(data stored in SCRATCH zone)

SWISSPROT: D1YVV4_METPS

ID   D1YVV4_METPS            Unreviewed;       392 AA.
AC   D1YVV4;
DT   09-FEB-2010, integrated into UniProtKB/TrEMBL.
DT   09-FEB-2010, sequence version 1.
DT   11-DEC-2019, entry version 60.
DE   RecName: Full=Digeranylgeranylglycerophospholipid reductase {ECO:0000256|HAMAP-Rule:MF_01287};
DE            Short=DGGGPL reductase {ECO:0000256|HAMAP-Rule:MF_01287};
DE            EC=1.3.7.11 {ECO:0000256|HAMAP-Rule:MF_01287};
DE   AltName: Full=2,3-bis-O-geranylgeranylglyceryl phosphate reductase {ECO:0000256|HAMAP-Rule:MF_01287};
DE   AltName: Full=Geranylgeranyl reductase {ECO:0000256|HAMAP-Rule:MF_01287};
DE            Short=GGR {ECO:0000256|HAMAP-Rule:MF_01287};
GN   OrderedLocusNames=MCP_0504 {ECO:0000313|EMBL:BAI60576.1};
OS   Methanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 /
OS   SANAE).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanocellales; Methanocellaceae; Methanocella.
OX   NCBI_TaxID=304371 {ECO:0000313|EMBL:BAI60576.1, ECO:0000313|Proteomes:UP000001882};
RN   [1] {ECO:0000313|Proteomes:UP000001882}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 17711 / JCM 13418 / NBRC 101707 / SANAE
RC   {ECO:0000313|Proteomes:UP000001882};
RX   PubMed=21829548; DOI=10.1371/journal.pone.0022898;
RA   Sakai S., Takaki Y., Shimamura S., Sekine M., Tajima T., Kosugi H.,
RA   Ichikawa N., Tasumi E., Hiraki A.T., Shimizu A., Kato Y., Nishiko R.,
RA   Mori K., Fujita N., Imachi H., Takai K.;
RT   "Genome sequence of a mesophilic hydrogenotrophic methanogen Methanocella
RT   paludicola, the first cultivated representative of the order
RT   Methanocellales.";
RL   PLoS ONE 6:E22898-E22898(2011).
CC   -!- FUNCTION: Is involved in the reduction of 2,3-
CC       digeranylgeranylglycerophospholipids (unsaturated archaeols) into 2,3-
CC       diphytanylglycerophospholipids (saturated archaeols) in the
CC       biosynthesis of archaeal membrane lipids. Catalyzes the formation of
CC       archaetidic acid (2,3-di-O-phytanyl-sn-glyceryl phosphate) from 2,3-di-
CC       O-geranylgeranylglyceryl phosphate (DGGGP) via the hydrogenation of
CC       each double bond of the isoprenoid chains. {ECO:0000256|HAMAP-
CC       Rule:MF_01287}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=a 2,3-bis-O-phytanyl-sn-glycerol 1-phospholipid + 16 oxidized
CC         [2Fe-2S]-[ferredoxin] = a 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-
CC         phospholipid + 16 H(+) + 16 reduced [2Fe-2S]-[ferredoxin];
CC         Xref=Rhea:RHEA:54324, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738,
CC         ChEBI:CHEBI:138139, ChEBI:CHEBI:138140; EC=1.3.7.11;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01287};
CC   -!- COFACTOR:
CC       Name=FAD; Xref=ChEBI:CHEBI:57692;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01287};
CC       Note=Binds 1 FAD per subunit. {ECO:0000256|HAMAP-Rule:MF_01287};
CC   -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC       {ECO:0000256|HAMAP-Rule:MF_01287}.
CC   -!- MISCELLANEOUS: Reduction reaction proceeds via syn addition of hydrogen
CC       for double bonds. {ECO:0000256|HAMAP-Rule:MF_01287}.
CC   -!- SIMILARITY: Belongs to the geranylgeranyl reductase family. DGGGPL
CC       reductase subfamily. {ECO:0000256|HAMAP-Rule:MF_01287}.
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DR   EMBL; AP011532; BAI60576.1; -; Genomic_DNA.
