV RFLVYIFGNY L
//
