HEXPP_SACS2
ID HEXPP_SACS2 Reviewed; 281 AA.
AC Q97W92;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Hexaprenyl pyrophosphate synthase;
DE Short=HexPP;
DE EC=2.5.1.82 {ECO:0000269|PubMed:11790729, ECO:0000269|PubMed:16291686};
DE AltName: Full=Medium-chain HexPP;
GN Name=gdS-2; OrderedLocusNames=SSO2345;
OS Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)
OS (Sulfolobus solfataricus).
OC Archaea; Crenarchaeota; Thermoprotei; Sulfolobales; Sulfolobaceae;
OC Saccharolobus.
OX NCBI_TaxID=273057;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35092 / DSM 1617 / JCM 11322 / P2;
RX PubMed=11427726; DOI=10.1073/pnas.141222098;
RA She Q., Singh R.K., Confalonieri F., Zivanovic Y., Allard G., Awayez M.J.,
RA Chan-Weiher C.C.-Y., Clausen I.G., Curtis B.A., De Moors A., Erauso G.,
RA Fletcher C., Gordon P.M.K., Heikamp-de Jong I., Jeffries A.C., Kozera C.J.,
RA Medina N., Peng X., Thi-Ngoc H.P., Redder P., Schenk M.E., Theriault C.,
RA Tolstrup N., Charlebois R.L., Doolittle W.F., Duguet M., Gaasterland T.,
RA Garrett R.A., Ragan M.A., Sensen C.W., Van der Oost J.;
RT "The complete genome of the crenarchaeon Sulfolobus solfataricus P2.";
RL Proc. Natl. Acad. Sci. U.S.A. 98:7835-7840(2001).
RN [2]
RP FUNCTION AS A HEXAPRENYL PYROPHOSPHATE SYNTHASE, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, AND COFACTOR.
RX PubMed=11790729; DOI=10.1128/jb.184.3.615-620.2002;
RA Hemmi H., Ikejiri S., Yamashita S., Nishino T.;
RT "Novel medium-chain prenyl diphosphate synthase from the thermoacidophilic
RT archaeon Sulfolobus solfataricus.";
RL J. Bacteriol. 184:615-620(2002).
RN [3] {ECO:0007744|PDB:2AZJ, ECO:0007744|PDB:2AZK}
RP X-RAY CRYSTALLOGRAPHY (2.40 ANGSTROMS) OF MUTANT CYS-81, MUTAGENESIS OF
RP TYR-124; LEU-164 AND TYR-174, FUNCTION, CATALYTIC ACTIVITY, SUBSTRATE
RP SPECIFICITY, AND SUBUNIT.
RX PubMed=16291686; DOI=10.1128/jb.187.23.8137-8148.2005;
RA Sun H.Y., Ko T.P., Kuo C.J., Guo R.T., Chou C.C., Liang P.H., Wang A.H.;
RT "Homodimeric hexaprenyl pyrophosphate synthase from the thermoacidophilic
RT crenarchaeon Sulfolobus solfataricus displays asymmetric subunit
RT structures.";
RL J. Bacteriol. 187:8137-8148(2005).
CC -!- FUNCTION: Catalyzes consecutive E-type condensation of two isopentenyl
CC pyrophosphate (IPP) molecules with an allylic substrate such as
CC geranylgeranyl diphosphate (GGPP), farnesyl diphosphate (FPP) or
CC geranyl diphosphate (GPP) to yield the medium-chain product trans-C30-
CC hexaprenyl pyrophosphate (HexPP). GGPP is the physiological substrate.
CC {ECO:0000269|PubMed:11790729, ECO:0000269|PubMed:16291686}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E,10E)-geranylgeranyl diphosphate + 2 isopentenyl
CC diphosphate = all-trans-hexaprenyl diphosphate + 2 diphosphate;
CC Xref=Rhea:RHEA:27555, ChEBI:CHEBI:33019, ChEBI:CHEBI:58179,
CC ChEBI:CHEBI:58756, ChEBI:CHEBI:128769; EC=2.5.1.82;
CC Evidence={ECO:0000269|PubMed:11790729, ECO:0000269|PubMed:16291686};
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC Evidence={ECO:0000269|PubMed:11790729};
CC Note=Binds 2 Mg(2+) ions per subunit. {ECO:0000250|UniProtKB:P14324};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC pH dependence:
CC Optimum pH is 6. {ECO:0000269|PubMed:11790729};
CC Temperature dependence:
CC Highly thermostable, remains fully active after 2 hours at 80 degrees
CC Celsius. {ECO:0000269|PubMed:11790729};
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:16291686,
CC ECO:0000305|PubMed:11790729}.
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; AE006641; AAK42496.1; -; Genomic_DNA.
DR PIR; A99405; A99405.
DR RefSeq; WP_009989514.1; NC_002754.1.
DR PDB; 2AZJ; X-ray; 2.40 A; A/B=1-281.
DR PDB; 2AZK; X-ray; 2.70 A; A/B=1-281.
