ISPB_ECOLI
ID ISPB_ECOLI Reviewed; 323 AA.
AC P0AD57; P19641; Q2M925;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Octaprenyl diphosphate synthase {ECO:0000303|PubMed:8037730};
DE EC=2.5.1.90 {ECO:0000269|PubMed:8037730};
DE AltName: Full=All-trans-octaprenyl-diphosphate synthase;
DE AltName: Full=Octaprenyl pyrophosphate synthase;
DE Short=OPP synthase;
GN Name=ispB; Synonyms=cel, yhbD; OrderedLocusNames=b3187, JW3154;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=8312607; DOI=10.3109/10425179309015624;
RA Jeong J.H., Kitakawa M.S., Isono S., Isono K.;
RT "Cloning and nucleotide sequencing of the genes, rpIU and rpmA, for
RT ribosomal proteins L21 and L27 of Escherichia coli.";
RL DNA Seq. 4:59-67(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 196-323.
RX PubMed=2670911; DOI=10.1128/jb.171.9.5222-5225.1989;
RA Choi Y.-L., Nishida T., Kawamukai M., Utsumi R., Sakai H., Komano T.;
RT "Cloning and sequencing of an Escherichia coli gene, nlp, highly homologous
RT to the ner genes of bacteriophages Mu and D108.";
RL J. Bacteriol. 171:5222-5225(1989).
RN [5]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RC STRAIN=K12 / JM109 / ATCC 53323;
RX PubMed=8037730; DOI=10.1006/bbrc.1994.1933;
RA Asai K., Fujisaki S., Nishimura Y., Nishino T., Okada K., Nakagawa T.,
RA Kawamukai M., Matsuda H.;
RT "The identification of Escherichia coli ispB (cel) gene encoding the
RT octaprenyl diphosphate synthase.";
RL Biochem. Biophys. Res. Commun. 202:340-345(1994).
CC -!- FUNCTION: Supplies octaprenyl diphosphate, the precursor for the side
CC chain of the isoprenoid quinones ubiquinone and menaquinone.
CC {ECO:0000269|PubMed:8037730}.
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 Evidence={ECO:0000269|PubMed:8037730};
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 -!- INTERACTION:
CC P0AD57; P0AD57: ispB; NbExp=2; IntAct=EBI-1131851, EBI-1131851;
CC P0AD57; O13851: dlp1; Xeno; NbExp=2; IntAct=EBI-1131851, EBI-7701234;
CC P0AD57; O43091: dps1; Xeno; NbExp=2; IntAct=EBI-1131851, EBI-7701164;
CC -!- SIMILARITY: Belongs to the FPP/GGPP synthase family. {ECO:0000305}.
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DR EMBL; D13267; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; U18997; AAA57988.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76219.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77231.1; -; Genomic_DNA.
DR EMBL; X68873; CAA48735.1; -; Genomic_DNA.
DR PIR; E65109; E65109.
DR RefSeq; NP_417654.1; NC_000913.3.
DR RefSeq; WP_001047336.1; NZ_STEB01000012.1.
DR PDB; 5ZE6; X-ray; 2.50 A; A/B/C/D=1-323.
DR PDB; 5ZLF; X-ray; 2.85 A; A/B/C/D=1-323.
DR PDBsum; 5ZE6; -.
DR PDBsum; 5ZLF; -.
DR AlphaFoldDB; P0AD57; -.
DR SMR; P0AD57; -.
DR BioGRID; 4261111; 137.
DR BioGRID; 851687; 3.
DR IntAct; P0AD57; 5.
DR MINT; P0AD57; -.
DR STRING; 511145.b3187; -.
DR ChEMBL; CHEMBL3309021; -.
DR jPOST; P0AD57; -.
DR PaxDb; P0AD57; -.
DR PRIDE; P0AD57; -.
DR DNASU; 947364; -.
DR EnsemblBacteria; AAC76219; AAC76219; b3187.
DR EnsemblBacteria; BAE77231; BAE77231; BAE77231.
DR GeneID; 66672911; -.
DR GeneID; 947364; -.
DR KEGG; ecj:JW3154; -.
DR KEGG; eco:b3187; -.
