GGR_PICTO
ID GGR_PICTO Reviewed; 397 AA.
AC Q6L0M1;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Digeranylgeranylglycerophospholipid reductase {ECO:0000255|HAMAP-Rule:MF_01287};
DE Short=DGGGPL reductase {ECO:0000255|HAMAP-Rule:MF_01287};
DE EC=1.3.1.101 {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=PTO0896;
OS Picrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC
OS 100828).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Picrophilaceae; Picrophilus.
OX NCBI_TaxID=263820;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828;
RX PubMed=15184674; DOI=10.1073/pnas.0401356101;
RA Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C.,
RA Schepers B., Dock C., Antranikian G., Liebl W.;
RT "Genome sequence of Picrophilus torridus and its implications for life
RT around pH 0.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004).
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=2,3-bis-O-(phytanyl)-sn-glycerol 1-phosphate + 8 NADP(+) =
CC 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + 8 H(+) + 8
CC NADPH; Xref=Rhea:RHEA:36035, ChEBI:CHEBI:15378, ChEBI:CHEBI:57783,
CC ChEBI:CHEBI:58349, ChEBI:CHEBI:58837, ChEBI:CHEBI:73125;
CC EC=1.3.1.101; Evidence={ECO:0000255|HAMAP-Rule:MF_01287};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:36037;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01287};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2,3-bis-O-(phytanyl)-sn-glycerol 1-phosphate + 8 NAD(+) = 2,3-
CC bis-O-(geranylgeranyl)-sn-glycerol 1-phosphate + 8 H(+) + 8 NADH;
CC Xref=Rhea:RHEA:36039, ChEBI:CHEBI:15378, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945, ChEBI:CHEBI:58837, ChEBI:CHEBI:73125;
CC EC=1.3.1.101; Evidence={ECO:0000255|HAMAP-Rule:MF_01287};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:36041;
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; AE017261; AAT43481.1; -; Genomic_DNA.
DR RefSeq; WP_011177697.1; NC_005877.1.
DR AlphaFoldDB; Q6L0M1; -.
DR SMR; Q6L0M1; -.
DR STRING; 263820.PTO0896; -.
DR EnsemblBacteria; AAT43481; AAT43481; PTO0896.
DR GeneID; 2844118; -.
DR KEGG; pto:PTO0896; -.
DR PATRIC; fig|263820.9.peg.934; -.
DR eggNOG; arCOG00570; Archaea.
DR HOGENOM; CLU_024648_0_0_2; -.
DR OMA; CSCAQYE; -.
DR OrthoDB; 31233at2157; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000000438; Chromosome.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0045550; F:geranylgeranyl reductase activity; IEA:InterPro.
DR GO; GO:0051287; F:NAD binding; IEA:UniProtKB-UniRule.
DR GO; GO:0050661; F:NADP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016628; F:oxidoreductase activity, acting on the CH-CH group of donors, NAD or NADP as acceptor; IEA:UniProtKB-UniRule.
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; NAD; NADP;
KW Oxidoreductase; Phospholipid biosynthesis; Phospholipid metabolism;
KW Reference proteome.
FT CHAIN 1..397
FT /note="Digeranylgeranylglycerophospholipid reductase"
FT /id="PRO_0000351474"
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 101
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01287"
FT BINDING 209..215
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01287"
FT BINDING 284
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01287"
FT BINDING 292..295
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01287"
FT BINDING 296..297
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01287"
SQ SEQUENCE 397 AA; 43748 MW; CCC07B962BEB6398 CRC64;
MEVNYDVLVI GAGPAGSSAA RFAARKGLKT LLIEKRPDIG SPVRCGEGVS KSWMPEVELK
PEDHWISDEV KGARIYGPSE KKPIMLTAEN AGNEVGYVVE RDKFDKHIAA LAASEGADVW
VKSPALSVIK DGNRIVGAKV RHNSEIVDVR AKMVIAADGF ESEFGRWAGL KSLILAKNDI
ISCVEYRMIN VDSDEDYTDF YLGSCAPAGY IWVFPKGKHE ANVGIGVTIS KMRDRFDVKN
YLDAFIKSHP GYSKGKTIQL ITGGVSVSKV RDKFTLPGLL TVGDAARLID PITGGGIANG
MISGKYAAEV SKKAIDNEDY SQEMMNNYER MVKDKFERKH LRNWFAKEKL GTLSDETLDK
LVDVIADVKI NEISVEEILK AVQLKYPELV EELESLI
