GGR_THEAC
ID GGR_THEAC Reviewed; 396 AA.
AC Q9HKS9;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=Digeranylgeranylglycerophospholipid reductase;
DE Short=DGGGPL reductase;
DE EC=1.3.1.101 {ECO:0000269|PubMed:16788058};
DE AltName: Full=2,3-bis-O-geranylgeranylglyceryl phosphate reductase;
DE AltName: Full=Geranylgeranyl reductase;
DE Short=GGR;
GN OrderedLocusNames=Ta0516;
OS Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC
OS 15155 / AMRC-C165).
OC Archaea; Candidatus Thermoplasmatota; Thermoplasmata; Thermoplasmatales;
OC Thermoplasmataceae; Thermoplasma.
OX NCBI_TaxID=273075;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=11029001; DOI=10.1038/35035069;
RA Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C.,
RA Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.;
RT "The genome sequence of the thermoacidophilic scavenger Thermoplasma
RT acidophilum.";
RL Nature 407:508-513(2000).
RN [2]
RP PROTEIN SEQUENCE OF 1-20, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=16788058; DOI=10.1093/jb/mvj118;
RA Nishimura Y., Eguchi T.;
RT "Biosynthesis of archaeal membrane lipids:
RT digeranylgeranylglycerophospholipid reductase of the thermoacidophilic
RT archaeon Thermoplasma acidophilum.";
RL J. Biochem. 139:1073-1081(2006).
RN [3]
RP FUNCTION, COFACTOR, AND REACTION STEREOCHEMISTRY.
RC STRAIN=ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165;
RX PubMed=17275067; DOI=10.1016/j.bioorg.2006.12.001;
RA Nishimura Y., Eguchi T.;
RT "Stereochemistry of reduction in digeranylgeranylglycerophospholipid
RT reductase involved in the biosynthesis of archaeal membrane lipids from
RT Thermoplasma acidophilum.";
RL Bioorg. Chem. 35:276-283(2007).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEX WITH FAD AND LIPID,
RP COFACTOR, AND SUBUNIT.
RX PubMed=20869368; DOI=10.1016/j.jmb.2010.09.032;
RA Xu Q., Eguchi T., Mathews I.I., Rife C.L., Chiu H.J., Farr C.L.,
RA Feuerhelm J., Jaroszewski L., Klock H.E., Knuth M.W., Miller M.D.,
RA Weekes D., Elsliger M.A., Deacon A.M., Godzik A., Lesley S.A., Wilson I.A.;
RT "Insights into substrate specificity of geranylgeranyl reductases revealed
RT by the structure of digeranylgeranylglycerophospholipid reductase, an
RT essential enzyme in the biosynthesis of archaeal membrane lipids.";
RL J. Mol. Biol. 404:403-417(2010).
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. Can use both NADH and NADPH
CC as electron donors. Also catalyzes the reduction of the naturally
CC occurring 2,3-di-O-geranylgeranylglyceryl phosphate derivatives such as
CC 2,3-di-O-phytyl-sn-glyceryl phosphate (DPHGP), 3-O-(2,3-di-O-phytyl-sn-
CC glycero-phospho)-sn-glycerol (DPHGPG) and 2,3-di-O-phytyl-sn-glycero-
CC phosphoethanolamine (DPHGPE). Is not active toward 2,3-di-O-
CC geranylgeranylglycerol. {ECO:0000269|PubMed:16788058,
CC ECO:0000269|PubMed:17275067}.
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:0000269|PubMed:16788058};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:36037;
CC Evidence={ECO:0000305|PubMed:16788058};
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:0000269|PubMed:16788058};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:36041;
CC Evidence={ECO:0000305|PubMed:16788058};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:16788058, ECO:0000269|PubMed:17275067,
CC ECO:0000269|PubMed:20869368};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:16788058,
CC ECO:0000269|PubMed:17275067, ECO:0000269|PubMed:20869368};
CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20869368}.
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:16788058}.
CC -!- MISCELLANEOUS: Reduction reaction proceeds via syn addition of hydrogen
CC for double bonds.
CC -!- SIMILARITY: Belongs to the geranylgeranyl reductase family. DGGGPL
CC reductase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAC11656.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR EMBL; AL445064; CAC11656.1; ALT_INIT; Genomic_DNA.
DR RefSeq; WP_010900941.1; NC_002578.1.
DR PDB; 3OZ2; X-ray; 1.60 A; A=1-396.
DR PDBsum; 3OZ2; -.
DR AlphaFoldDB; Q9HKS9; -.
DR SMR; Q9HKS9; -.
DR STRING; 273075.Ta0516m; -.
DR EnsemblBacteria; CAC11656; CAC11656; CAC11656.
DR GeneID; 1457015; -.
DR KEGG; tac:Ta0516; -.
DR eggNOG; arCOG00570; Archaea.
DR HOGENOM; CLU_024648_0_0_2; -.
DR OMA; GMCRREV; -.
DR OrthoDB; 31233at2157; -.
DR BioCyc; MetaCyc:MON-17979; -.
DR BRENDA; 1.3.1.101; 6324.
DR BRENDA; 1.3.7.11; 6324.
DR UniPathway; UPA00940; -.
