ISPA_GEOSE
ID ISPA_GEOSE Reviewed; 297 AA.
AC Q08291; Q53435; Q53436; Q53437; Q53438;
DT 01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1994, sequence version 1.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Farnesyl diphosphate synthase;
DE Short=FPP synthase;
DE EC=2.5.1.10;
DE AltName: Full=(2E,6E)-farnesyl diphosphate synthase;
DE AltName: Full=Geranyltranstransferase;
OS Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=1422;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=ATCC 10149 / DSM 6790 / CCM 5965 / CIP 105453 / JCM 11297 / NRS T15;
RX PubMed=8486607; DOI=10.1093/oxfordjournals.jbchem.a124051;
RA Koyama T., Obata S., Osabe M., Takeshita A., Yokoyama K., Uchida M.,
RA Nishino T., Ogura K.;
RT "Thermostable farnesyl diphosphate synthase of Bacillus stearothermophilus:
RT molecular cloning, sequence determination, overproduction, and
RT purification.";
RL J. Biochem. 113:355-363(1993).
RN [2]
RP MUTAGENESIS OF CYSTEINE RESIDUES.
RX PubMed=7918490; DOI=10.1021/bi00208a015;
RA Koyama T., Obata S., Saito K., Takeshita-Koike A., Ogura K.;
RT "Structural and functional roles of the cysteine residues of Bacillus
RT stearothermophilus farnesyl diphosphate synthase.";
RL Biochemistry 33:12644-12648(1994).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E)-geranyl diphosphate + isopentenyl diphosphate = (2E,6E)-
CC farnesyl diphosphate + diphosphate; Xref=Rhea:RHEA:19361,
CC ChEBI:CHEBI:33019, ChEBI:CHEBI:58057, ChEBI:CHEBI:128769,
CC ChEBI:CHEBI:175763; EC=2.5.1.10;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; D13293; BAA02551.1; -; Genomic_DNA.
DR EMBL; S72629; AAB32272.1; -; Genomic_DNA.
DR EMBL; S72630; AAB32273.2; ALT_SEQ; Genomic_DNA.
DR EMBL; S72633; AAB32274.1; -; Genomic_DNA.
DR EMBL; S72635; AAB32275.2; ALT_SEQ; Genomic_DNA.
DR PIR; JX0257; JX0257.
DR RefSeq; WP_033016440.1; NZ_RCTH01000002.1.
DR PDB; 5AYP; X-ray; 2.31 A; A/B=1-297.
DR PDBsum; 5AYP; -.
DR AlphaFoldDB; Q08291; -.
DR SMR; Q08291; -.
DR ChEMBL; CHEMBL4786; -.
DR BRENDA; 2.5.1.10; 623.
DR SABIO-RK; Q08291; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0004337; F:geranyltranstransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW.
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 InterPro; IPR033749; Polyprenyl_synt_CS.
DR Pfam; PF00348; polyprenyl_synt; 1.
DR SUPFAM; SSF48576; SSF48576; 1.
DR PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
DR PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Direct protein sequencing; Isoprene biosynthesis;
KW Magnesium; Metal-binding; Transferase.
FT CHAIN 1..297
FT /note="Farnesyl diphosphate synthase"
FT /id="PRO_0000123985"
FT BINDING 47
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 50
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 79
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 86
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 86
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 92
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 92
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 97
FT /ligand="(2E)-geranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58057"
FT /evidence="ECO:0000250"
FT BINDING 98
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 183
FT /ligand="(2E)-geranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58057"
FT /evidence="ECO:0000250"
FT BINDING 184
FT /ligand="(2E)-geranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58057"
FT /evidence="ECO:0000250"
FT BINDING 221
FT /ligand="(2E)-geranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58057"
FT /evidence="ECO:0000250"
FT BINDING 238
FT /ligand="(2E)-geranyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58057"
FT /evidence="ECO:0000250"
FT MUTAGEN 73
FT /note="C->F,S: No loss of activity."
FT /evidence="ECO:0000269|PubMed:7918490"
FT MUTAGEN 289
FT /note="C->F,S: No loss of activity."
FT /evidence="ECO:0000269|PubMed:7918490"
FT HELIX 5..26
FT /evidence="ECO:0007829|PDB:5AYP"
FT HELIX 32..42
FT /evidence="ECO:0007829|PDB:5AYP"
FT HELIX 49..60
FT /evidence="ECO:0007829|PDB:5AYP"
FT HELIX 65..68
FT /evidence="ECO:0007829|PDB:5AYP"
FT HELIX 69..87
FT /evidence="ECO:0007829|PDB:5AYP"
FT TURN 89..92
FT /evidence="ECO:0007829|PDB:5AYP"
FT HELIX 103..128
FT /evidence="ECO:0007829|PDB:5AYP"
FT HELIX 137..151
FT /evidence="ECO:0007829|PDB:5AYP"
FT HELIX 156..164
FT /evidence="ECO:0007829|PDB:5AYP"
FT HELIX 173..183
FT /evidence="ECO:0007829|PDB:5AYP"
FT HELIX 185..199
FT /evidence="ECO:0007829|PDB:5AYP"
FT HELIX 203..220
FT /evidence="ECO:0007829|PDB:5AYP"
FT HELIX 252..255
FT /evidence="ECO:0007829|PDB:5AYP"
FT HELIX 258..277
FT /evidence="ECO:0007829|PDB:5AYP"
FT HELIX 283..293
FT /evidence="ECO:0007829|PDB:5AYP"
SQ SEQUENCE 297 AA; 32310 MW; 0F921C3F029EEBB6 CRC64;
MAQLSVEQFL NEQKQAVETA LSRYIERLEG PAKLKKAMAY SLEAGGKRIR PLLLLSTVRA
LGKDPAVGLP VACAIEMIHT YSLIHDDLPS MDNDDLRRGK PTNHKVFGEA MAILAGDGLL
TYAFQLITEI DDERIPPSVR LRLIERLAKA AGPEGMVAGQ AADMEGEGKT LTLSELEYIH
RHKTGKMLQY SVHAGALIGG ADARQTRELD EFAAHLGLAF QIRDDILDIE GAEEKIGKPV
GSDQSNNKAT YPALLSLAGA KEKLAFHIEA AQRHLRNADV DGAALAYICE LVAARDH
