ID   ISPG_LYSSC              Reviewed;         371 AA.
AC   B1HSS4;
DT   24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT   29-APR-2008, sequence version 1.
DT   03-AUG-2022, entry version 90.
DE   RecName: Full=4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (flavodoxin) {ECO:0000255|HAMAP-Rule:MF_00159};
DE            EC=1.17.7.3 {ECO:0000255|HAMAP-Rule:MF_00159};
DE   AltName: Full=1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate synthase {ECO:0000255|HAMAP-Rule:MF_00159};
GN   Name=ispG {ECO:0000255|HAMAP-Rule:MF_00159}; OrderedLocusNames=Bsph_3646;
OS   Lysinibacillus sphaericus (strain C3-41).
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Lysinibacillus.
OX   NCBI_TaxID=444177;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C3-41;
RX   PubMed=18296527; DOI=10.1128/jb.01652-07;
RA   Hu X., Fan W., Han B., Liu H., Zheng D., Li Q., Dong W., Yan J., Gao M.,
RA   Berry C., Yuan Z.;
RT   "Complete genome sequence of the mosquitocidal bacterium Bacillus
RT   sphaericus C3-41 and comparison with those of closely related Bacillus
RT   species.";
RL   J. Bacteriol. 190:2892-2902(2008).
CC   -!- FUNCTION: Converts 2C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-
CC       2,4cPP) into 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate.
CC       {ECO:0000255|HAMAP-Rule:MF_00159}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) + H2O +
CC         oxidized [flavodoxin] = 2-C-methyl-D-erythritol 2,4-cyclic
CC         diphosphate + reduced [flavodoxin]; Xref=Rhea:RHEA:43604, Rhea:RHEA-
CC         COMP:10622, Rhea:RHEA-COMP:10623, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:57618, ChEBI:CHEBI:58210,
CC         ChEBI:CHEBI:58483, ChEBI:CHEBI:128753; EC=1.17.7.3;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00159};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00159};
CC       Note=Binds 1 [4Fe-4S] cluster. {ECO:0000255|HAMAP-Rule:MF_00159};
CC   -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis
CC       via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-
CC       phosphate: step 5/6. {ECO:0000255|HAMAP-Rule:MF_00159}.
CC   -!- SIMILARITY: Belongs to the IspG family. {ECO:0000255|HAMAP-
CC       Rule:MF_00159}.
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DR   EMBL; CP000817; ACA41132.1; -; Genomic_DNA.
DR   RefSeq; WP_012295189.1; NC_010382.1.
DR   AlphaFoldDB; B1HSS4; -.
DR   SMR; B1HSS4; -.
DR   EnsemblBacteria; ACA41132; ACA41132; Bsph_3646.
DR   KEGG; lsp:Bsph_3646; -.
DR   HOGENOM; CLU_042258_0_0_9; -.
DR   OMA; PTCGRTQ; -.
DR   UniPathway; UPA00056; UER00096.
DR   Proteomes; UP000002164; Chromosome.
DR   GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046429; F:4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniRule.
DR   Gene3D; 3.20.20.20; -; 1.
DR   Gene3D; 3.30.413.10; -; 1.
DR   HAMAP; MF_00159; IspG; 1.
DR   InterPro; IPR011005; Dihydropteroate_synth-like.
DR   InterPro; IPR016425; IspG_bac.
DR   InterPro; IPR004588; IspG_bac-typ.
DR   InterPro; IPR045854; NO2/SO3_Rdtase_4Fe4S_sf.
DR   PANTHER; PTHR30454; PTHR30454; 1.
DR   Pfam; PF04551; GcpE; 1.
DR   PIRSF; PIRSF004640; IspG; 1.
DR   SUPFAM; SSF51717; SSF51717; 1.
DR   SUPFAM; SSF56014; SSF56014; 1.
DR   TIGRFAMs; TIGR00612; ispG_gcpE; 1.
PE   3: Inferred from homology;
KW   4Fe-4S; Iron; Iron-sulfur; Isoprene biosynthesis; Metal-binding;
KW   Oxidoreductase.
FT   CHAIN           1..371
FT                   /note="4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase
FT                   (flavodoxin)"
FT                   /id="PRO_1000097168"
FT   BINDING         268
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00159"
FT   BINDING         271
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00159"
FT   BINDING         303
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00159"
FT   BINDING         310
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00159"
SQ   SEQUENCE   371 AA;  40015 MW;  064A03E63B57A5D0 CRC64;
     MSEICHRSNT RPVRVGNLTI GGSNELFIQS MCTTKTHDVE ATVAEILRLE EAGCQIVRVA
     VPDERAADAI AEIKKRIHIP LVADIHFDYR LALKAIENGI DKVRINPGNI GRKEKVEAVV
     NAAKAKGIPI RIGVNAGSLE RHILEKYGYP TADGMVESAL HHIKILEDLD FHDIIVSMKA
     SDVNLAIEAY EKAAKAFNYP LHLGITESGT LFAGTVKSAA GLGAILSKGI GNTLRISLSA
     DPVEEIKVAR ELLKSFGLAS NMATLISCPT CGRIEIDLIS IANEVEEYIS KLNVPLKVAV
     LGCAVNGPGE AREADIGIAG ARGEGLLFMK GKTVRKVPEE TMVEELKKEI DKLAAEMEEK
     RAAEEVQKAN A