ISPB_SHIFL
ID ISPB_SHIFL Reviewed; 323 AA.
AC P0AD58; P19641;
DT 06-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 06-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 99.
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=SF3227, S3445;
OS Shigella flexneri.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Shigella.
OX NCBI_TaxID=623;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=301 / Serotype 2a;
RX PubMed=12384590; DOI=10.1093/nar/gkf566;
RA Jin Q., Yuan Z., Xu J., Wang Y., Shen Y., Lu W., Wang J., Liu H., Yang J.,
RA Yang F., Zhang X., Zhang J., Yang G., Wu H., Qu D., Dong J., Sun L.,
RA Xue Y., Zhao A., Gao Y., Zhu J., Kan B., Ding K., Chen S., Cheng H.,
RA Yao Z., He B., Chen R., Ma D., Qiang B., Wen Y., Hou Y., Yu J.;
RT "Genome sequence of Shigella flexneri 2a: insights into pathogenicity
RT through comparison with genomes of Escherichia coli K12 and O157.";
RL Nucleic Acids Res. 30:4432-4441(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700930 / 2457T / Serotype 2a;
RX PubMed=12704152; DOI=10.1128/iai.71.5.2775-2786.2003;
RA Wei J., Goldberg M.B., Burland V., Venkatesan M.M., Deng W., Fournier G.,
RA Mayhew G.F., Plunkett G. III, Rose D.J., Darling A., Mau B., Perna N.T.,
RA Payne S.M., Runyen-Janecky L.J., Zhou S., Schwartz D.C., Blattner F.R.;
RT "Complete genome sequence and comparative genomics of Shigella flexneri
RT serotype 2a strain 2457T.";
RL Infect. Immun. 71:2775-2786(2003).
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; AE005674; AAN44693.1; -; Genomic_DNA.
DR EMBL; AE014073; AAP18507.1; -; Genomic_DNA.
DR RefSeq; NP_708986.1; NC_004337.2.
DR RefSeq; WP_001047336.1; NZ_WPGW01000004.1.
DR AlphaFoldDB; P0AD58; -.
DR SMR; P0AD58; -.
DR STRING; 198214.SF3227; -.
DR EnsemblBacteria; AAN44693; AAN44693; SF3227.
DR EnsemblBacteria; AAP18507; AAP18507; S3445.
DR GeneID; 1024423; -.
DR GeneID; 66672911; -.
DR KEGG; sfl:SF3227; -.
DR KEGG; sfx:S3445; -.
DR PATRIC; fig|198214.7.peg.3828; -.
DR HOGENOM; CLU_014015_2_0_6; -.
DR OMA; GKQMRPM; -.
DR OrthoDB; 1861068at2; -.
DR Proteomes; UP000001006; Chromosome.
DR Proteomes; UP000002673; 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: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 3: Inferred from homology;
KW Isoprene biosynthesis; Magnesium; Metal-binding; Reference proteome;
KW Transferase.
FT CHAIN 1..323
FT /note="Octaprenyl diphosphate synthase"
FT /id="PRO_0000124007"
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"
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
