ID A0A0U3DT93_9EURY Unreviewed; 392 AA.
AC A0A0U3DT93;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 34.
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=sm9_1381 {ECO:0000313|EMBL:ALT69162.1};
OS Methanobrevibacter millerae.
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=230361 {ECO:0000313|EMBL:ALT69162.1, ECO:0000313|Proteomes:UP000067738};
RN [1] {ECO:0000313|EMBL:ALT69162.1, ECO:0000313|Proteomes:UP000067738}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SM9 {ECO:0000313|EMBL:ALT69162.1,
RC ECO:0000313|Proteomes:UP000067738};
RA Leahy S.C., Kelly W.J., Pacheco D.M., Li D., Altermann E., Attwood G.T.;
RT "The complete genome sequence of the rumen methanogen Methanobrevibacter
RT millerae SM9.";
RL Submitted (APR-2015) 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}.
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DR EMBL; CP011266; ALT69162.1; -; Genomic_DNA.
DR RefSeq; WP_058739414.1; NZ_CP011266.1.
DR AlphaFoldDB; A0A0U3DT93; -.
DR GeneID; 26736329; -.
DR KEGG; mmil:sm9_1381; -.
DR PATRIC; fig|230361.4.peg.1425; -.
DR OrthoDB; 6062at2157; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000067738; 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}.
FT DOMAIN 3..328
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 100
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01287"
FT BINDING 207..213
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01287"
FT BINDING 280
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01287"
FT BINDING 288..291
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01287"
FT BINDING 292..293
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01287"
SQ SEQUENCE 392 AA; 42422 MW; A6EE8EA55DF8D828 CRC64;
MIETDVIVVG AGPAGSTAAK HAALGGAKVI LMDKKSEIGA PKRCAEGVSI QGLEKLGIEP
SPRFVTQEIQ GVRLQAPDGT DVWLTKDEVQ LPEAGYILER KVFDKFMAMD AARAGAEIKI
KTLVTGIDKI DNGYIVETES MGKQETYKCK ILIAADGPEG HIARWAGLKP AAKAKEMESG
VQYEMCNVEF ERPGVIEFYF GSCAPGGYVW IFPKGDDIAN IGLAVLPHMA EKPAIEYLDD
FIAKCPYTQN AQAVELNVGG DPVGGMTKKL YDDNIMVVGD AAGQVNPLTG GGIISGMTGG
MCAGQVAAEA IKEDCSKKFL KQYDQMAHDE LDYEIKRYKK VQEYLLTLSD EELDSIAHAF
EGESFEKIST TEIVKKLIKI SPKALLKLGK FI
//
