GGR_METAC
ID GGR_METAC Reviewed; 407 AA.
AC Q8TQQ6;
DT 14-OCT-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Digeranylgeranylglycerophospholipid reductase {ECO:0000255|HAMAP-Rule:MF_01287};
DE Short=DGGGPL reductase {ECO:0000255|HAMAP-Rule:MF_01287};
DE EC=1.3.7.11 {ECO:0000255|HAMAP-Rule:MF_01287, ECO:0000269|PubMed:24214941};
DE AltName: Full=2,3-bis-O-geranylgeranylglyceryl phosphate reductase {ECO:0000255|HAMAP-Rule:MF_01287};
DE AltName: Full=Geranylgeranyl reductase {ECO:0000255|HAMAP-Rule:MF_01287, ECO:0000303|PubMed:24214941};
DE Short=GGR {ECO:0000255|HAMAP-Rule:MF_01287, ECO:0000303|PubMed:24214941};
GN OrderedLocusNames=MA_1484;
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(2002).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, AND PATHWAY.
RX PubMed=24214941; DOI=10.1128/jb.00927-13;
RA Isobe K., Ogawa T., Hirose K., Yokoi T., Yoshimura T., Hemmi H.;
RT "Geranylgeranyl reductase and ferredoxin from Methanosarcina acetivorans
RT are required for the synthesis of fully reduced archaeal membrane lipid in
RT Escherichia coli cells.";
RL J. Bacteriol. 196:417-423(2014).
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 (By similarity)
CC (PubMed:24214941). Requires the adjacently encoded ferredoxin MA_1485
CC as the electron donor (PubMed:24214941). {ECO:0000255|HAMAP-
CC Rule:MF_01287, ECO:0000269|PubMed:24214941}.
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 Evidence={ECO:0000255|HAMAP-Rule:MF_01287,
CC ECO:0000269|PubMed:24214941};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:54326;
CC Evidence={ECO:0000305|PubMed:24214941};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2,3-bis-O-(phytanyl)-sn-glycerol 1-phosphate + 8 oxidized
CC 2[4Fe-4S]-[ferredoxin] = 2,3-bis-O-(geranylgeranyl)-sn-glycerol 1-
CC phosphate + 16 H(+) + 8 reduced 2[4Fe-4S]-[ferredoxin];
CC Xref=Rhea:RHEA:36159, Rhea:RHEA-COMP:10002, Rhea:RHEA-COMP:10004,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33722, ChEBI:CHEBI:33723,
CC ChEBI:CHEBI:58837, ChEBI:CHEBI:73125; EC=1.3.7.11;
CC Evidence={ECO:0000305|PubMed:24214941};
CC PhysiologicalDirection=right-to-left; Xref=Rhea:RHEA:36161;
CC Evidence={ECO:0000305|PubMed:24214941};
CC -!- COFACTOR:
CC Name=FAD; Xref=ChEBI:CHEBI:57692;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01287};
CC Note=Binds 1 FAD per subunit. {ECO:0000255|HAMAP-Rule:MF_01287};
CC -!- PATHWAY: Membrane lipid metabolism; glycerophospholipid metabolism.
CC {ECO:0000255|HAMAP-Rule:MF_01287, ECO:0000305|PubMed:24214941}.
CC -!- MISCELLANEOUS: Reduction reaction proceeds via syn addition of hydrogen
CC for double bonds. {ECO:0000255|HAMAP-Rule:MF_01287}.
CC -!- SIMILARITY: Belongs to the geranylgeranyl reductase family. DGGGPL
CC reductase subfamily. {ECO:0000255|HAMAP-Rule:MF_01287}.
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DR EMBL; AE010299; AAM04898.1; -; Genomic_DNA.
DR RefSeq; WP_011021498.1; NC_003552.1.
DR AlphaFoldDB; Q8TQQ6; -.
DR SMR; Q8TQQ6; -.
DR STRING; 188937.MA_1484; -.
DR EnsemblBacteria; AAM04898; AAM04898; MA_1484.
DR GeneID; 1473372; -.
DR KEGG; mac:MA_1484; -.
DR HOGENOM; CLU_024648_0_0_2; -.
DR InParanoid; Q8TQQ6; -.
DR OMA; GMCRREV; -.
DR OrthoDB; 31233at2157; -.
DR PhylomeDB; Q8TQQ6; -.
DR BioCyc; MetaCyc:MON-19243; -.
DR BRENDA; 1.3.7.11; 7224.
DR UniPathway; UPA00940; -.
DR Proteomes; UP000002487; Chromosome.
DR GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR GO; GO:0045550; F:geranylgeranyl reductase activity; IEA:InterPro.
DR GO; GO:0016636; F:oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor; IEA:UniProtKB-UniRule.
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 FAD; Flavoprotein; Lipid biosynthesis; Lipid metabolism; Oxidoreductase;
KW Phospholipid biosynthesis; Phospholipid metabolism; Reference proteome.
FT CHAIN 1..407
FT /note="Digeranylgeranylglycerophospholipid reductase"
FT /id="PRO_0000351453"
FT BINDING 11..15
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01287"
FT BINDING 34..36
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01287"
FT BINDING 45..48
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01287"
FT BINDING 99
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01287"
FT BINDING 207..213
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01287"
FT BINDING 281
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01287"
FT BINDING 289..292
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01287"
FT BINDING 293..294
FT /ligand="FAD"
FT /ligand_id="ChEBI:CHEBI:57692"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01287"
SQ SEQUENCE 407 AA; 44503 MW; B654EF039EF5D401 CRC64;
MKDIYDVLVI GAGPAGSIAA KTAAEKGLDV LLIEKRQEIG DPVRCAEGVN KEYLKKHVEI
DNSWICADLK GSRIYSPNGT KVEMAEEISG GEVGYVLERK IFDRALAEHA AKAGAEVRVK
TRATGLIIED DFVKGARLMN LGKEYEVRAK IVIGADGVES KVGRWAGIDT SLKPIDIETC
AQYLIAGADI DPEYCEFYIG NEIAPGGYVW IFPKGEGKAN VGVGILGNRT GKFKPRPVDY
LNNFVEKKFP NAKIVEMVFG GVPVSGSIEK TSVNGLMLVG DAARQSDPIT GGGILNAMDA
GKIAGEAAYE AISSGDVSLE KLEEVYEKRW RETTGHDIDM SLIVKNCFIN LKDEDLDSLA
DSLKEVKFES MRLFDLLQAL FKANKKLLWD LRVLFKDAAK EVMKNRT
