ID B2JPR0_PARP8 Unreviewed; 314 AA. AC B2JPR0; DT 10-JUN-2008, integrated into UniProtKB/TrEMBL. DT 10-JUN-2008, sequence version 1. DT 02-SEP-2026, entry version 94. DE RecName: Full=4-hydroxy-3-methylbut-2-enyl diphosphate reductase {ECO:0000256|HAMAP-Rule:MF_00191}; DE Short=HMBPP reductase {ECO:0000256|HAMAP-Rule:MF_00191}; DE EC=1.17.7.4 {ECO:0000256|HAMAP-Rule:MF_00191}; GN Name=ispH {ECO:0000256|HAMAP-Rule:MF_00191}; GN OrderedLocusNames=Bphy_4130 {ECO:0000313|EMBL:ACC73251.1}; OS Paraburkholderia phymatum (strain DSM 17167 / CIP 108236 / LMG 21445 / OS STM815) (Burkholderia phymatum). OC Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; OC Burkholderiales; Burkholderiaceae; Paraburkholderia. OX NCBI_TaxID=391038 {ECO:0000313|EMBL:ACC73251.1, ECO:0000313|Proteomes:UP000001192}; RN [1] {ECO:0000313|Proteomes:UP000001192} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 17167 / CIP 108236 / LMG 21445 / STM815 RC {ECO:0000313|Proteomes:UP000001192}; RX PubMed=25197461; DOI=10.4056/sigs.4861021; RA Moulin L., Klonowska A., Caroline B., Booth K., Vriezen J.A., Melkonian R., RA James E.K., Young J.P., Bena G., Hauser L., Land M., Kyrpides N., Bruce D., RA Chain P., Copeland A., Pitluck S., Woyke T., Lizotte-Waniewski M., RA Bristow J., Riley M.; RT "Complete genome sequence of Burkholderia phymatum STM815(T), a broad host RT range and efficient nitrogen-fixing symbiont of Mimosa species."; RL Stand. Genomic Sci. 9:763-774(2014). 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:0000256|HAMAP-Rule:MF_00191}. CC -!- CATALYTIC ACTIVITY: CC Reaction=dimethylallyl diphosphate + 2 oxidized [2Fe-2S]-[ferredoxin] + CC H2O = (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 reduced [2Fe- CC 2S]-[ferredoxin] + 2 H(+); 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:0000256|HAMAP-Rule:MF_00191}; CC -!- CATALYTIC ACTIVITY: CC Reaction=isopentenyl diphosphate + 2 oxidized [2Fe-2S]-[ferredoxin] + CC H2O = (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 reduced [2Fe- CC 2S]-[ferredoxin] + 2 H(+); 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:0000256|HAMAP-Rule:MF_00191}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000256|HAMAP-Rule:MF_00191}; CC Note=Binds 1 [4Fe-4S] cluster per subunit. {ECO:0000256|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:0000256|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:0000256|HAMAP-Rule:MF_00191}. CC -!- SIMILARITY: Belongs to the IspH family. {ECO:0000256|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; CP001044; ACC73251.1; -; Genomic_DNA. DR RefSeq; WP_012403424.1; NC_010623.1. DR AlphaFoldDB; B2JPR0; -. DR STRING; 391038.Bphy_4130; -. DR KEGG; bph:Bphy_4130; -. DR eggNOG; COG0761; Bacteria. DR HOGENOM; CLU_027486_1_0_4; -. DR OrthoDB; 9804068at2; -. DR UniPathway; UPA00056; UER00097. DR UniPathway; UPA00059; UER00105. DR Proteomes; UP000001192; Chromosome 2. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-UniRule. DR GO; GO:0051745; F:4-hydroxy-3-methylbut-2-enyl diphosphate reductase activity; IEA:UniProtKB-UniRule. DR GO; GO:0046872; F:metal ion binding; IEA:InterPro. 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 Gene3D; 3.40.50.11270; -; 1. DR Gene3D; 3.40.1010.20; 4-hydroxy-3-methylbut-2-enyl diphosphate reductase, catalytic domain; 2. DR HAMAP; MF_00191; IspH; 1. DR InterPro; IPR003451; LytB/IspH. DR NCBIfam; TIGR00216; ispH_lytB; 1. DR NCBIfam; NF002188; PRK01045.1-2; 1. DR NCBIfam; NF002190; PRK01045.1-4; 1. DR PANTHER; PTHR30426; 4-HYDROXY-3-METHYLBUT-2-ENYL DIPHOSPHATE REDUCTASE; 1. DR PANTHER; PTHR30426:SF0; 4-HYDROXY-3-METHYLBUT-2-ENYL DIPHOSPHATE REDUCTASE; 1. DR Pfam; PF02401; LYTB; 1. PE 3: Inferred from homology; KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, ECO:0000256|HAMAP-Rule:MF_00191}; KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00191}; KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP- KW Rule:MF_00191}; Isoprene biosynthesis {ECO:0000256|HAMAP-Rule:MF_00191}; KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP- KW Rule:MF_00191}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00191, KW ECO:0000313|EMBL:ACC73251.1}; KW Reference proteome {ECO:0000313|Proteomes:UP000001192}. FT ACT_SITE 126 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 12 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 41 FT /ligand="(2E)-4-hydroxy-3-methylbut-2-enyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128753" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 41 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 41 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 74 FT /ligand="(2E)-4-hydroxy-3-methylbut-2-enyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128753" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 74 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 74 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 96 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 124 FT /ligand="(2E)-4-hydroxy-3-methylbut-2-enyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128753" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 124 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 124 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 164 FT /ligand="(2E)-4-hydroxy-3-methylbut-2-enyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128753" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 194 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 222 FT /ligand="(2E)-4-hydroxy-3-methylbut-2-enyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128753" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 222 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 222 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 223 FT /ligand="(2E)-4-hydroxy-3-methylbut-2-enyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128753" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 223 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 223 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 224 FT /ligand="(2E)-4-hydroxy-3-methylbut-2-enyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128753" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 224 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 224 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 266 FT /ligand="(2E)-4-hydroxy-3-methylbut-2-enyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128753" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 266 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 266 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" SQ SEQUENCE 314 AA; 33907 MW; 080299681213B0E0 CRC64; MRVILAQPRG FCAGVVRAIE IVDRALQQHG APVYVRHEIV HNRHVVDNLR QKGARFVEEL DEVPQGAVAI FSAHGVSQSV ERDAEQRGLD VLDATCPLVT KVHVQGRQYV AGGRTLILIG HAGHPEVEGT IGQIPGKVLL VQSEAEVAQL ELPIDTPLAY VTQTTLSVDD TRGIINALKR RFPDIVGPDT RDICYATQNR QAAVRELSSQ VDVLLVVGAT NSSNSNRLRE IGSESGVPSY LVADGSEIKP EWFANVTTVG ITAGASAPEE MVENVIDALR ALGPVDVTTM AGREEKVEFK LPSKLTQPLA AREV //