ID ISPH_METPP Reviewed; 329 AA. AC A2SJA8; DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot. DT 06-MAR-2007, sequence version 1. DT 02-DEC-2020, entry version 92. 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=Mpe_A2693; OS Methylibium petroleiphilum (strain ATCC BAA-1232 / LMG 22953 / PM1). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; Methylibium. OX NCBI_TaxID=420662; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC BAA-1232 / LMG 22953 / PM1; RX PubMed=17158667; DOI=10.1128/jb.01259-06; RA Kane S.R., Chakicherla A.Y., Chain P.S.G., Schmidt R., Shin M.W., RA Legler T.C., Scow K.M., Larimer F.W., Lucas S.M., Richardson P.M., RA Hristova K.R.; RT "Whole-genome analysis of the methyl tert-butyl ether-degrading beta- RT proteobacterium Methylibium petroleiphilum PM1."; RL J. Bacteriol. 189:1931-1945(2007). 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; CP000555; ABM95647.1; -; Genomic_DNA. DR RefSeq; WP_011830277.1; NC_008825.1. DR SMR; A2SJA8; -. DR STRING; 420662.Mpe_A2693; -. DR PRIDE; A2SJA8; -. DR EnsemblBacteria; ABM95647; ABM95647; Mpe_A2693. DR KEGG; mpt:Mpe_A2693; -. DR eggNOG; COG0761; Bacteria. DR HOGENOM; CLU_027486_1_0_4; -. DR OMA; HNKYVVD; -. DR OrthoDB; 1311145at2; -. DR BioCyc; MPET420662:G1G81-2741-MONOMER; -. DR UniPathway; UPA00056; UER00097. DR UniPathway; UPA00059; UER00105. DR Proteomes; UP000000366; 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; Reference proteome. FT CHAIN 1..329 FT /note="4-hydroxy-3-methylbut-2-enyl diphosphate reductase" FT /id="PRO_1000098957" FT REGION 237..239 FT /note="Substrate binding" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT ACT_SITE 141 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT METAL 27 FT /note="Iron-sulfur (4Fe-4S)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT METAL 111 FT /note="Iron-sulfur (4Fe-4S)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT METAL 209 FT /note="Iron-sulfur (4Fe-4S)" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 56 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 89 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 139 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 179 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 281 FT /note="Substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" SQ SEQUENCE 329 AA; 35761 MW; 7E32240F0B957138 CRC64; MTMDTSPSHD AERGVTDVLL AEPRGFCAGV DRAIEIVERA IRKFGAPIYV RHEIVHNTFV VNDLKAKGAI FIEDLADVPP GATLVFSAHG VSRAVRDEAE ARGFSVYDAT CPLVTKVHVE VAKLHKEGYE FIMIGHKGHP EVEGTMGQLS EGIYLVEDVD DVAQLRVTRP DRLAVVTQTT LSTDDAAEIL AAVKRRFPQV REPKQQDICY ATQNRQDAVK VLAPQVDVVV VVGSPTSSNS NRLRELAERL GTPAYMVDSA SDLRPEWFEG SARVGLTAGA SAPELLVREV IERLRALGAV SVRKMAGVEE TVRFPLPLGL GDKSMEGVA //