DR   STRING; 304371.MCP_0504; -.
DR   EnsemblBacteria; BAI60576; BAI60576; MCP_0504.
DR   KEGG; mpd:MCP_0504; -.
DR   PATRIC; fig|304371.9.peg.518; -.
DR   eggNOG; arCOG00570; Archaea.
DR   eggNOG; COG0644; LUCA.
DR   HOGENOM; HOG000226367; -.
DR   KO; K17830; -.
DR   OMA; KPNRYTI; -.
DR   BioCyc; MPAL304371:GI7G-518-MONOMER; -.
DR   UniPathway; UPA00940; -.
DR   Proteomes; UP000001882; Chromosome.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0045550; F:geranylgeranyl reductase activity; IEA:InterPro.
DR   GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IEA:InterPro.
DR   GO; GO:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0046467; P:membrane lipid biosynthetic process; IEA:InterPro.
DR   GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.50.50.60; -; 1.
DR   HAMAP; MF_01287; DGGGPL_reductase; 1.
DR   InterPro; IPR023590; DGGGPL_reductase.
DR   InterPro; IPR002938; FAD-bd.
DR   InterPro; IPR036188; FAD/NAD-bd_sf.
DR   InterPro; IPR011777; Geranylgeranyl_Rdtase_fam.
DR   Pfam; PF01494; FAD_binding_3; 1.
DR   SUPFAM; SSF51905; SSF51905; 1.
DR   TIGRFAMs; TIGR02032; GG-red-SF; 1.
PE   3: Inferred from homology;
DR   PRODOM; D1YVV4.
DR   SWISS-2DPAGE; D1YVV4.
KW   FAD {ECO:0000256|HAMAP-Rule:MF_01287};
KW   Flavoprotein {ECO:0000256|HAMAP-Rule:MF_01287};
KW   Lipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01287};
KW   Lipid metabolism {ECO:0000256|HAMAP-Rule:MF_01287};
KW   NAD {ECO:0000256|HAMAP-Rule:MF_01287};
KW   Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01287};
KW   Phospholipid biosynthesis {ECO:0000256|HAMAP-Rule:MF_01287};
KW   Phospholipid metabolism {ECO:0000256|HAMAP-Rule:MF_01287};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001882}.
FT   DOMAIN          100..329
FT                   /note="FAD_binding_3"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
FT   NP_BIND         11..15
FT                   /note="FAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01287"
FT   NP_BIND         34..36
FT                   /note="FAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01287"
FT   NP_BIND         45..48
FT                   /note="FAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01287"
FT   NP_BIND         291..292
FT                   /note="FAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01287"
FT   REGION          207..213
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01287"
FT   REGION          287..290
FT                   /note="Substrate binding"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01287"
FT   BINDING         99
FT                   /note="FAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01287"
FT   BINDING         279
FT                   /note="FAD"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01287"
SQ   SEQUENCE   392 AA;  42320 MW;  419CB75708107B1F CRC64;
     MKSNYDVIVV GAGPAGSIAA RTAAEQGLDV LLIEKRQEIG DPVRCAEGTG KMGLSQFIEP
     DPRWICAEVT GARIFAPDGT CIELNEKLAG KEVGYVLERK IFDRAVAKTA ARAGAEVQVK
     TQATSLIKEN GVVCGIKGKH RGEDFEARAK VVVGADGIES KVGKWAGINT TLKPKDIETC
     AQFLVTDIDI RADSCDFYMG NLRAPGGYVW IFPKGKREAN VGLGMLGSRF TGKHPIDYLH
     EFMAWKFPEG KIIETVVGAV PASGMLKQLS TSGLVLVGDA GRVSDPITGG GIYNGMVSGR
     IAGNVLADAI KANDLSVKKL QRYDREVREA LGKQLDRNYK AKEFVVKAED SLMNSVARSL
     HGVNFEEMSV PKLLKEIITR NPSMFLELAG LF
//

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