ISPB_HAEIN
ID ISPB_HAEIN Reviewed; 329 AA.
AC P44916;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 113.
DE RecName: Full=Octaprenyl diphosphate synthase;
DE EC=2.5.1.90;
DE AltName: Full=All-trans-octaprenyl-diphosphate synthase;
DE AltName: Full=Octaprenyl pyrophosphate synthase;
DE Short=OPP synthase;
GN Name=ispB; OrderedLocusNames=HI_0881;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=10675023;
RX DOI=10.1002/(sici)1522-2683(20000101)21:2<411::aid-elps411>3.0.co;2-4;
RA Langen H., Takacs B., Evers S., Berndt P., Lahm H.W., Wipf B., Gray C.,
RA Fountoulakis M.;
RT "Two-dimensional map of the proteome of Haemophilus influenzae.";
RL Electrophoresis 21:411-429(2000).
CC -!- FUNCTION: Supplies octaprenyl diphosphate, the precursor for the side
CC chain of the isoprenoid quinones ubiquinone and menaquinone.
CC {ECO:0000250}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2E,6E)-farnesyl diphosphate + 5 isopentenyl diphosphate =
CC all-trans-octaprenyl diphosphate + 5 diphosphate;
CC Xref=Rhea:RHEA:27798, ChEBI:CHEBI:33019, ChEBI:CHEBI:57711,
CC ChEBI:CHEBI:128769, ChEBI:CHEBI:175763; EC=2.5.1.90;
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 -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; L42023; AAC22540.1; -; Genomic_DNA.
DR PIR; I64160; I64160.
DR RefSeq; NP_439042.1; NC_000907.1.
DR RefSeq; WP_005693233.1; NC_000907.1.
DR AlphaFoldDB; P44916; -.
DR SMR; P44916; -.
DR STRING; 71421.HI_0881; -.
DR PRIDE; P44916; -.
DR EnsemblBacteria; AAC22540; AAC22540; HI_0881.
DR KEGG; hin:HI_0881; -.
DR PATRIC; fig|71421.8.peg.923; -.
DR eggNOG; COG0142; Bacteria.
DR HOGENOM; CLU_014015_2_0_6; -.
DR OMA; GKQMRPM; -.
DR PhylomeDB; P44916; -.
DR BioCyc; HINF71421:G1GJ1-921-MON; -.
DR BRENDA; 2.5.1.90; 2529.
DR Proteomes; UP000000579; Chromosome.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0106350; F:octaprenyl pyrophosphate synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0004659; F:prenyltransferase activity; IBA:GO_Central.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IBA:GO_Central.
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 Isoprene biosynthesis; Magnesium; Metal-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..329
FT /note="Octaprenyl diphosphate synthase"
FT /id="PRO_0000124006"
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 176
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 177
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 214
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
SQ SEQUENCE 329 AA; 35912 MW; 65DBC4CCDAD72E04 CRC64;
MKKQDLMSID EIQKLADPDM QKVNQNILAQ LNSDVPLIGQ LGFYIVQGGG KRIRPLIAVL
AARSLGFEGS NSITCATFVE FIHTASLLHD DVVDESDMRR GRATANAEFG NAASVLVGDF
IYTRAFQLVA QLESLKILSI MADATNVLAE GEVQQLMNVN DPETSEANYM RVIYSKTARL
FEVAGQAAAI VAGGTEAQEK ALQDYGRYLG TAFQLVDDVL DYSANTQALG KNVGDDLAEG
KPTLPLLHAM RHGNAQQAAL IREAIEQGGK REAIDEVLAI MTEHKSLDYA MNRAKEEAQK
AVDAIEILPE SEYKQALISL AYLSVDRNY
