(data stored in SCRATCH zone)

SWISSPROT: E6UXP1_VARPE

ID   E6UXP1_VARPE            Unreviewed;       423 AA.
AC   E6UXP1;
DT   08-MAR-2011, integrated into UniProtKB/TrEMBL.
DT   08-MAR-2011, sequence version 1.
DT   08-MAY-2019, entry version 44.
DE   RecName: Full=Cardiolipin synthase B {ECO:0000256|HAMAP-Rule:MF_01917};
DE            Short=CL synthase {ECO:0000256|HAMAP-Rule:MF_01917};
DE            EC=2.7.8.- {ECO:0000256|HAMAP-Rule:MF_01917};
GN   Name=clsB {ECO:0000256|HAMAP-Rule:MF_01917};
GN   OrderedLocusNames=Varpa_0012 {ECO:0000313|EMBL:ADU34235.1};
OS   Variovorax paradoxus (strain EPS).
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Comamonadaceae; Variovorax.
OX   NCBI_TaxID=595537 {ECO:0000313|EMBL:ADU34235.1, ECO:0000313|Proteomes:UP000008917};
RN   [1] {ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|Proteomes:UP000008917};
RG   US DOE Joint Genome Institute;
RA   Lucas S., Copeland A., Lapidus A., Cheng J.-F., Goodwin L.,
RA   Pitluck S., Teshima H., Detter J.C., Han C., Tapia R., Land M.,
RA   Hauser L., Kyrpides N., Ivanova N., Ovchinnikova G., Orwin P.,
RA   Han J.-I.G., Woyke T.;
RT   "Complete sequence of Variovorax paradoxus EPS.";
RL   Submitted (DEC-2010) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:ADU34235.1, ECO:0000313|Proteomes:UP000008917}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=EPS {ECO:0000313|EMBL:ADU34235.1,
RC   ECO:0000313|Proteomes:UP000008917};
RX   PubMed=24158554;
RA   Han J.I., Spain J.C., Leadbetter J.R., Ovchinnikova G., Goodwin L.A.,
RA   Han C.S., Woyke T., Davenport K.W., Orwin P.M.;
RT   "Genome of the Root-Associated Plant Growth-Promoting Bacterium
RT   Variovorax paradoxus Strain EPS.";
RL   Genome Announc. 1:e00843-13(2013).
CC   -!- FUNCTION: Catalyzes the phosphatidyl group transfer from one
CC       phosphatidylglycerol molecule to another to form cardiolipin (CL)
CC       (diphosphatidylglycerol) and glycerol. {ECO:0000256|HAMAP-
CC       Rule:MF_01917}.
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;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01917};
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|HAMAP-
CC       Rule:MF_01917}; Peripheral membrane protein {ECO:0000256|HAMAP-
CC       Rule:MF_01917}.
CC   -!- SIMILARITY: Belongs to the phospholipase D family. Cardiolipin
CC       synthase subfamily. ClsB sub-subfamily. {ECO:0000256|HAMAP-
CC       Rule:MF_01917}.
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DR   EMBL; CP002417; ADU34235.1; -; Genomic_DNA.
DR   RefSeq; WP_013538482.1; NC_014931.1.
DR   STRING; 595537.Varpa_0012; -.
DR   EnsemblBacteria; ADU34235; ADU34235; Varpa_0012.
DR   GeneID; 29718977; -.
DR   KEGG; vpe:Varpa_0012; -.
DR   eggNOG; ENOG4105DZQ; Bacteria.
DR   eggNOG; COG1502; LUCA.
DR   HOGENOM; HOG000264393; -.
DR   KO; K06131; -.
DR   OMA; GEEYFPR; -.
DR   OrthoDB; 1881748at2; -.
DR   BioCyc; VPAR595537:G1GQO-12-MONOMER; -.
DR   Proteomes; UP000008917; 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   HAMAP; MF_01917; Cardiolipin_synth_ClsB; 1.
DR   InterPro; IPR030872; Cardiolipin_synth_ClsB.
DR   InterPro; IPR025202; PLD-like_dom.
DR   InterPro; IPR001736; PLipase_D/transphosphatidylase.
DR   Pfam; PF13091; PLDc_2; 2.
DR   SMART; SM00155; PLDc; 2.
DR   PROSITE; PS50035; PLD; 2.
PE   3: Inferred from homology;
DR   PRODOM; E6UXP1.
DR   SWISS-2DPAGE; E6UXP1.
KW   Cell membrane {ECO:0000256|HAMAP-Rule:MF_01917};
KW   Complete proteome {ECO:0000313|Proteomes:UP000008917};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01917};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01917};
KW   Membrane {ECO:0000256|HAMAP-Rule:MF_01917};
KW   Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01917};
KW   Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_01917};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008917};
KW   Repeat {ECO:0000256|SAAS:SAAS00723978};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_01917}.
FT   DOMAIN      110    137       PLD phosphodiesterase.
FT                                {ECO:0000259|PROSITE:PS50035}.
FT   DOMAIN      290    317       PLD phosphodiesterase.
FT                                {ECO:0000259|PROSITE:PS50035}.
FT   ACT_SITE    115    115       {ECO:0000256|HAMAP-Rule:MF_01917}.
FT   ACT_SITE    117    117       {ECO:0000256|HAMAP-Rule:MF_01917}.
FT   ACT_SITE    122    122       {ECO:0000256|HAMAP-Rule:MF_01917}.
FT   ACT_SITE    295    295       {ECO:0000256|HAMAP-Rule:MF_01917}.
FT   ACT_SITE    297    297       {ECO:0000256|HAMAP-Rule:MF_01917}.
FT   ACT_SITE    302    302       {ECO:0000256|HAMAP-Rule:MF_01917}.
SQ   SEQUENCE   423 AA;  48163 MW;  2FF9CF1847A18644 CRC64;
     MSHGNHWVGG NRIELLENGE EFFPRVFDAI RAAEREVIVE TFILFEDKVG LGLHAALREA
     AQRGAKVDLM IDGFGSPDLS REFIEGLTSV GVKVRVFDPG HRFMGQRLNV FRRMHRKIVV
     VDGERAFVGG INYSADHLLD FGPKAKQDWA VELAGPIVAE IHQFVLRAIA VGGKGAGWFR
     RRLKQAPPVR QLTAGEADAM FVTRDNRRHT NDIERHYRAA IRAARERIVI ANAYFFPGYR
     LIKELRRAAR RGVDVRLILQ GEPDMPIVKT AASMLYHHLL HAGVRIYEYC DRPLHGKVAL
     MDDRWSTVGS SNLDPLSLSL NLEANVVVRD KAFNEVLWKR MDQLMQESCK RIETTDLASE
     WSGWRLVRSF FIFHFLRWYP AWLDRLPRHV PRLTPAEATD LAERQKNEKN SNNTGGATPT
     EAA
//

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