GGR_ARCFU
ID GGR_ARCFU Reviewed; 387 AA.
AC O29786;
DT 23-SEP-2008, integrated into UniProtKB/Swiss-Prot.
DT 23-SEP-2008, sequence version 2.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=Digeranylgeranylglycerophospholipid reductase;
DE Short=DGGGPL reductase;
DE EC=1.3.-.- {ECO:0000269|PubMed:17288560};
DE AltName: Full=2,3-bis-O-geranylgeranylglyceryl phosphate reductase;
DE AltName: Full=Geranylgeranyl reductase;
DE Short=GGR;
GN OrderedLocusNames=AF_0464;
OS Archaeoglobus fulgidus (strain ATCC 49558 / DSM 4304 / JCM 9628 / NBRC
OS 100126 / VC-16).
OC Archaea; Euryarchaeota; Archaeoglobi; Archaeoglobales; Archaeoglobaceae;
OC Archaeoglobus.
OX NCBI_TaxID=224325;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 49558 / DSM 4304 / JCM 9628 / NBRC 100126 / VC-16;
RX PubMed=9389475; DOI=10.1038/37052;
RA Klenk H.-P., Clayton R.A., Tomb J.-F., White O., Nelson K.E., Ketchum K.A.,
RA Dodson R.J., Gwinn M.L., Hickey E.K., Peterson J.D., Richardson D.L.,
RA Kerlavage A.R., Graham D.E., Kyrpides N.C., Fleischmann R.D.,
RA Quackenbush J., Lee N.H., Sutton G.G., Gill S.R., Kirkness E.F.,
RA Dougherty B.A., McKenney K., Adams M.D., Loftus B.J., Peterson S.N.,
RA Reich C.I., McNeil L.K., Badger J.H., Glodek A., Zhou L., Overbeek R.,
RA Gocayne J.D., Weidman J.F., McDonald L.A., Utterback T.R., Cotton M.D.,
RA Spriggs T., Artiach P., Kaine B.P., Sykes S.M., Sadow P.W., D'Andrea K.P.,
RA Bowman C., Fujii C., Garland S.A., Mason T.M., Olsen G.J., Fraser C.M.,
RA Smith H.O., Woese C.R., Venter J.C.;
RT "The complete genome sequence of the hyperthermophilic, sulphate-reducing
RT archaeon Archaeoglobus fulgidus.";
RL Nature 390:364-370(1997).
RN [2]
RP PROTEIN SEQUENCE OF 1-9, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE
RP SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=17288560; DOI=10.1111/j.1742-4658.2006.05625.x;
RA Murakami M., Shibuya K., Nakayama T., Nishino T., Yoshimura T., Hemmi H.;
RT "Geranylgeranyl reductase involved in the biosynthesis of archaeal membrane
RT lipids in the hyperthermophilic archaeon Archaeoglobus fulgidus.";
RL FEBS J. 274:805-814(2007).
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. Is not active with NADPH as
CC an electron donor. Is not able to reduce the prenyl group of
CC respiratory quinones. {ECO:0000269|PubMed:17288560}.
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;
CC Evidence={ECO:0000269|PubMed:17288560};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64378;
CC Evidence={ECO:0000305|PubMed:17288560};
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;
CC Evidence={ECO:0000269|PubMed:17288560};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:64370;
CC Evidence={ECO:0000305|PubMed:17288560};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000269|PubMed:17288560};
CC Note=Binds 1 FAD per subunit. {ECO:0000269|PubMed:17288560};
CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305|PubMed:17288560}.
CC -!- MISCELLANEOUS: Reduction reaction proceeds via syn addition of hydrogen
CC for double bonds. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the geranylgeranyl reductase family. DGGGPL
CC reductase subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB90773.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AE000782; AAB90773.1; ALT_INIT; Genomic_DNA.
DR PIR; H69307; H69307.
DR RefSeq; WP_048064241.1; NC_000917.1.
DR AlphaFoldDB; O29786; -.
DR SMR; O29786; -.
DR STRING; 224325.AF_0464; -.
DR DNASU; 1483680; -.
DR EnsemblBacteria; AAB90773; AAB90773; AF_0464.
DR GeneID; 24794003; -.
DR KEGG; afu:AF_0464; -.
DR eggNOG; arCOG00570; Archaea.
DR HOGENOM; CLU_024648_0_0_2; -.
DR OMA; GMCRREV; -.
DR OrthoDB; 31233at2157; -.
DR BioCyc; MetaCyc:MON-17978; -.
DR BRENDA; 1.3.7.11; 414.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000002199; Chromosome.
DR GO; GO:0005737; C:cytoplasm; 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: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; 3.50.50.60; -; 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 Cytoplasm; Direct protein sequencing; FAD; Flavoprotein;
KW Lipid biosynthesis; Lipid metabolism; Oxidoreductase;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome.
FT CHAIN 1..387
FT /note="Digeranylgeranylglycerophospholipid reductase"
FT /id="PRO_0000350722"
FT BINDING 8..12
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 31..33
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 42..45
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 96
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 203..209
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 274
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 282..285
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 286..287
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 387 AA; 42400 MW; 90E373C2CA99449A CRC64;
MYDVVVVGAG PAGSMAAKTA AEQGLKVLLV EKRQEIGTPV RCAEGISRES IEKFFEVDKK
WIAAEVTGAK IYAPNKTEIV MSEEMAGNEV GYVLERKIFD RHVARLAAKA GAEVYVKTAM
VDFERKDGKV KVKLRRLGED WEVETKILIG ADGVESKIGR KAGIIKTLKL NEVESCAQYL
MTGLDIDESY TYFYLGRELA PGGYAWIFPK GNGSANVGIG VLPKMAERTA KEYLDAFIEK
EGIEGKIVEF VAGAVPVYGE IETAVADNIM LAGDAAYHAD PITGGGIANA LSAGYYAGKV
AAEAVQKNDF SADFLRRYDE LWKNDFGKKL RRNKKLQLKF IDMDDALLNK LAGAIAGKNL
REMSVAAIVK ELLKAHPKLL WDLKDLF
