ID ISPH_BACC3 Reviewed; 316 AA. AC C1ESI2; DT 28-JUL-2009, integrated into UniProtKB/Swiss-Prot. DT 26-MAY-2009, sequence version 1. DT 25-OCT-2017, entry version 62. DE RecName: Full=4-hydroxy-3-methylbut-2-enyl diphosphate reductase {ECO:0000255|HAMAP-Rule:MF_00191}; DE Short=HMBPP reductase {ECO:0000255|HAMAP-Rule:MF_00191}; DE EC=1.17.7.4 {ECO:0000255|HAMAP-Rule:MF_00191}; GN Name=ispH {ECO:0000255|HAMAP-Rule:MF_00191}; GN OrderedLocusNames=BCA_4399; OS Bacillus cereus (strain 03BB102). OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus; OC Bacillus cereus group. OX NCBI_TaxID=572264; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=03BB102; RA Dodson R.J., Jackson P., Munk A.C., Brettin T., Bruce D., Detter C., RA Tapia R., Han C., Sutton G., Sims D.; RT "Genome sequence of Bacillus cereus 03BB102."; RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Catalyzes the conversion of 1-hydroxy-2-methyl-2-(E)- CC butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl CC diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in CC the terminal step of the DOXP/MEP pathway for isoprenoid precursor CC biosynthesis. {ECO:0000255|HAMAP-Rule:MF_00191}. CC -!- CATALYTIC ACTIVITY: Isopentenyl diphosphate + 2 oxidized CC ferredoxin [iron-sulfur] cluster + H(2)O = (E)-4-hydroxy-3- CC methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron- CC sulfur] cluster + 2 H(+). {ECO:0000255|HAMAP-Rule:MF_00191}. CC -!- CATALYTIC ACTIVITY: Dimethylallyl diphosphate + 2 oxidized CC ferredoxin [iron-sulfur] cluster + H(2)O = (E)-4-hydroxy-3- CC methylbut-2-en-1-yl diphosphate + 2 reduced ferredoxin [iron- CC sulfur] cluster + 2 H(+). {ECO:0000255|HAMAP-Rule:MF_00191}. CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00191}; CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000255|HAMAP- CC Rule:MF_00191}; CC -!- PATHWAY: Isoprenoid biosynthesis; dimethylallyl diphosphate CC biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3- CC methylbutenyl diphosphate: step 1/1. {ECO:0000255|HAMAP- CC Rule:MF_00191}. CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate CC biosynthesis via DXP pathway; isopentenyl diphosphate from 1- CC deoxy-D-xylulose 5-phosphate: step 6/6. {ECO:0000255|HAMAP- CC Rule:MF_00191}. CC -!- SIMILARITY: Belongs to the IspH family. {ECO:0000255|HAMAP- CC Rule:MF_00191}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP001407; ACO28637.1; -; Genomic_DNA. DR RefSeq; WP_000706665.1; NZ_CP009318.1. DR SMR; C1ESI2; -. DR EnsemblBacteria; ACO28637; ACO28637; BCA_4399. DR KEGG; bcx:BCA_4399; -. DR PATRIC; fig|572264.18.peg.4347; -. DR HOGENOM; HOG000220192; -. DR KO; K03527; -. DR OMA; TKVHKEA; -. DR UniPathway; UPA00056; UER00097. DR UniPathway; UPA00059; UER00105. DR Proteomes; UP000002210; Chromosome. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0051745; F:4-hydroxy-3-methylbut-2-en-1-yl diphosphate reductase activity; IEA:InterPro. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0050992; P:dimethylallyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniPathway. DR CDD; cd13944; lytB_ispH; 1. DR HAMAP; MF_00191; IspH; 1. DR InterPro; IPR003451; LytB/IspH. DR PANTHER; PTHR30426; PTHR30426; 1. DR Pfam; PF02401; LYTB; 1. DR TIGRFAMs; TIGR00216; ispH_lytB; 1. PE 3: Inferred from homology; KW 4Fe-4S; Complete proteome; Iron; Iron-sulfur; Isoprene biosynthesis; KW Metal-binding; Oxidoreductase. FT CHAIN 1 316 4-hydroxy-3-methylbut-2-enyl diphosphate FT reductase. FT /FTId=PRO_1000124275. FT REGION 226 228 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00191}. FT ACT_SITE 133 133 Proton donor. {ECO:0000255|HAMAP- FT Rule:MF_00191}. FT METAL 12 12 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00191}. FT METAL 103 103 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00191}. FT METAL 198 198 Iron-sulfur (4Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00191}. FT BINDING 43 43 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00191}. FT BINDING 81 81 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00191}. FT BINDING 131 131 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00191}. FT BINDING 170 170 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00191}. FT BINDING 271 271 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00191}. SQ SEQUENCE 316 AA; 34939 MW; 6C2B8D19112976BB CRC64; MKIVKISPRG YCYGVVDAMV IARNAALDTS LPRPIYILGM IVHNKHVTDA FEEDGIITLD GPSRLDILDK IDSGTVIFTA HGVSPEVKQR AKEKGLTTID ATCPDVTKTH DLIEAKKAEG YHVIYIGKKN HPEPEGAVGI APDIVHLIEK ADDLKTLEIP TDKILVTNQT TMSQWDVQHL MEDIQKKFPT AEFHKEICLA TQVRQEAVAK QADVADLTIV VGDPKSNNSN RLAQVSQEIA GTKAYRVADV SEIKLEWLQG VENVAVTAGA STPTPITKEV IAFLEQYDPM NPATWERVRK VPLQKILPRV KVKKEQ //