ID ISPH_CHLPM Reviewed; 313 AA. AC A4SGC0; DT 20-MAY-2008, integrated into UniProtKB/Swiss-Prot. DT 15-MAY-2007, sequence version 1. DT 02-SEP-2026, entry version 99. 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=Cvib_1518; OS Chlorobium phaeovibrioides (strain DSM 265 / 1930) (Prosthecochloris OS vibrioformis (strain DSM 265)). OC Bacteria; Pseudomonadati; Chlorobiota; Chlorobiia; Chlorobiales; OC Chlorobiaceae; Chlorobium/Pelodictyon group; Chlorobium. OX NCBI_TaxID=290318; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 265 / 1930; RG US DOE Joint Genome Institute; RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., RA Glavina del Rio T., Hammon N., Israni S., Pitluck S., Schmutz J., RA Larimer F., Land M., Hauser L., Mikhailova N., Li T., Overmann J., RA Schuster S.C., Bryant D.A., Richardson P.; RT "Complete sequence of Prosthecochloris vibrioformis DSM 265."; RL Submitted (MAR-2007) 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=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; CP000607; ABP37529.1; -; Genomic_DNA. DR AlphaFoldDB; A4SGC0; -. DR SMR; A4SGC0; -. DR STRING; 290318.Cvib_1518; -. DR KEGG; pvi:Cvib_1518; -. DR eggNOG; COG0761; Bacteria. DR HOGENOM; CLU_027486_0_1_10; -. DR OrthoDB; 9777362at2; -. DR UniPathway; UPA00056; UER00097. DR UniPathway; UPA00059; UER00105. 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; NF002187; PRK01045.1-1; 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. FT CHAIN 1..313 FT /note="4-hydroxy-3-methylbut-2-enyl diphosphate reductase" FT /id="PRO_1000077523" FT ACT_SITE 127 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 13 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 75 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 75 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 75 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 97 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 125 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 125 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 125 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 218 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 246 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 246 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 246 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 247 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 247 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 247 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 248 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 248 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 248 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 295 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 295 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 295 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" SQ SEQUENCE 313 AA; 34900 MW; D3FF21F0B929B880 CRC64; MKVNLDRNSS GFCFGVQSTI NVAEEKLRKE KGLYSLGDVV HNEVEVKRLE ALGLITIDTP AFNELKNAPV LIRAHGEPPS TYETANRNNL TLTDTTCPVV AKLQRTASQL NELGYQIIIY GKHLHPEVIG INGHCQNRAL IIKHADLSDP EETLPIDLSK KTALISQTTM DVSGFYELKK NLEKLFSKGG RETGPWAEVK SIGEAEPMPE FIFKDTICRQ ISNRNQKLQD FSRANERIIF VAGKKSSNGQ VLYAICKEAN PESHFIEDVE ELQSEWFTTT QGKTVESIGV CGATSTPMWL LEKVANHIEA HYA //