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 22-APR-2020, entry version 68. 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}; 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)-butenyl CC 4-diphosphate (HMBPP) into a mixture of isopentenyl diphosphate (IPP) CC and dimethylallyl diphosphate (DMAPP). Acts in the terminal step of the CC DOXP/MEP pathway for isoprenoid precursor biosynthesis. CC {ECO:0000255|HAMAP-Rule:MF_00191}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + isopentenyl diphosphate + 2 oxidized [2Fe-2S]- CC [ferredoxin] = (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) CC + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:24488, Rhea:RHEA- CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, CC ChEBI:CHEBI:128753, ChEBI:CHEBI:128769; EC=1.17.7.4; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00191}; CC -!- CATALYTIC ACTIVITY: CC Reaction=dimethylallyl diphosphate + H2O + 2 oxidized [2Fe-2S]- CC [ferredoxin] = (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 H(+) CC + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:24825, Rhea:RHEA- CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, CC ChEBI:CHEBI:57623, ChEBI:CHEBI:128753; EC=1.17.7.4; CC Evidence={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-Rule:MF_00191}. CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis CC via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5- CC phosphate: step 6/6. {ECO:0000255|HAMAP-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 KO; K03527; -. DR OMA; HNKYVVD; -. DR BioCyc; BCER572264:G1GV1-4457-MONOMER; -. 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-UniRule. DR GO; GO:0051745; F:4-hydroxy-3-methylbut-2-en-1-yl diphosphate reductase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0050992; P:dimethylallyl diphosphate biosynthetic process; IEA:UniProtKB-UniRule. DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-UniRule. DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-UniRule. 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; Iron; Iron-sulfur; Isoprene biosynthesis; Metal-binding; KW Oxidoreductase. FT CHAIN 1..316 FT /note="4-hydroxy-3-methylbut-2-enyl diphosphate reductase" FT /id="PRO_1000124275" FT REGION 226..228 FT /note="Substrate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT ACT_SITE 133 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT METAL 12 FT /note="Iron-sulfur (4Fe-4S)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT METAL 103 FT /note="Iron-sulfur (4Fe-4S)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT METAL 198 FT /note="Iron-sulfur (4Fe-4S)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 43 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 81 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 131 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 170 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 271 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-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 //