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Database: UniProt
Entry: A0A133US50_9EURY
LinkDB: A0A133US50_9EURY
Original site: A0A133US50_9EURY 
ID   A0A133US50_9EURY        Unreviewed;       394 AA.
AC   A0A133US50;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 29.
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=AKJ37_03815 {ECO:0000313|EMBL:KXA97064.1};
OS   candidate division MSBL1 archaeon SCGC-AAA259I09.
OC   Archaea; Euryarchaeota; candidate division MSBL1.
OX   NCBI_TaxID=1698267 {ECO:0000313|EMBL:KXA97064.1, ECO:0000313|Proteomes:UP000070463};
RN   [1] {ECO:0000313|EMBL:KXA97064.1, ECO:0000313|Proteomes:UP000070463}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCGC-AAA259I09 {ECO:0000313|EMBL:KXA97064.1};
RX   PubMed=26758088; DOI=10.1038/srep19181;
RA   Mwirichia R., Alam I., Rashid M., Vinu M., Ba-Alawi W., Anthony Kamau A.,
RA   Kamanda Ngugi D., Goker M., Klenk H.P., Bajic V., Stingl U.;
RT   "Metabolic traits of an uncultured archaeal lineage -MSBL1- from brine
RT   pools of the Red Sea.";
RL   Sci. Rep. 6:19181-19181(2016).
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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:KXA97064.1}.
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DR   EMBL; LHXR01000046; KXA97064.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A133US50; -.
DR   PATRIC; fig|1698267.3.peg.1353; -.
DR   UniPathway; UPA00940; -.
DR   Proteomes; UP000070463; Unassembled WGS sequence.
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}; Reference proteome {ECO:0000313|Proteomes:UP000070463}.
FT   DOMAIN          5..328
FT                   /note="FAD-binding"
FT                   /evidence="ECO:0000259|Pfam:PF01494"
FT   BINDING         12..16
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01287"
FT   BINDING         35..37
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01287"
FT   BINDING         46..49
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         208..214
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01287"
FT   BINDING         281
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01287"
FT   BINDING         289..292
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01287"
FT   BINDING         293..294
FT                   /ligand="FAD"
FT                   /ligand_id="ChEBI:CHEBI:57692"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01287"
SQ   SEQUENCE   394 AA;  42862 MW;  C293351D1C86A6D5 CRC64;
     MPKSEYDVIV VGAGPAGATA AKAAAENGAD VLMVDKRREL GVPVQCGEAL SEEILKKLDI
     DPDPRWAINK INRAMLVSPS GKPVEIKQKK SAKIGYILDR KVFDKYLAIL AIRSGADIRI
     DTFVNGLVKE NGGINGVTLQ GKKGEEIRSD LIIAADGVMS RVARWAGFDT TLGMEDIESG
     AQFKMVNVDV EEKSMMKFYF GNEIAPGGYI WIFPRGDDIA NVGIGVMPKK AEKKSIEYLK
     DFISARPDLE NGRIIEINVG GVPVSGPIEK TYGDDIMIVG DAARQVNALT GGGIDWSMHA
     GNIAGEVAAR AVAEGDTSEG NLKEYEDRWR DEMGDSLNKY YKGKEVLMDL SDGDLDDLAD
     SLQDVDFEKI SLTSMLRVIM KANPKLMIKL RGLL
//
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