DR PATRIC; fig|1411691.4.peg.3544; -.
DR EchoBASE; EB0017; -.
DR eggNOG; COG0142; Bacteria.
DR HOGENOM; CLU_014015_2_0_6; -.
DR InParanoid; P0AD57; -.
DR OMA; GKQMRPM; -.
DR PhylomeDB; P0AD57; -.
DR BioCyc; EcoCyc:OPPSYN-MON; -.
DR BioCyc; MetaCyc:OPPSYN-MON; -.
DR BRENDA; 2.5.1.90; 2026.
DR SABIO-RK; P0AD57; -.
DR PRO; PR:P0AD57; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
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; IDA:EcoCyc.
DR GO; GO:0008299; P:isoprenoid biosynthetic process; IBA:GO_Central.
DR GO; GO:0016094; P:polyprenol biosynthetic process; IMP:EcoCyc.
DR GO; GO:0006744; P:ubiquinone biosynthetic process; IMP:EcoCyc.
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; Isoprene biosynthesis; Magnesium; Metal-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..323
FT /note="Octaprenyl diphosphate synthase"
FT /id="PRO_0000124005"
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="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
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="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 171
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT BINDING 208
FT /ligand="an all-trans-polyprenyl diphosphate"
FT /ligand_id="ChEBI:CHEBI:58914"
FT /evidence="ECO:0000250"
FT HELIX 3..24
FT /evidence="ECO:0007829|PDB:5ZE6"
FT HELIX 30..40
FT /evidence="ECO:0007829|PDB:5ZE6"
FT HELIX 47..58
FT /evidence="ECO:0007829|PDB:5ZE6"
FT HELIX 65..87
FT /evidence="ECO:0007829|PDB:5ZE6"
FT STRAND 91..93
FT /evidence="ECO:0007829|PDB:5ZE6"
FT HELIX 99..103
FT /evidence="ECO:0007829|PDB:5ZE6"
FT HELIX 105..124
FT /evidence="ECO:0007829|PDB:5ZE6"
FT TURN 125..127
FT /evidence="ECO:0007829|PDB:5ZE6"
FT HELIX 129..151
FT /evidence="ECO:0007829|PDB:5ZE6"
FT HELIX 160..169
FT /evidence="ECO:0007829|PDB:5ZE6"
FT TURN 170..172
FT /evidence="ECO:0007829|PDB:5ZE6"
FT HELIX 173..185
FT /evidence="ECO:0007829|PDB:5ZE6"
FT HELIX 190..214
FT /evidence="ECO:0007829|PDB:5ZE6"
FT HELIX 229..232
FT /evidence="ECO:0007829|PDB:5ZE6"
FT HELIX 238..246
FT /evidence="ECO:0007829|PDB:5ZE6"
FT HELIX 249..261
FT /evidence="ECO:0007829|PDB:5ZE6"
FT HELIX 268..278
FT /evidence="ECO:0007829|PDB:5ZE6"
FT HELIX 280..298
FT /evidence="ECO:0007829|PDB:5ZE6"
FT HELIX 299..301
FT /evidence="ECO:0007829|PDB:5ZE6"
FT HELIX 306..318
FT /evidence="ECO:0007829|PDB:5ZE6"
SQ SEQUENCE 323 AA; 35217 MW; 08AD7AE7AC230EF8 CRC64;
MNLEKINELT AQDMAGVNAA ILEQLNSDVQ LINQLGYYIV SGGGKRIRPM IAVLAARAVG
YEGNAHVTIA ALIEFIHTAT LLHDDVVDES DMRRGKATAN AAFGNAASVL VGDFIYTRAF
QMMTSLGSLK VLEVMSEAVN VIAEGEVLQL MNVNDPDITE ENYMRVIYSK TARLFEAAAQ
CSGILAGCTP EEEKGLQDYG RYLGTAFQLI DDLLDYNADG EQLGKNVGDD LNEGKPTLPL
LHAMHHGTPE QAQMIRTAIE QGNGRHLLEP VLEAMNACGS LEWTRQRAEE EADKAIAALQ
VLPDTPWREA LIGLAHIAVQ RDR
