ID   HEPS2_GEOSE             Reviewed;         320 AA.
AC   P55785;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1997, sequence version 1.
DT   03-AUG-2022, entry version 82.
DE   RecName: Full=Heptaprenyl diphosphate synthase component 2;
DE            Short=HepPP synthase subunit 2;
DE            EC=2.5.1.30;
GN   Name=hepT; Synonyms=hepS-2;
OS   Geobacillus stearothermophilus (Bacillus stearothermophilus).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX   NCBI_TaxID=1422;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 10149 / DSM 6790 / CCM 5965 / CIP 105453 / JCM 11297 / NRS T15;
RX   PubMed=7629164; DOI=10.1074/jbc.270.31.18396;
RA   Koike-Takeshita A., Koyama T., Obata S., Ogura K.;
RT   "Molecular cloning and nucleotide sequences of the genes for two essential
RT   proteins constituting a novel enzyme system for heptaprenyl diphosphate
RT   synthesis.";
RL   J. Biol. Chem. 270:18396-18400(1995).
CC   -!- FUNCTION: Supplies heptaprenyl diphosphate, the precursor for the side
CC       chain of the isoprenoid quinone menaquinone-7 (MQ-7).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E,6E)-farnesyl diphosphate + 4 isopentenyl diphosphate =
CC         all-trans-heptaprenyl diphosphate + 4 diphosphate;
CC         Xref=Rhea:RHEA:27794, ChEBI:CHEBI:33019, ChEBI:CHEBI:58206,
CC         ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.30;
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   -!- SUBUNIT: Heterodimer of component I and II.
CC   -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR   EMBL; D49976; BAA08725.1; -; Genomic_DNA.
DR   RefSeq; WP_033009740.1; NZ_RCTK01000002.1.
DR   AlphaFoldDB; P55785; -.
DR   SMR; P55785; -.
DR   GeneID; 58572464; -.
DR   BRENDA; 2.5.1.30; 623.
DR   GO; GO:0036422; F:heptaprenyl diphosphate synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016765; F:transferase activity, transferring alkyl or aryl (other than methyl) groups; IDA:UniProtKB.
DR   GO; GO:0008299; P:isoprenoid biosynthetic process; IEA:UniProtKB-KW.
DR   GO; GO:0009234; P:menaquinone biosynthetic process; ISS:UniProtKB.
DR   CDD; cd00685; Trans_IPPS_HT; 1.
DR   Gene3D; 1.10.600.10; -; 1.
DR   InterPro; IPR014119; GerC3_HepT.
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   TIGRFAMs; TIGR02748; GerC3_HepT; 1.
DR   PROSITE; PS00723; POLYPRENYL_SYNTHASE_1; 1.
DR   PROSITE; PS00444; POLYPRENYL_SYNTHASE_2; 1.
PE   3: Inferred from homology;
KW   Isoprene biosynthesis; Magnesium; Metal-binding; Transferase.
FT   CHAIN           1..320
FT                   /note="Heptaprenyl diphosphate synthase component 2"
FT                   /id="PRO_0000124003"
FT   BINDING         45
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         48
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         77
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:Q12051"
FT   BINDING         84
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         84
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         88
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         88
FT                   /ligand="Mg(2+)"
FT                   /ligand_id="ChEBI:CHEBI:18420"
FT                   /ligand_label="2"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         93
FT                   /ligand="all-trans-hexaprenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58179"
FT                   /evidence="ECO:0000250"
FT   BINDING         94
FT                   /ligand="isopentenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:128769"
FT                   /evidence="ECO:0000250|UniProtKB:P14324"
FT   BINDING         170
FT                   /ligand="all-trans-hexaprenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58179"
FT                   /evidence="ECO:0000250"
FT   BINDING         171
FT                   /ligand="all-trans-hexaprenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58179"
FT                   /evidence="ECO:0000250"
FT   BINDING         208
FT                   /ligand="all-trans-hexaprenyl diphosphate"
FT                   /ligand_id="ChEBI:CHEBI:58179"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   320 AA;  35808 MW;  A51B6630E6B88F46 CRC64;
     MKLKAMYSFL SDDLAAVEEE LERAVQSEYG PLGEAALHLL QAGGKRIRPV FVLLAARFGQ
     YDLERMKHVA VALELIHMAS LVHDDVIDDA DLRRGRPTIK AKWSNRFAMY TGDYLFARSL
     ERMAELGNPR AHQVLAKTIV EVCRGEIEQI KDKYRFDQPL RTYLRRIRRK TALLIAASCQ
     LGALAAGAPE PIVKRLYWFG HYVGMSFQIT DDILDFTGTE EQLGKPAGSD LLQGNVTLPV
     LYALSDERVK AAIAAVGPET DVAEMAAVIS AIKRTDAIER SYALSDRYLD KALHLLDGLP
     MNEARGLLRD LALYIGKRDY