ID E5D6N0_9BACT Unreviewed; 485 AA.
AC E5D6N0;
DT 08-FEB-2011, integrated into UniProtKB/TrEMBL.
DT 08-FEB-2011, sequence version 1.
DT 13-SEP-2023, entry version 45.
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 ORFNames=nle15_4 {ECO:0000313|EMBL:ADQ39287.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:ADQ39287.1};
RN [1] {ECO:0000313|EMBL:ADQ39287.1}
RP NUCLEOTIDE SEQUENCE.
RA Peng Q., Shang M., Wang X., Guan G.H., Li Y.;
RT "Isolation of novel lipolytic genes from neritic sediment metagenomic
RT library of South China Sea.";
RL Submitted (NOV-2009) 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 membrane {ECO:0000256|HAMAP-Rule:MF_01916};
CC Multi-pass membrane protein {ECO:0000256|HAMAP-Rule:MF_01916}. Membrane
CC {ECO:0000256|ARBA:ARBA00004141}; Multi-pass membrane protein
CC {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; GU187944; ADQ39287.1; -; Genomic_DNA.
DR AlphaFoldDB; E5D6N0; -.
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 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}; 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 12..31
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT TRANSMEM 38..59
FT /note="Helical"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT DOMAIN 221..248
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT DOMAIN 398..425
FT /note="PLD phosphodiesterase"
FT /evidence="ECO:0000259|PROSITE:PS50035"
FT ACT_SITE 226
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 228
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 233
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 403
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 405
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
FT ACT_SITE 410
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01916"
SQ SEQUENCE 485 AA; 56331 MW; E01D2CDDB48D6529 CRC64;
MLSYLEENFW VSVLLINYII AVGTAIFIVL HNRNPTKTLS FILGLLALPF IGIFIYYFFG
QEYRKSKIFK REDVYSHKRI KAWEKKFLFA EGMVQELKDP LIAKKFKLIN LLQYNQKAAI
TFRNNVRILQ NAENKFKALF EDLRNARKHI HLEYYIFNDD IIGSELLEIL CEKSREGVSV
KVIYDYVGSE MSRKGVKRMK DAGVEVHAFM PVWFPNLTRR LNYRDHRKIV VIDGIIGYVG
GVNICDLYVN RDDSEVYWRD THSRIEGHAV KSLQTQFLYN WNFLTESKAE IIEEYFPKVE
IEENVAVQIA ASGPDTDYPN IMEAVLTAIT TAEKYIYITT PYFIPNDEIL TALCIASRSG
VDVRLIIPLV GDSWAAKYAT NSYIEEMLES GLQVHHYHKG MVHAKTMVVD GVFSTVGTCN
MDNRSFQLNF EINALFYNKK ISDELTETFM DDLKDCTSNN LEEWRERASI EKVKESFCRL
WAPLL
//
