GFPS_METMA
ID GFPS_METMA Reviewed; 295 AA.
AC Q8PYS1;
DT 03-OCT-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2002, sequence version 1.
DT 03-AUG-2022, entry version 117.
DE RecName: Full=Geranylfarnesyl diphosphate synthase;
DE Short=GFPS;
DE EC=2.5.1.81;
DE AltName: Full=Farnesylgeranyl diphosphate synthase;
DE Short=FGPP synthase;
GN OrderedLocusNames=MM_0789;
OS Methanosarcina mazei (strain ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM
OS 11833 / OCM 88) (Methanosarcina frisia).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=192952;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-159 / DSM 3647 / Goe1 / Go1 / JCM 11833 / OCM 88;
RX PubMed=12125824;
RA Deppenmeier U., Johann A., Hartsch T., Merkl R., Schmitz R.A.,
RA Martinez-Arias R., Henne A., Wiezer A., Baeumer S., Jacobi C.,
RA Brueggemann H., Lienard T., Christmann A., Boemecke M., Steckel S.,
RA Bhattacharyya A., Lykidis A., Overbeek R., Klenk H.-P., Gunsalus R.P.,
RA Fritz H.-J., Gottschalk G.;
RT "The genome of Methanosarcina mazei: evidence for lateral gene transfer
RT between Bacteria and Archaea.";
RL J. Mol. Microbiol. Biotechnol. 4:453-461(2002).
RN [2]
RP FUNCTION AS A GERANYLFARNESYL DIPHOSPHATE SYNTHASE, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, COFACTOR, AND SUBSTRATE SPECIFICITY.
RX PubMed=20097171; DOI=10.1016/j.bbrc.2010.01.063;
RA Ogawa T., Yoshimura T., Hemmi H.;
RT "Geranylfarnesyl diphosphate synthase from Methanosarcina mazei: Different
RT role, different evolution.";
RL Biochem. Biophys. Res. Commun. 393:16-20(2010).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 12-295.
RA Kumaran D., Mohammed M.B., Brown A., Burley S.K., Swaminathan S.;
RT "Crystal Structure of a Geranyltranstransferase from the Methanosarcina
RT mazei.";
RL Submitted (AUG-2009) to the PDB data bank.
CC -!- FUNCTION: Involved in biosynthesis of the polyprenyl side-chain of
CC methanophenazine, an electron carrier utilized for methanogenesis.
CC Catalyzes the condensation of isopentenyl pyrophosphate with the
CC allylic pyrophosphates to yield geranylfarnesyl diphosphate (GFPP). It
CC prefers geranylgeranyl diphosphate (GGPP) and farnesyl diphosphate
CC (FPP) as allylic substrate. {ECO:0000269|PubMed:20097171}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E)-geranylgeranyl diphosphate + isopentenyl
CC diphosphate = (2E,6E,10E,14E)-geranylfarnesyl diphosphate +
CC diphosphate; Xref=Rhea:RHEA:25694, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57907, ChEBI:CHEBI:58756, ChEBI:CHEBI:128769;
CC EC=2.5.1.81; Evidence={ECO:0000269|PubMed:20097171};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000305|PubMed:20097171};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000305|PubMed:20097171};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 7. {ECO:0000269|PubMed:20097171};
CC Temperature dependence:
CC Optimum temperature is 40 degrees Celsius.
CC {ECO:0000269|PubMed:20097171};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; AE008384; AAM30485.1; -; Genomic_DNA.
DR RefSeq; WP_011032739.1; NC_003901.1.
DR PDB; 3IPI; X-ray; 1.90 A; A=12-295.
DR PDBsum; 3IPI; -.
DR AlphaFoldDB; Q8PYS1; -.
DR SMR; Q8PYS1; -.
DR STRING; 192952.MM_0789; -.
DR DNASU; 1479131; -.
DR EnsemblBacteria; AAM30485; AAM30485; MM_0789.
DR GeneID; 24838119; -.
DR KEGG; mma:MM_0789; -.
DR PATRIC; fig|192952.21.peg.937; -.
DR eggNOG; arCOG01727; Archaea.
DR HOGENOM; CLU_014015_2_0_2; -.
DR OMA; WLIAESI; -.
DR BRENDA; 2.5.1.81; 3270.
DR EvolutionaryTrace; Q8PYS1; -.
DR Proteomes; UP000000595; Chromosome.
DR GO; GO:0044687; F:geranylfarnesyl diphosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004659; F:prenyltransferase activity; IDA:UniProtKB.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:InterPro.
DR CDD; cd00685; Trans_IPPS_HT; 1.
DR Gene3D; 1.10.600.10; -; 1.
DR InterPro; IPR008949; Isoprenoid_synthase_dom_sf.
DR InterPro; IPR000092; Polyprenyl_synt.
DR Pfam; PF00348; polyprenyl_synt; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Magnesium; Metal-binding; Reference proteome; Transferase.
FT CHAIN 1..295
FT /note="Geranylfarnesyl diphosphate synthase"
FT /id="PRO_0000419205"
FT BINDING 51
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 54
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 83
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 90
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 90
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 94
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 94
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 99
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 100
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 174
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 175
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 212
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT HELIX 13..15
FT /evidence="ECO:0007829|PDB:3IPI"
FT HELIX 17..31
FT /evidence="ECO:0007829|PDB:3IPI"
FT HELIX 36..46
FT /evidence="ECO:0007829|PDB:3IPI"
FT HELIX 53..66
FT /evidence="ECO:0007829|PDB:3IPI"
FT HELIX 70..72
FT /evidence="ECO:0007829|PDB:3IPI"
FT HELIX 73..96
FT /evidence="ECO:0007829|PDB:3IPI"
FT HELIX 111..129
FT /evidence="ECO:0007829|PDB:3IPI"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:3IPI"
FT HELIX 134..155
FT /evidence="ECO:0007829|PDB:3IPI"
FT HELIX 165..174
FT /evidence="ECO:0007829|PDB:3IPI"
FT HELIX 176..189
FT /evidence="ECO:0007829|PDB:3IPI"
FT HELIX 194..225
FT /evidence="ECO:0007829|PDB:3IPI"
FT HELIX 236..240
FT /evidence="ECO:0007829|PDB:3IPI"
FT TURN 241..243
FT /evidence="ECO:0007829|PDB:3IPI"
FT HELIX 246..268
FT /evidence="ECO:0007829|PDB:3IPI"
FT HELIX 275..286
FT /evidence="ECO:0007829|PDB:3IPI"
FT HELIX 289..292
FT /evidence="ECO:0007829|PDB:3IPI"
SQ SEQUENCE 295 AA; 32747 MW; CBDBAF279BB8B53F CRC64;
MPVKVHGVIL MNIEEWEEYR YVEAGIKESI TLIEDPGLKK MVEHVCHSGG KRIRPIILLL
VSEICSGSYS RSLNAALAVE MMHSASLIHD DLLDQGLVRR NLPSAPEKFG PSGALLCGDY
LIAKSIAFIS PYGEKVIQDF GKAGMDMAEG EVLDLKLEDE SFGENDYFKC IYKKTASLFA
ISASIGAYTG GAEEELAERF SHFGNALGTA YQIVDDILEF LEVVEGKESK FTSETLPHIY
MKSTSKEEAL KKSIDCVKLH VAAAKETLET FRECPARDKL FQITDYITVD MLENL
