GGR_PYRAB
ID GGR_PYRAB Reviewed; 393 AA.
AC Q9V2B0; G8ZFZ9;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 126.
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=PYRAB01640; ORFNames=PAB0109;
OS Pyrococcus abyssi (strain GE5 / Orsay).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=272844;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GE5 / Orsay;
RX PubMed=12622808; DOI=10.1046/j.1365-2958.2003.03381.x;
RA Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O.,
RA Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J.,
RA Weissenbach J., Zivanovic Y., Forterre P.;
RT "An integrated analysis of the genome of the hyperthermophilic archaeon
RT Pyrococcus abyssi.";
RL Mol. Microbiol. 47:1495-1512(2003).
RN [2]
RP GENOME REANNOTATION.
RC STRAIN=GE5 / Orsay;
RX PubMed=22057919; DOI=10.1007/s00284-011-0035-x;
RA Gao J., Wang J.;
RT "Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and
RT Pyrococcus furiosus DSM 3638.";
RL Curr. Microbiol. 64:118-129(2012).
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}.
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; AJ248283; CAB49088.1; -; Genomic_DNA.
DR EMBL; HE613800; CCE69540.1; -; Genomic_DNA.
DR PIR; A75205; A75205.
DR RefSeq; WP_010867288.1; NC_000868.1.
DR AlphaFoldDB; Q9V2B0; -.
DR SMR; Q9V2B0; -.
DR STRING; 272844.PAB0109; -.
DR EnsemblBacteria; CAB49088; CAB49088; PAB0109.
DR GeneID; 1495051; -.
DR KEGG; pab:PAB0109; -.
DR PATRIC; fig|272844.11.peg.179; -.
DR eggNOG; arCOG00570; Archaea.
DR HOGENOM; CLU_024648_0_0_2; -.
DR OMA; GMCRREV; -.
DR OrthoDB; 31233at2157; -.
DR PhylomeDB; Q9V2B0; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000000810; Chromosome.
DR Proteomes; UP000009139; 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;
KW FAD; Flavoprotein; Lipid biosynthesis; Lipid metabolism; Oxidoreductase;
KW Phospholipid biosynthesis; Phospholipid metabolism.
FT CHAIN 1..393
FT /note="Digeranylgeranylglycerophospholipid reductase"
FT /id="PRO_0000351475"
FT BINDING 9..13
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01287"
FT BINDING 32..34
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01287"
FT BINDING 43..46
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01287"
FT BINDING 95
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01287"
FT BINDING 203..209
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01287"
FT BINDING 274
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01287"
FT BINDING 282..285
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01287"
FT BINDING 286..287
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01287"
SQ SEQUENCE 393 AA; 43835 MW; D8F63109BBCBE532 CRC64;
MKYDVVVVGS GVAGPTVARD VAKAGFSVLL VDKKAAIGTP KQCAEGITIE VFKEFDIPYD
KRFINREIYG AKIYSPSGYT AELRYKHVSG VILERKVFDK MLAYYAAKAG AEVLARTEVV
DVIRRNGKIV GVRAKHEGEP LEIEAKVIVA ADGVESTIAR KAGINTYAPP HEFDSGYEYE
MLIEGYDPDL IHLFFGNEVA PRGYVWIFPK DEDRANVGIG IASDHPQTAK YYLDKWLKEN
NIPMRKILEV NVGLVPVGGF VKELVKDNVL VVGDAARQVN PVHGGGMKEA MKAASIAAKW
IIKALEEENL ELLKNYSEEW WRTEGPRMEK LLKLRKAMEK LTDEDLDVFV QLVSGTDLEK
LAGGNYLEVV KALMKHPKVL MSRRRLEILK ALL
