GGR_METLZ
ID GGR_METLZ Reviewed; 397 AA.
AC A2SQK1;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Digeranylgeranylglycerophospholipid reductase {ECO:0000255|HAMAP-Rule:MF_01287};
DE Short=DGGGPL reductase {ECO:0000255|HAMAP-Rule:MF_01287};
DE EC=1.3.7.11 {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=Mlab_0431;
OS Methanocorpusculum labreanum (strain ATCC 43576 / DSM 4855 / Z).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanocorpusculaceae; Methanocorpusculum.
OX NCBI_TaxID=410358;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43576 / DSM 4855 / Z;
RX PubMed=21304657; DOI=10.4056/sigs.35575;
RA Anderson I.J., Sieprawska-Lupa M., Goltsman E., Lapidus A., Copeland A.,
RA Glavina Del Rio T., Tice H., Dalin E., Barry K., Pitluck S., Hauser L.,
RA Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.;
RT "Complete genome sequence of Methanocorpusculum labreanum type strain Z.";
RL Stand. Genomic Sci. 1:197-203(2009).
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=a 2,3-bis-O-phytanyl-sn-glycerol 1-phospholipid + 8 oxidized
CC 2[4Fe-4S]-[ferredoxin] = a 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-
CC phospholipid + 16 H(+) + 8 reduced 2[4Fe-4S]-[ferredoxin];
CC Xref=Rhea:RHEA:54324, Rhea:RHEA-COMP:10002, Rhea:RHEA-COMP:10004,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33722, ChEBI:CHEBI:33723,
CC ChEBI:CHEBI:138139, ChEBI:CHEBI:138140; EC=1.3.7.11;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01287};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:54326;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01287};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2,3-bis-O-(phytanyl)-sn-glycerol 1-phosphate + 8 oxidized
CC 2[4Fe-4S]-[ferredoxin] = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-
CC phosphate + 16 H(+) + 8 reduced 2[4Fe-4S]-[ferredoxin];
CC Xref=Rhea:RHEA:36159, Rhea:RHEA-COMP:10002, Rhea:RHEA-COMP:10004,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33722, ChEBI:CHEBI:33723,
CC ChEBI:CHEBI:58837, ChEBI:CHEBI:73125; EC=1.3.7.11;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01287};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:36161;
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; CP000559; ABN06607.1; -; Genomic_DNA.
DR RefSeq; WP_011832808.1; NC_008942.1.
DR AlphaFoldDB; A2SQK1; -.
DR SMR; A2SQK1; -.
DR STRING; 410358.Mlab_0431; -.
DR EnsemblBacteria; ABN06607; ABN06607; Mlab_0431.
DR GeneID; 4794769; -.
DR KEGG; mla:Mlab_0431; -.
DR eggNOG; arCOG00570; Archaea.
DR HOGENOM; CLU_024648_0_0_2; -.
DR OMA; SLCDPFL; -.
DR OrthoDB; 31233at2157; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000000365; Chromosome.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0045550; F:geranylgeranyl reductase activity; IEA:InterPro.
DR GO; GO:0016636; F:oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor; IEA:UniProtKB-UniRule.
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;
KW FAD; Flavoprotein; Lipid biosynthesis; Lipid metabolism; Oxidoreductase;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome.
FT CHAIN 1..397
FT /note="Digeranylgeranylglycerophospholipid reductase"
FT /id="PRO_0000351460"
FT BINDING 11..15
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01287"
FT BINDING 34..36
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01287"
FT BINDING 45..48
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 207..213
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01287"
FT BINDING 280
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01287"
FT BINDING 288..291
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01287"
FT BINDING 292..293
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01287"
SQ SEQUENCE 397 AA; 42483 MW; AAE8D34EEFA6048E CRC64;
MKEAYDVLVV GGGPGGALAA KAAAEQGLSV LLVEKRPAIG APVRCAEGIG KEALAEFIEP
DPKWIAADLD KAVLIGPDGT KFTIGDSHSG GKVGYVLDRK VFDRELVWQA AEAGAEIQVH
ARASAPIMID GKVSGAVIHQ HGKTYEVRAK VIIAADGVES KFAKWAGINT TVPLAELETC
AQYIVNDIDI DERANLFYFS YTDAPWGYIW VFPKGHRCAN VGIGIAGTKS GEGHRAKDYL
DRFIAREFPN GKVTELIVGG VSVCKPLDCT VADNLIIVGD AARLSDPITG GGIYNAMYTG
KLAGEVAAAA LKKGDTSKKA LMVYDNTWRE GPLGHALARN YAVKESFIKM DDAKFNSIVH
SMSDLSLDEI TVKSLVIAIF KANPWLALEL PRLLMTL