DR PDBsum; 2AZJ; -.
DR PDBsum; 2AZK; -.
DR AlphaFoldDB; Q97W92; -.
DR SMR; Q97W92; -.
DR STRING; 273057.SSO2345; -.
DR PRIDE; Q97W92; -.
DR EnsemblBacteria; AAK42496; AAK42496; SSO2345.
DR GeneID; 44128070; -.
DR KEGG; sso:SSO2345; -.
DR PATRIC; fig|273057.12.peg.2429; -.
DR eggNOG; arCOG01727; Archaea.
DR HOGENOM; CLU_014015_5_0_2; -.
DR InParanoid; Q97W92; -.
DR OMA; WLIAESI; -.
DR PhylomeDB; Q97W92; -.
DR BioCyc; MetaCyc:MON-15679; -.
DR BRENDA; 2.5.1.82; 6163.
DR EvolutionaryTrace; Q97W92; -.
DR Proteomes; UP000001974; Chromosome.
DR GO; GO:0052922; F:hexaprenyl diphosphate synthase (geranylgeranyl-diphosphate specific) activity; IDA:UniProtKB.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004659; F:prenyltransferase activity; IBA:GO_Central.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IDA:UniProtKB.
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; PS00444; POLYPRENYL_SYNTHASE_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Isoprene biosynthesis; Magnesium; Metal-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..281
FT /note="Hexaprenyl pyrophosphate synthase"
FT /id="PRO_0000418599"
FT BINDING 42
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 45
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 74
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:Q12051"
FT BINDING 81
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 81
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 85
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 85
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT BINDING 91
FT /ligand="isopentenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:128769"
FT /evidence="ECO:0000250|UniProtKB:P14324"
FT MUTAGEN 124
FT /note="Y->A: Generates the same C30 product as the wild-
FT type."
FT /evidence="ECO:0000269|PubMed:16291686"
FT MUTAGEN 164
FT /note="L->A: Generates only one C5-prenyl unit longer C35
FT product."
FT /evidence="ECO:0000269|PubMed:16291686"
FT MUTAGEN 174
FT /note="Y->A: Generates the same C30 product as the wild-
FT type."
FT /evidence="ECO:0000269|PubMed:16291686"
FT HELIX 2..24
FT /evidence="ECO:0007829|PDB:2AZJ"
FT TURN 28..30
FT /evidence="ECO:0007829|PDB:2AZJ"
FT HELIX 31..38
FT /evidence="ECO:0007829|PDB:2AZJ"
FT HELIX 44..55
FT /evidence="ECO:0007829|PDB:2AZJ"
FT HELIX 60..63
FT /evidence="ECO:0007829|PDB:2AZJ"
FT HELIX 64..84
FT /evidence="ECO:0007829|PDB:2AZJ"
FT STRAND 89..94
FT /evidence="ECO:0007829|PDB:2AZJ"
FT HELIX 96..124
FT /evidence="ECO:0007829|PDB:2AZJ"
FT HELIX 126..145
FT /evidence="ECO:0007829|PDB:2AZJ"
FT TURN 146..150
FT /evidence="ECO:0007829|PDB:2AZJ"
FT HELIX 153..160
FT /evidence="ECO:0007829|PDB:2AZJ"
FT HELIX 162..175
FT /evidence="ECO:0007829|PDB:2AZJ"
FT HELIX 179..181
FT /evidence="ECO:0007829|PDB:2AZJ"
FT HELIX 182..205
FT /evidence="ECO:0007829|PDB:2AZJ"
FT TURN 210..212
FT /evidence="ECO:0007829|PDB:2AZJ"
FT HELIX 217..220
FT /evidence="ECO:0007829|PDB:2AZJ"
FT HELIX 221..224
FT /evidence="ECO:0007829|PDB:2AZJ"
FT TURN 225..227
FT /evidence="ECO:0007829|PDB:2AZJ"
FT HELIX 229..249
FT /evidence="ECO:0007829|PDB:2AZJ"
FT HELIX 255..257
FT /evidence="ECO:0007829|PDB:2AZJ"
FT HELIX 258..262
FT /evidence="ECO:0007829|PDB:2AZJ"
FT HELIX 264..274
FT /evidence="ECO:0007829|PDB:2AZJ"
SQ SEQUENCE 281 AA; 32275 MW; AD14ABD58DE76CCB CRC64;
MSIIEFWLEA KATIDRLIEQ FLNSNRDWDL VDISSYILKD GKRFRGTLNM FFTVALGGDI
KDSYGGALAI EILHSASLAL DDIVDLDATR RGDKAAWVVY GNRKVIFITN YLIPTALRII
QTSYGDDALN TSIELWKDTS VGALRDMYDN SDYIRTIELK TGSLFKLSTV LSAYASKHYN
TKQQMLDVGK YLGIIYQVID DFVDYKTKKV EEIDGSAKQL FKYYREGKLE EYVRSVYLEY
KQKYDELISN IPFQSKYLSE IRSLPEFLAN GLLKEANIDK I
