ID A8ZV42_DESOH Unreviewed; 480 AA.
AC A8ZV42;
DT 15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT 15-JAN-2008, sequence version 1.
DT 24-JAN-2024, entry version 86.
DE RecName: Full=Cardiolipin synthase {ECO:0000256|HAMAP-Rule:MF_01916};
DE Short=CL synthase {ECO:0000256|HAMAP-Rule:MF_01916};
DE EC=2.7.8.- {ECO:0000256|HAMAP-Rule:MF_01916};
GN OrderedLocusNames=Dole_2328 {ECO:0000313|EMBL:ABW68132.1};
OS Desulfosudis oleivorans (strain DSM 6200 / JCM 39069 / Hxd3) (Desulfococcus
OS oleovorans).
OC Bacteria; Thermodesulfobacteriota; Desulfobacteria; Desulfobacterales;
OC Desulfosudaceae; Desulfosudis.
OX NCBI_TaxID=96561 {ECO:0000313|EMBL:ABW68132.1, ECO:0000313|Proteomes:UP000008561};
RN [1] {ECO:0000313|EMBL:ABW68132.1, ECO:0000313|Proteomes:UP000008561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 6200 / JCM 39069 / Hxd3
RC {ECO:0000313|Proteomes:UP000008561};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Kiss H., Brettin T., Bruce D., Detter J.C., Han C.,
RA Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Kim E., Wawrik B.,
RA Richardson P.;
RT "Complete sequence of Desulfococcus oleovorans Hxd3.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the reversible phosphatidyl group transfer from one
CC phosphatidylglycerol molecule to another to form cardiolipin (CL)
CC (diphosphatidylglycerol) and glycerol. {ECO:0000256|HAMAP-
CC Rule:MF_01916}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 1,2-diacyl-sn-glycero-3-phospho-(1'-sn-glycerol) = a
CC cardiolipin + glycerol; Xref=Rhea:RHEA:31451, ChEBI:CHEBI:17754,
CC ChEBI:CHEBI:62237, ChEBI:CHEBI:64716; Evidence={ECO:0000256|HAMAP-
CC Rule:MF_01916};
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000256|HAMAP-
CC Rule:MF_01916}; Multi-pass membrane protein {ECO:0000256|HAMAP-
CC Rule:MF_01916}. Membrane {ECO:0000256|ARBA:ARBA00004141}; Multi-pass
CC membrane protein {ECO:0000256|ARBA:ARBA00004141}.
CC -!- SIMILARITY: Belongs to the phospholipase D family. Cardiolipin synthase
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_01916}.
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DR EMBL; CP000859; ABW68132.1; -; Genomic_DNA.
DR RefSeq; WP_012175744.1; NC_009943.1.
DR AlphaFoldDB; A8ZV42; -.
DR STRING; 96561.Dole_2328; -.
DR KEGG; dol:Dole_2328; -.
DR eggNOG; COG1502; Bacteria.
DR HOGENOM; CLU_038053_1_1_7; -.
DR OMA; TRFILDW; -.
DR OrthoDB; 9762009at2; -.
DR Proteomes; UP000008561; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR GO; GO:0008808; F:cardiolipin synthase activity; IEA:InterPro.
DR GO; GO:0032049; P:cardiolipin biosynthetic process; IEA:InterPro.
DR CDD; cd09110; PLDc_CLS_1; 1.
DR CDD; cd09112; PLDc_CLS_2; 1.
DR Gene3D; 3.30.870.10; Endonuclease Chain A; 2.
DR HAMAP; MF_01916; Cardiolipin_synth_Cls; 1.
DR InterPro; IPR030874; Cardiolipin_synth_Firmi.
DR InterPro; IPR022924; Cardiolipin_synthase.
DR InterPro; IPR027379; CLS_N.
DR InterPro; IPR025202; PLD-like_dom.
DR InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR NCBIfam; TIGR04265; bac_cardiolipin; 1.
DR PANTHER; PTHR21248; CARDIOLIPIN SYNTHASE; 1.
DR PANTHER; PTHR21248:SF22; PHOSPHOLIPASE D; 1.
DR Pfam; PF13091; PLDc_2; 2.
DR Pfam; PF13396; PLDc_N; 1.
DR SMART; SM00155; PLDc; 2.
DR SUPFAM; SSF56024; Phospholipase D/nuclease; 2.
DR PROSITE; PS50035; PLD; 2.
PE 3: Inferred from homology;
KW Cell inner membrane {ECO:0000256|HAMAP-Rule:MF_01916};
KW Cell membrane {ECO:0000256|ARBA:ARBA00022475, ECO:0000256|HAMAP-
KW Rule:MF_01916};
KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP-
KW Rule:MF_01916};
KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP-
KW Rule:MF_01916};
KW Membrane {ECO:0000256|ARBA:ARBA00023136, ECO:0000256|HAMAP-Rule:MF_01916};
KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209,
KW ECO:0000256|HAMAP-Rule:MF_01916};
KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264, ECO:0000256|HAMAP-
KW Rule:MF_01916}; Reference proteome {ECO:0000313|Proteomes:UP000008561};
KW Repeat {ECO:0000256|ARBA:ARBA00022737};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_01916};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|HAMAP-
KW Rule:MF_01916};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989, ECO:0000256|HAMAP-
KW Rule:MF_01916}.
FT TRANSMEM 7..25
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT TRANSMEM 31..54
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT DOMAIN 218..245
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 393..420
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT ACT_SITE 223
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 225
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 230
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 398
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 400
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 405
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
SQ SEQUENCE 480 AA; 55289 MW; 9EFCB4749416F55F CRC64;
MVPWDTILIV ALYIYIAVTI VYLLLDNRET ASTLSWLLVF IFLPVLGLVV YFLVGRGMRK
KTTRTLVRQD LETRLQDSHE SLVTQQKDEA DALHVRYPSP ETRKLIRLLD RNSDSILTRH
NELSVFFNGQ EKFEVLFNDL MRARHYIHME YFIWKADDLT EMVVAVLKEK AVQGVAVRVL
YDAVGNYLSG RYLRRLRRAG IQIYPYYNFV SPLKIHTLNY RNHRKVVVID GETGYLGGMN
MGQEYVDGGK RFPVWRDTHI RIQGEAVAVL EEVFAVSWFN TTGETIDVKA FVPQPPPDIT
HIQITTSGPD SQWHSIKQVY FLLISSAENS VFIQTPYFIP DASILMALKT AALSGIDVRI
MLTGMLDKRV PYWAALTYIE ELLQAGVRFY YYTEGFMHAK TIVVDSLCCS VGTANMDIRS
FELNYEINAL IYDANVAKVF EAMFRKDLAA AREFTLEDYS RMSRLKKFRN SLARLFAPLL
//