ID A0A833DPH2_9EURY Unreviewed; 392 AA. AC A0A833DPH2; DT 29-SEP-2021, integrated into UniProtKB/TrEMBL. DT 29-SEP-2021, sequence version 1. DT 12-OCT-2022, entry version 5. 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.-.- {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 ORFNames=EYG77_04445 {ECO:0000313|EMBL:HIP16434.1}; OS Methanothermococcus okinawensis. OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales; OC Methanococcaceae; Methanothermococcus. OX NCBI_TaxID=155863 {ECO:0000313|EMBL:HIP16434.1, ECO:0000313|Proteomes:UP000609164}; RN [1] {ECO:0000313|EMBL:HIP16434.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=SZUA-1388 {ECO:0000313|EMBL:HIP16434.1}; RX PubMed=32820229; RA Zhou Z., Liu Y., Pan J., Cron B.R., Toner B.M., Anantharaman K., RA Breier J.A., Dick G.J., Li M.; RT "Gammaproteobacteria mediating utilization of methyl-, sulfur- and RT petroleum organic compounds in deep ocean hydrothermal plumes."; RL ISME J. 14:3136-3148(2020). 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=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:0000256|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:0000256|HAMAP- CC 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}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:HIP16434.1}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DQSW01000202; HIP16434.1; -; Genomic_DNA. DR UniPathway; UPA00940; -. DR Proteomes; UP000609164; Unassembled WGS sequence. 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 {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|HAMAP-Rule:MF_01287}; KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630, ECO:0000256|HAMAP- KW Rule:MF_01287}; KW Lipid biosynthesis {ECO:0000256|ARBA:ARBA00022516, ECO:0000256|HAMAP- KW Rule:MF_01287}; KW Lipid metabolism {ECO:0000256|ARBA:ARBA00023098, ECO:0000256|HAMAP- KW Rule:MF_01287}; Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01287}; KW Phospholipid biosynthesis {ECO:0000256|ARBA:ARBA00023209, KW ECO:0000256|HAMAP-Rule:MF_01287}; KW Phospholipid metabolism {ECO:0000256|ARBA:ARBA00023264, ECO:0000256|HAMAP- KW Rule:MF_01287}. FT BINDING 15..19 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01287" FT BINDING 38..40 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01287" FT BINDING 49..52 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01287" FT BINDING 99 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01287" FT BINDING 206..212 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01287" FT BINDING 279 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01287" FT BINDING 287..290 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01287" FT BINDING 291..292 FT /ligand="FAD" FT /ligand_id="ChEBI:CHEBI:57692" FT /evidence="ECO:0000256|HAMAP-Rule:MF_01287" SQ SEQUENCE 392 AA; 43731 MW; 58625A5753FD7BED CRC64; MRWVLKDEYD VVVVGAGPAG SMASYYASKN GVKTLLVEKS QEIGEPVRCA EAIPKLEEFN IPLSEEFVRS YIKGGYLIAP NGKKVEIRGS KTEGYVVERK IFDKYLAIRS AKVGTKIAVK SRVVDLYPYK DGFKVKVIHL GEEYTVKTKI VIAADGMESS VAEMVGLRCK KNPMEVCSCA EYEMTGVKLL DKHMMEFYFG DLSPKGYAWI FPKGDTANVG LGVIDKSKKA IDYLNEFLEH PILEDRLKDA TPVEFKCGGV PVGGPIERTV DDNIMVVGDA AGQVSPLTGG GIYLAMSCGS IAGEVASKAV KKEDYSKETL MEYERRWKEK FYNTLMTELK YKNILQKLNE EDLNIIAEVI DDKLEDIDVK KIIFKVIKKA PSLLKYFKDI IG //