ID H1YX47_9EURY Unreviewed; 399 AA.
AC H1YX47;
DT 21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2012, sequence version 1.
DT 24-JAN-2024, entry version 57.
DE RecName: Full=Digeranylgeranylglycerophospholipid reductase {ECO:0000256|HAMAP-Rule:MF_01287};
DE Short=DGGGPL reductase {ECO:0000256|HAMAP-Rule:MF_01287};
DE EC=1.3.7.11 {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=Metlim_1749 {ECO:0000313|EMBL:EHQ35850.1};
OS Methanoplanus limicola DSM 2279.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanomicrobiales; Methanomicrobiaceae; Methanoplanus.
OX NCBI_TaxID=937775 {ECO:0000313|EMBL:EHQ35850.1, ECO:0000313|Proteomes:UP000005741};
RN [1] {ECO:0000313|EMBL:EHQ35850.1, ECO:0000313|Proteomes:UP000005741}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 2279 {ECO:0000313|EMBL:EHQ35850.1,
RC ECO:0000313|Proteomes:UP000005741};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Peters L., Mikhailova N., Lu M.,
RA Kyrpides N., Mavromatis K., Ivanova N., Markowitz V., Cheng J.-F.,
RA Hugenholtz P., Woyke T., Wu D., Wirth R., Brambilla E.-M., Klenk H.-P.,
RA Eisen J.A.;
RT "The Improved High-Quality Draft genome of Methanoplanus limicola DSM
RT 2279.";
RL Submitted (OCT-2011) to the EMBL/GenBank/DDBJ databases.
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 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:0000256|HAMAP-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:0000256|HAMAP-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}.
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DR EMBL; CM001436; EHQ35850.1; -; Genomic_DNA.
DR RefSeq; WP_004077774.1; NZ_CM001436.1.
DR AlphaFoldDB; H1YX47; -.
DR STRING; 937775.Metlim_1749; -.
DR PATRIC; fig|937775.9.peg.1962; -.
DR HOGENOM; CLU_024648_0_0_2; -.
DR InParanoid; H1YX47; -.
DR OrthoDB; 6062at2157; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000005741; 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; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 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 NCBIfam; TIGR02032; GG-red-SF; 1.
DR PANTHER; PTHR42685:SF18; DIGERANYLGERANYLGLYCEROPHOSPHOLIPID REDUCTASE; 1.
DR PANTHER; PTHR42685; GERANYLGERANYL DIPHOSPHATE REDUCTASE; 1.
DR Pfam; PF01494; FAD_binding_3; 1.
DR Pfam; PF12831; FAD_oxidored; 1.
DR PRINTS; PR00420; RNGMNOXGNASE.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 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};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW 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}; Reference proteome {ECO:0000313|Proteomes:UP000005741}.
FT DOMAIN 103..298
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT BINDING 11..15
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01287"
FT BINDING 34..36
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01287"
FT BINDING 45..48
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01287"
FT BINDING 100
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01287"
FT BINDING 208..214
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01287"
FT BINDING 281
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01287"
FT BINDING 289..292
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01287"
FT BINDING 293..294
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01287"
SQ SEQUENCE 399 AA; 43547 MW; CCDF514D56146D31 CRC64;
MKSEYDVLII GGGPGGALAA KTAAEKGLSV ALAEKRPAIG APVRCAEGIG EDLICEFFDE
IDPKWISAKI EGAKLIAPDG SYFYLNPEMA GNEVGFVLDR KFFDRDLIWQ AVHAGAEIFV
KARAVGAIVE NGVVCGAKIE YNGEVREVRA KITIAADGVE SKFTRWCGID TTVPLREMET
CAQYLMTDIN IEPNITVFHV GREIAPEGYL WIFPKGHRSA NVGIGISGTQ SGDGQRAKDY
LDRYVSENFP EGKIIEQIAG GVSVCEPLEC TVSDGLMIIG DAARISDPMT GGGIYNAMYT
GRLAAEVASK CIESGDLSKE ALMEYDSVWR DSKMGRALER NYQMKEIFVK LTDKQLNAIL
TSVKNLKMAD FSTLSLVKEI VKLNPKLIKD LTGLKKYFE
//
