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PGPS1_DICDI
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   03-AUG-2022, entry version 92.
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 (Slime mold).
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.DDB0237934; -.
DR   PaxDb; Q7KWX2; -.
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; YLSTLYI; -.
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   InterPro; IPR016270; PGS1.
DR   InterPro; IPR025202; PLD-like_dom.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   PANTHER; PTHR12586; PTHR12586; 1.
DR   Pfam; PF13091; PLDc_2; 1.
DR   SMART; SM00155; PLDc; 2.
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
 
 
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