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Database: UniProt
Entry: K8PDI5_9BRAD
LinkDB: K8PDI5_9BRAD
Original site: K8PDI5_9BRAD 
ID   K8PDI5_9BRAD            Unreviewed;       181 AA.
AC   K8PDI5;
DT   06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT   06-FEB-2013, sequence version 1.
DT   27-MAR-2024, entry version 35.
DE   RecName: Full=CDP-diacylglycerol--glycerol-3-phosphate 1-phosphatidyltransferase {ECO:0000256|ARBA:ARBA00013170};
DE            EC=2.7.8.5 {ECO:0000256|ARBA:ARBA00013170};
GN   ORFNames=HMPREF9695_01587 {ECO:0000313|EMBL:EKS39626.1};
OS   Afipia broomeae ATCC 49717.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Nitrobacteraceae; Afipia.
OX   NCBI_TaxID=883078 {ECO:0000313|EMBL:EKS39626.1, ECO:0000313|Proteomes:UP000001096};
RN   [1] {ECO:0000313|EMBL:EKS39626.1, ECO:0000313|Proteomes:UP000001096}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 49717 {ECO:0000313|EMBL:EKS39626.1,
RC   ECO:0000313|Proteomes:UP000001096};
RG   The Broad Institute Genome Sequencing Platform;
RA   Earl A., Ward D., Feldgarden M., Gevers D., Huys G., Walker B., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA   Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA   Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA   Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT   "The Genome Sequence of Afipia broomeae ATCC 49717.";
RL   Submitted (APR-2012) to the EMBL/GenBank/DDBJ databases.
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   -!- PATHWAY: Lipid metabolism. {ECO:0000256|ARBA:ARBA00005189}.
CC   -!- PATHWAY: Phospholipid metabolism. {ECO:0000256|ARBA:ARBA00025707}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004651};
CC       Multi-pass membrane protein {ECO:0000256|ARBA:ARBA00004651}. Membrane
CC       {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC       {ECO:0000256|ARBA:ARBA00004141}.
CC   -!- SIMILARITY: Belongs to the CDP-alcohol phosphatidyltransferase class-I
CC       family. {ECO:0000256|ARBA:ARBA00010441}.
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:EKS39626.1}.
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DR   EMBL; AGWX01000002; EKS39626.1; -; Genomic_DNA.
DR   RefSeq; WP_006020304.1; NZ_KB375282.1.
DR   AlphaFoldDB; K8PDI5; -.
DR   PATRIC; fig|883078.3.peg.1627; -.
DR   eggNOG; COG0558; Bacteria.
DR   HOGENOM; CLU_051314_6_2_5; -.
DR   Proteomes; UP000001096; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0008444; F:CDP-diacylglycerol-glycerol-3-phosphate 3-phosphatidyltransferase activity; IEA:InterPro.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR   Gene3D; 1.20.120.1760; -; 1.
DR   InterPro; IPR000462; CDP-OH_P_trans.
DR   InterPro; IPR043130; CDP-OH_PTrfase_TM_dom.
DR   InterPro; IPR004570; Phosphatidylglycerol_P_synth.
DR   PANTHER; PTHR14269:SF60; CARDIOLIPIN SYNTHASE (CMP-FORMING); 1.
DR   PANTHER; PTHR14269; CDP-DIACYLGLYCEROL--GLYCEROL-3-PHOSPHATE 3-PHOSPHATIDYLTRANSFERASE-RELATED; 1.
DR   Pfam; PF01066; CDP-OH_P_transf; 1.
DR   PIRSF; PIRSF000847; Phos_ph_gly_syn; 1.
PE   3: Inferred from homology;
KW   Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516};
KW   Lipid metabolism {ECO:0000256|ARBA:ARBA00023098};
KW   Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|SAM:Phobius};
KW   Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209};
KW   Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001096};
KW   Transferase {ECO:0000313|EMBL:EKS39626.1};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        12..37
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        86..108
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        120..143
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        149..168
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
SQ   SEQUENCE   181 AA;  19541 MW;  893E1B8225C79F99 CRC64;
     MNLPNIITLG RILLVPVIVW AIASNQMTIA FVIFVVAGVS DAIDGFLAKR FNMTTEIGAL
     LDPVADKALL VSIYVTLGIS GDIPRWLVIL VVSRDFMIVG AVIISWLLDN PVPMKPLMVS
     KLNTVAQVAF AALVLASLGF QFNASPYEVI LAGFVTVLTL LSVSFYLVEW ARHMSATAPI
     P
//
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