GGR_HALVD
ID GGR_HALVD Reviewed; 410 AA.
AC D4GSC3;
DT 14-MAY-2014, integrated into UniProtKB/Swiss-Prot.
DT 18-MAY-2010, sequence version 1.
DT 03-AUG-2022, entry version 59.
DE RecName: Full=Digeranylgeranylglycerophospholipid reductase;
DE Short=DGGGPL reductase;
DE EC=1.3.7.11;
DE AltName: Full=2,3-bis-O-geranylgeranylglyceryl phosphate reductase;
DE AltName: Full=Geranylgeranyl reductase;
DE Short=GGR;
GN OrderedLocusNames=HVO_1799; ORFNames=C498_04308;
OS Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 /
OS NCIMB 2012 / VKM B-1768 / DS2) (Halobacterium volcanii).
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Haloferacales;
OC Haloferacaceae; Haloferax.
OX NCBI_TaxID=309800;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=20333302; DOI=10.1371/journal.pone.0009605;
RA Hartman A.L., Norais C., Badger J.H., Delmas S., Haldenby S., Madupu R.,
RA Robinson J., Khouri H., Ren Q., Lowe T.M., Maupin-Furlow J.,
RA Pohlschroder M., Daniels C., Pfeiffer F., Allers T., Eisen J.A.;
RT "The complete genome sequence of Haloferax volcanii DS2, a model
RT archaeon.";
RL PLoS ONE 5:E9605-E9605(2010).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM
RC B-1768 / DS2;
RX PubMed=25393412; DOI=10.1371/journal.pgen.1004784;
RA Becker E.A., Seitzer P.M., Tritt A., Larsen D., Krusor M., Yao A.I., Wu D.,
RA Madern D., Eisen J.A., Darling A.E., Facciotti M.T.;
RT "Phylogenetically driven sequencing of extremely halophilic archaea reveals
RT strategies for static and dynamic osmo-response.";
RL PLoS Genet. 10:E1004784-E1004784(2014).
RN [3]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RC STRAIN=WR536;
RX PubMed=22469971; DOI=10.1016/j.bbalip.2012.03.002;
RA Naparstek S., Guan Z., Eichler J.;
RT "A predicted geranylgeranyl reductase reduces the omega-position isoprene
RT of dolichol phosphate in the halophilic archaeon, Haloferax volcanii.";
RL Biochim. Biophys. Acta 1821:923-933(2012).
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. Can fully reduce the
CC unsaturated isoprenoid side chains of membrane phospholipids and
CC glycolipids. Is also able to reduce the omega-position isoprene of
CC dolichol phosphate. {ECO:0000269|PubMed:22469971}.
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 -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692; Evidence={ECO:0000250};
CC Note=Binds 1 FAD per subunit. {ECO:0000250};
CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC -!- DISRUPTION PHENOTYPE: Reduced pigmentation of cell colonies and lack of
CC fully reduced isoprene chains of membrane phospholipids and
CC glycolipids. {ECO:0000269|PubMed:22469971}.
CC -!- SIMILARITY: Belongs to the geranylgeranyl reductase family. DGGGPL
CC reductase subfamily. {ECO:0000305}.
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DR EMBL; CP001956; ADE03171.1; -; Genomic_DNA.
DR EMBL; AOHU01000033; ELY35164.1; -; Genomic_DNA.
DR RefSeq; WP_004041683.1; NZ_AOHU01000033.1.
DR AlphaFoldDB; D4GSC3; -.
DR SMR; D4GSC3; -.
DR STRING; 309800.C498_04308; -.
DR EnsemblBacteria; ADE03171; ADE03171; HVO_1799.
DR EnsemblBacteria; ELY35164; ELY35164; C498_04308.
DR GeneID; 8923972; -.
DR KEGG; hvo:HVO_1799; -.
DR PATRIC; fig|309800.29.peg.838; -.
DR eggNOG; arCOG00570; Archaea.
DR HOGENOM; CLU_664998_0_0_2; -.
DR OMA; GLCYIQN; -.
DR OrthoDB; 20866at2157; -.
DR BRENDA; 1.3.99.B15; 2561.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000008243; Chromosome.
DR Proteomes; UP000011532; Unassembled WGS sequence.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR GO; GO:0006650; P:glycerophospholipid metabolic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0008654; P:phospholipid biosynthetic process; IEA:UniProtKB-KW.
DR Gene3D; 3.50.50.60; -; 1.
DR InterPro; IPR002938; FAD-bd.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR Pfam; PF01494; FAD_binding_3; 1.
DR SUPFAM; SSF51905; SSF51905; 1.
PE 3: Inferred from homology;
KW FAD; Flavoprotein; Lipid biosynthesis; Lipid metabolism; Oxidoreductase;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome.
FT CHAIN 1..410
FT /note="Digeranylgeranylglycerophospholipid reductase"
FT /id="PRO_0000428875"
FT BINDING 11..15
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 34..36
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 205..211
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 286
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
FT BINDING 294..297
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 298..299
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000250"
SQ SEQUENCE 410 AA; 45449 MW; 44C37D8E4AD58BCC CRC64;
MTDNYDVIIA GAGPAGGQAA RDLAARGYDV CVLETESEDE FPSRSNKSTA GTFPSTMASF
NIPDEVVMNF TDDVVLESPN DHYHRHQPGA VLEFADFKNW LVDEAEADGA EYRFDARVSK
PIMEGGEIVG VRYNGDEEVY ADIVIDATGP SAPLAKALDL CDLRREKQAI GIEYEFEGMD
LAPDGYGDLT DAMMLRLDHD IAPGGYSWIF HTGGDTAKVG VCYIQNEGHR HNAKSGYTID
DYLQYWTESD PRFADAERIA GKQHRGSAHI QLPGRMSTDN FMAIGDTVPT VDPLWGEGID
KCMRSGRVAA ATADRALTNS ERDTSASELA IYDQLWHDRV APKVKNRLFM TEMLYRASNE
RYDKLLEDLH RLPDEQLDAA NGGSPLAMFR MLKFEDLSIL ASTAKDWFSN