DR EvolutionaryTrace; Q9HKS9; -.
DR Proteomes; UP000001024; Chromosome.
DR GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
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 1: Evidence at protein level;
KW 3D-structure; Cell membrane; Direct protein sequencing; FAD; Flavoprotein;
KW Lipid biosynthesis; Lipid metabolism; Membrane; NAD; NADP; Oxidoreductase;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome.
FT CHAIN 1..396
FT /note="Digeranylgeranylglycerophospholipid reductase"
FT /id="PRO_0000350723"
FT BINDING 10..14
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:20869368"
FT BINDING 33..35
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:20869368"
FT BINDING 44..47
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:20869368"
FT BINDING 49
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20869368"
FT BINDING 100
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:20869368"
FT BINDING 124
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:20869368"
FT BINDING 162
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:20869368"
FT BINDING 208..214
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20869368"
FT BINDING 283
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:20869368"
FT BINDING 291..294
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20869368"
FT BINDING 295..296
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000269|PubMed:20869368"
FT BINDING 338
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20869368"
FT BINDING 372..374
FT /ligand="substrate"
FT /evidence="ECO:0000269|PubMed:20869368"
FT STRAND 1..9
FT /evidence="ECO:0007829|PDB:3OZ2"
FT HELIX 13..24
FT /evidence="ECO:0007829|PDB:3OZ2"
FT STRAND 29..32
FT /evidence="ECO:0007829|PDB:3OZ2"
FT STRAND 34..37
FT /evidence="ECO:0007829|PDB:3OZ2"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:3OZ2"
FT HELIX 51..55
FT /evidence="ECO:0007829|PDB:3OZ2"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:3OZ2"
FT STRAND 65..75
FT /evidence="ECO:0007829|PDB:3OZ2"
FT STRAND 83..86
FT /evidence="ECO:0007829|PDB:3OZ2"
FT STRAND 88..91
FT /evidence="ECO:0007829|PDB:3OZ2"
FT STRAND 95..98
FT /evidence="ECO:0007829|PDB:3OZ2"
FT HELIX 100..114
FT /evidence="ECO:0007829|PDB:3OZ2"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:3OZ2"
FT STRAND 124..130
FT /evidence="ECO:0007829|PDB:3OZ2"
FT STRAND 133..141
FT /evidence="ECO:0007829|PDB:3OZ2"
FT STRAND 144..155
FT /evidence="ECO:0007829|PDB:3OZ2"
FT HELIX 162..167
FT /evidence="ECO:0007829|PDB:3OZ2"
FT HELIX 170..172
FT /evidence="ECO:0007829|PDB:3OZ2"
FT HELIX 176..178
FT /evidence="ECO:0007829|PDB:3OZ2"
FT STRAND 179..189
FT /evidence="ECO:0007829|PDB:3OZ2"
FT STRAND 196..200
FT /evidence="ECO:0007829|PDB:3OZ2"
FT STRAND 208..216
FT /evidence="ECO:0007829|PDB:3OZ2"
FT STRAND 219..227
FT /evidence="ECO:0007829|PDB:3OZ2"
FT TURN 228..230
FT /evidence="ECO:0007829|PDB:3OZ2"
FT HELIX 234..246
FT /evidence="ECO:0007829|PDB:3OZ2"
FT HELIX 249..252
FT /evidence="ECO:0007829|PDB:3OZ2"
FT STRAND 254..265
FT /evidence="ECO:0007829|PDB:3OZ2"
FT STRAND 278..280
FT /evidence="ECO:0007829|PDB:3OZ2"
FT HELIX 282..285
FT /evidence="ECO:0007829|PDB:3OZ2"
FT TURN 290..292
FT /evidence="ECO:0007829|PDB:3OZ2"
FT HELIX 296..316
FT /evidence="ECO:0007829|PDB:3OZ2"
FT HELIX 321..350
FT /evidence="ECO:0007829|PDB:3OZ2"
FT HELIX 354..364
FT /evidence="ECO:0007829|PDB:3OZ2"
FT HELIX 374..384
FT /evidence="ECO:0007829|PDB:3OZ2"
FT HELIX 386..395
FT /evidence="ECO:0007829|PDB:3OZ2"
SQ SEQUENCE 396 AA; 43353 MW; C607688CD4144EF8 CRC64;
METYDVLVVG GGPGGSTAAR YAAKYGLKTL MIEKRPEIGS PVRCGEGLSK GILNEADIKA
DRSFIANEVK GARIYGPSEK RPIILQSEKA GNEVGYVLER DKFDKHLAAL AAKAGADVWV
KSPALGVIKE NGKVAGAKIR HNNEIVDVRA KMVIAADGFE SEFGRWAGLK SVILARNDII
SALQYRMINV DVDPDYTDFY LGSIAPAGYI WVFPKGEGMA NVGIGSSINW IHNRFELKNY
LDRFIENHPG LKKGQDIQLV TGGVSVSKVK MPITMPGLML VGDAARLIDP ITGGGIANAI
VSGMYAAQVT KEAIESNDYS PQMMQKYEKL IKERFERKHL RNWVAKEKLA MLSDDTLDKL
VDIVSEQVLT TISVEAILKA IAEKYPEVVK ELEDLI
