ID ISPH_PSEPK Reviewed; 315 AA. AC Q88Q89; DT 31-OCT-2003, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2003, sequence version 1. DT 28-JAN-2026, entry version 117. 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=PP_0606; OS Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 OS / KT2440). OC Bacteria; Pseudomonadati; Pseudomonadota; Gammaproteobacteria; OC Pseudomonadales; Pseudomonadaceae; Pseudomonas. OX NCBI_TaxID=160488; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440; RX PubMed=12534463; DOI=10.1046/j.1462-2920.2002.00366.x; RA Nelson K.E., Weinel C., Paulsen I.T., Dodson R.J., Hilbert H., RA Martins dos Santos V.A.P., Fouts D.E., Gill S.R., Pop M., Holmes M., RA Brinkac L.M., Beanan M.J., DeBoy R.T., Daugherty S.C., Kolonay J.F., RA Madupu R., Nelson W.C., White O., Peterson J.D., Khouri H.M., Hance I., RA Chris Lee P., Holtzapple E.K., Scanlan D., Tran K., Moazzez A., RA Utterback T.R., Rizzo M., Lee K., Kosack D., Moestl D., Wedler H., RA Lauber J., Stjepandic D., Hoheisel J., Straetz M., Heim S., Kiewitz C., RA Eisen J.A., Timmis K.N., Duesterhoeft A., Tuemmler B., Fraser C.M.; RT "Complete genome sequence and comparative analysis of the metabolically RT versatile Pseudomonas putida KT2440."; RL Environ. Microbiol. 4:799-808(2002). 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=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:0000255|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: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; AE015451; AAN66232.1; -; Genomic_DNA. DR RefSeq; WP_010951872.1; NC_002947.4. DR AlphaFoldDB; Q88Q89; -. DR SMR; Q88Q89; -. DR STRING; 160488.PP_0606; -. DR PaxDb; 160488-PP_0606; -. DR DNASU; 1044422; -. DR GeneID; 83677937; -. DR KEGG; ppu:PP_0606; -. DR PATRIC; fig|160488.4.peg.646; -. DR eggNOG; COG0761; Bacteria. DR HOGENOM; CLU_027486_1_1_6; -. DR OrthoDB; 9804068at2; -. DR PhylomeDB; Q88Q89; -. DR BioCyc; PPUT160488:G1G01-663-MONOMER; -. DR UniPathway; UPA00056; UER00097. DR UniPathway; UPA00059; UER00105. DR Proteomes; UP000000556; 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-enyl 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 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; Iron; Iron-sulfur; Isoprene biosynthesis; Metal-binding; KW Oxidoreductase; Reference proteome. FT CHAIN 1..315 FT /note="4-hydroxy-3-methylbut-2-enyl diphosphate reductase" FT /id="PRO_0000128858" FT ACT_SITE 126 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 12 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|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:0000255|HAMAP-Rule:MF_00191" FT BINDING 41 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 41 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000255|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:0000255|HAMAP-Rule:MF_00191" FT BINDING 74 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 74 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 96 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|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:0000255|HAMAP-Rule:MF_00191" FT BINDING 124 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 124 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 168 FT /ligand="(2E)-4-hydroxy-3-methylbut-2-enyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128753" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 198 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 226 FT /ligand="(2E)-4-hydroxy-3-methylbut-2-enyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128753" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 226 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 226 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 227 FT /ligand="(2E)-4-hydroxy-3-methylbut-2-enyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128753" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 227 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 227 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 228 FT /ligand="(2E)-4-hydroxy-3-methylbut-2-enyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128753" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 228 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 228 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 270 FT /ligand="(2E)-4-hydroxy-3-methylbut-2-enyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128753" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 270 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 270 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" SQ SEQUENCE 315 AA; 34543 MW; 383B9398D327001C CRC64; MQIKLANPRG FCAGVDRAIE IVNRALEVFG PPIYVRHEVV HNKFVVEDLR NRGAIFVEEL DQVPDDVIVI FSAHGVSQAV RQEAAGRGLK VFDATCPLVT KVHIEVAKYS RDGRECILIG HEGHPEVEGT MGQYDASNGG AIYLVEDEED VANLQVRDPD HLAFVTQTTL SMDDTSRVID ALRARFPNIG GPRKDDICYA TQNRQDAVKQ LAGESDVVLV VGSPNSSNSN RLRELAERMG TPAYLIDGAE DLQRGWFDQA ARIGITAGAS APEVLVRGVI EQLKAWGATG AEELDGREEN ITFSMPKELR VRSLI //