GGR_META3
ID GGR_META3 Reviewed; 391 AA.
AC A6UWL1;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 83.
DE RecName: Full=Digeranylgeranylglycerophospholipid reductase {ECO:0000255|HAMAP-Rule:MF_01287};
DE Short=DGGGPL reductase {ECO:0000255|HAMAP-Rule:MF_01287};
DE EC=1.3.-.- {ECO:0000255|HAMAP-Rule:MF_01287};
DE AltName: Full=2,3-bis-O-geranylgeranylglyceryl phosphate reductase {ECO:0000255|HAMAP-Rule:MF_01287};
DE AltName: Full=Geranylgeranyl reductase {ECO:0000255|HAMAP-Rule:MF_01287};
DE Short=GGR {ECO:0000255|HAMAP-Rule:MF_01287};
GN OrderedLocusNames=Maeo_1307;
OS Methanococcus aeolicus (strain ATCC BAA-1280 / DSM 17508 / OCM 812 /
OS Nankai-3).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=419665;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1280 / DSM 17508 / OCM 812 / Nankai-3;
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., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Lykidis A.,
RA Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of Methanococcus aeolicus Nankai-3.";
RL Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases.
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:0000255|HAMAP-
CC Rule:MF_01287}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=8 A + a 2,3-bis-O-phytanyl-sn-glycerol 1-phospholipid = a 2,3-
CC bis-O-(geranylgeranyl)-sn-glycerol 1-phospholipid + 8 AH2;
CC Xref=Rhea:RHEA:64376, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:138139, ChEBI:CHEBI:138140; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01287};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64378;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01287};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2,3-bis-O-(phytanyl)-sn-glycerol 1-phosphate + 8 A = 2,3-bis-
CC O-(geranylgeranyl)-sn-glycerol 1-phosphate + 8 AH2;
CC Xref=Rhea:RHEA:64368, ChEBI:CHEBI:13193, ChEBI:CHEBI:17499,
CC ChEBI:CHEBI:58837, ChEBI:CHEBI:73125; Evidence={ECO:0000255|HAMAP-
CC Rule:MF_01287};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64370;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01287};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01287};
CC Note=Binds 1 FAD per subunit. {ECO:0000255|HAMAP-Rule:MF_01287};
CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC {ECO:0000255|HAMAP-Rule:MF_01287}.
CC -!- MISCELLANEOUS: Reduction reaction proceeds via syn addition of hydrogen
CC for double bonds. {ECO:0000255|HAMAP-Rule:MF_01287}.
CC -!- SIMILARITY: Belongs to the geranylgeranyl reductase family. DGGGPL
CC reductase subfamily. {ECO:0000255|HAMAP-Rule:MF_01287}.
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DR EMBL; CP000743; ABR56883.1; -; Genomic_DNA.
DR RefSeq; WP_011974015.1; NC_009635.1.
DR AlphaFoldDB; A6UWL1; -.
DR SMR; A6UWL1; -.
DR STRING; 419665.Maeo_1307; -.
DR EnsemblBacteria; ABR56883; ABR56883; Maeo_1307.
DR GeneID; 5327399; -.
DR KEGG; mae:Maeo_1307; -.
DR eggNOG; arCOG00570; Archaea.
DR HOGENOM; CLU_024648_0_0_2; -.
DR OMA; GMCRREV; -.
DR OrthoDB; 31233at2157; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000001106; Chromosome.
DR GO; GO:0050660; F:flavin adenine dinucleotide binding; IEA:UniProtKB-UniRule.
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; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR011777; Geranylgeranyl_Rdtase_fam.
DR SUPFAM; SSF51905; SSF51905; 1.
DR TIGRFAMs; TIGR02032; GG-red-SF; 1.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Lipid biosynthesis; Lipid metabolism; Oxidoreductase;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome.
FT CHAIN 1..391
FT /note="Digeranylgeranylglycerophospholipid reductase"
FT /id="PRO_0000351452"
FT BINDING 15..19
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01287"
FT BINDING 38..40
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01287"
FT BINDING 49..52
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01287"
FT BINDING 99
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01287"
FT BINDING 206..212
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01287"
FT BINDING 279
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01287"
FT BINDING 287..290
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01287"
FT BINDING 291..292
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01287"
SQ SEQUENCE 391 AA; 42781 MW; 2836F8C2191ED66D CRC64;
MRELLDSEYD VIVIGAGPGG SMASYHSSIN GAKTLLIDKS QEIGTPVRCA EAVPYLDEFG
INPDPSFIRS KIDGGILVAP NGKKIIVKGG KTQGYVVERK IFDKHLAVRS ANVGTKIAIK
SRVVGLDYDG EKYTVIVNHL GQIYAIKAKI VIAADGVESS IAEMAGIKCK KKVTEICSCA
EYEMTNVKLL DKNMMEFYFG DICPKGYVWI FPKGETANVG LGIIDSKKKA IDYLNEFLEH
PLLEGRLDNA TPIEFKCGGA PVGGPIEKTV ADNFMVVGDA AGQISPISGG GIYLSLSCGS
IAGKVAGEAI KSNNCSEDYL VEYENRWKEK YYKLLMDELK YKKVLQKFSE KELNALADAM
DERLEEIDVA KIAFRAVKRA PSLLKYFKDI I
