GGR_PYRHO
ID GGR_PYRHO Reviewed; 393 AA.
AC O57920;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1998, sequence version 1.
DT 03-AUG-2022, entry version 131.
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=PH0181;
OS Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC
OS 100139 / OT-3).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Pyrococcus.
OX NCBI_TaxID=70601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3;
RX PubMed=9679194; DOI=10.1093/dnares/5.2.55;
RA Kawarabayasi Y., Sawada M., Horikawa H., Haikawa Y., Hino Y., Yamamoto S.,
RA Sekine M., Baba S., Kosugi H., Hosoyama A., Nagai Y., Sakai M., Ogura K.,
RA Otsuka R., Nakazawa H., Takamiya M., Ohfuku Y., Funahashi T., Tanaka T.,
RA Kudoh Y., Yamazaki J., Kushida N., Oguchi A., Aoki K., Yoshizawa T.,
RA Nakamura Y., Robb F.T., Horikoshi K., Masuchi Y., Shizuya H., Kikuchi H.;
RT "Complete sequence and gene organization of the genome of a hyper-
RT thermophilic archaebacterium, Pyrococcus horikoshii OT3.";
RL DNA Res. 5:55-76(1998).
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; BA000001; BAA29250.1; -; Genomic_DNA.
DR PIR; C71240; C71240.
DR RefSeq; WP_010884290.1; NC_000961.1.
DR AlphaFoldDB; O57920; -.
DR SMR; O57920; -.
DR STRING; 70601.3256567; -.
DR DNASU; 1444072; -.
DR EnsemblBacteria; BAA29250; BAA29250; BAA29250.
DR GeneID; 1444072; -.
DR KEGG; pho:PH0181; -.
DR eggNOG; arCOG00570; Archaea.
DR OMA; GMCRREV; -.
DR OrthoDB; 31233at2157; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000000752; 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.
FT CHAIN 1..393
FT /note="Digeranylgeranylglycerophospholipid reductase"
FT /id="PRO_0000351477"
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; 43929 MW; 6BEC7E0B71C0D48C CRC64;
MRYDVVVVGS GVAGPIVARN VAKAGFSVLL VDKKPAIGAP KQCAEGLTIN AFKQFDIPYD
KRFINREIYG AKIYSPSGYT AELRYKEVSG VILERKVFDK MLAYYAAKAG AEVLARTEVV
DVIRREGKIV GVKAKHEGEP MEIEAKVIVA ADGVESTIAR KAGIDTYAPP HEFDSGYEYE
MIIEGFDPDL IHLFFGNEVA PRGYVWVFPK DEDRANVGIG INSDNEKTAK YYLDKWLKEN
NIPRNKILEV NVGLIPVGGF VKELVKENVL VVGDAARQVN PIHGGGMAEA MKASTIASKW
IIKALEEENL ELLKNYKEEW WKTEGPRMEK LLRLRRAMEK LTDEDLDVFV QLVSGTDLEK
IAGGNYIEVV KALMKHPKVL MSRRRLEILK ALL
