ID H3ZKS4_THELN Unreviewed; 393 AA.
AC H3ZKS4;
DT 18-APR-2012, integrated into UniProtKB/TrEMBL.
DT 18-APR-2012, sequence version 1.
DT 27-MAR-2024, entry version 69.
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=OCC_08470 {ECO:0000313|EMBL:EHR79506.1};
OS Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C).
OC Archaea; Euryarchaeota; Thermococci; Thermococcales; Thermococcaceae;
OC Thermococcus.
OX NCBI_TaxID=523849 {ECO:0000313|EMBL:EHR79506.1, ECO:0000313|Proteomes:UP000015502};
RN [1] {ECO:0000313|EMBL:EHR79506.1, ECO:0000313|Proteomes:UP000015502}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51850 / DSM 5473 / JCM 8560 / NS-C
RC {ECO:0000313|Proteomes:UP000015502};
RX PubMed=22493191; DOI=10.1128/JB.00123-12;
RA Gardner A.F., Kumar S., Perler F.B.;
RT "Genome sequence of the model hyperthermophilic archaeon Thermococcus
RT litoralis NS-C.";
RL J. Bacteriol. 194:2375-2376(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. 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; CP006670; EHR79506.1; -; Genomic_DNA.
DR RefSeq; WP_004066810.1; NC_022084.1.
DR AlphaFoldDB; H3ZKS4; -.
DR STRING; 523849.OCC_08470; -.
DR PaxDb; 523849-OCC_08470; -.
DR GeneID; 16550724; -.
DR KEGG; tlt:OCC_08470; -.
DR HOGENOM; CLU_024648_0_0_2; -.
DR OrthoDB; 6062at2157; -.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000015502; 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..319
FT /note="FAD-binding"
FT /evidence="ECO:0000259|Pfam:PF01494"
FT BINDING 9..13
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01287"
FT BINDING 32..34
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01287"
FT BINDING 43..46
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01287"
FT BINDING 95
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01287"
FT BINDING 203..209
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01287"
FT BINDING 274
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01287"
FT BINDING 282..285
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01287"
FT BINDING 286..287
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01287"
SQ SEQUENCE 393 AA; 43834 MW; 0CC66E6240D7CBB2 CRC64;
MRYDVVVVGS GIAGPIVARN VAKAGFSVLL IDKKPAIGTP KQCAEGISIK VFDKYDIPYD
RRYINREIYG AKLYSPSGYE LEMRYKEVSG VILERKVFDK MLAYYAAKAG ADVLARTEAL
DVIRKDGKIA GIKAKHEDEP VEIYADIIVA ADGVESTIAR KAGINTYAPP HEFDSGYEYE
MLIEGFDPDL IHLWFGNEVA PRGYVWVFPK DEDRANVGIG INSDNPKTAK YYLDKWLEEN
NIPAKKLLEI NVGVVPVGGF VKELAKDNVV VVGDAARQVN PMHGGGMAEA MEAGTIASKW
IVKALEEENI SLLQNYTKEW WEKDGKRLER VLKVRRVTEK LTDEDLDLFI QILSGADAEK
IAGGDYIEVI KALLKHPKVL MSKRRIALLK ELL
//
