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Database: UniProt
Entry: A8ZV42_DESOH
LinkDB: A8ZV42_DESOH
Original site: A8ZV42_DESOH 
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
//
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