ID R9SK26_9EURY Unreviewed; 396 AA.
AC R9SK26;
DT 18-SEP-2013, integrated into UniProtKB/TrEMBL.
DT 18-SEP-2013, sequence version 1.
DT 24-JAN-2024, entry version 49.
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=Abm4_1169 {ECO:0000313|EMBL:AGN17052.1};
OS Methanobrevibacter sp. AbM4.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=224719 {ECO:0000313|EMBL:AGN17052.1, ECO:0000313|Proteomes:UP000014066};
RN [1] {ECO:0000313|EMBL:AGN17052.1, ECO:0000313|Proteomes:UP000014066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AbM4 {ECO:0000313|EMBL:AGN17052.1};
RA Leahy S.C., Kelly W.J., Li D., Lambie S.C., Altermann E., Li Y.,
RA Attwood G.T.;
RL Submitted (JAN-2013) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AGN17052.1, ECO:0000313|Proteomes:UP000014066}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Abm4 {ECO:0000313|Proteomes:UP000014066};
RG Pastoral Greenhouse Gas Research Consortium;
RA Leahy S.C., Kelly W.J., Li D., Lambie S.C., Altermann E., Li Y.,
RA Attwood G.T.;
RT "The comlpete genome sequence of Methanobrevibacter sp. AbM4.";
RL Submitted (JUN-2013) 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 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: Lacks conserved residue(s) required for the propagation of
CC feature annotation. {ECO:0000256|HAMAP-Rule:MF_01287}.
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DR EMBL; CP004050; AGN17052.1; -; Genomic_DNA.
DR RefSeq; WP_016358751.1; NC_021355.1.
DR AlphaFoldDB; R9SK26; -.
DR STRING; 224719.Abm4_1169; -.
DR GeneID; 15798660; -.
DR KEGG; meb:Abm4_1169; -.
DR eggNOG; arCOG00570; Archaea.
DR HOGENOM; CLU_024648_0_0_2; -.
DR OrthoDB; 6062at2157; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000014066; 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; 3.30.9.10; 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 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:UP000014066}.
FT DOMAIN 4..324
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT BINDING 10..14
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01287"
FT BINDING 33..35
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01287"
FT BINDING 44..47
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01287"
FT BINDING 98
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
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 396 AA; 42811 MW; 4F9D716BF45D5652 CRC64;
MIDADIVVIG AGPAGSIAAK HAALRGAKVI LIDKKSEIGT PKRCAEGVYD PGLRLLGIEP
NPRWIAQTIY GGVLHSPDGN SIQFDEELLP VCGYVLERKV FDKYMAMDAA RAGAEIMIKT
FVSDLKREGD GFILDCDSFG EKFQIRAKIV IGADGPESTI GIKAGLNKHN SNKYMLSCAQ
YEMCNVELPR DDLIHIFLAD ENAEGGYAWI FTKGNGVANV GLGISSNIKD LDALECLDNF
VKSCPYTKNA QPVELNVGPD SLEGLKDNIY GDNIMLVGDA AGQIDPIEGG GILLGMYGGM
VAGNVAASAI KQGDYSADKL KEYYERFNQL TLNLVPKLTV VRDVVQSLNG DEFSNLIDAA
SQIDLANAST KDYLKVLFKI SPRTSLKFTK LIKVFI
//
