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 07-JAN-2015, entry version 66. DE RecName: Full=4-hydroxy-3-methylbut-2-enyl diphosphate reductase {ECO:0000255|HAMAP-Rule:MF_00191}; DE EC=1.17.1.2 {ECO:0000255|HAMAP-Rule:MF_00191}; GN Name=ispH {ECO:0000255|HAMAP-Rule:MF_00191}; GN OrderedLocusNames=Mpe_A2693; OS Methylibium petroleiphilum (strain PM1). OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Methylibium. OX NCBI_TaxID=420662; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=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: Converts 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate CC into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate CC (DMAPP). {ECO:0000255|HAMAP-Rule:MF_00191}. CC -!- CATALYTIC ACTIVITY: Isopentenyl diphosphate + NAD(P)(+) + H(2)O = CC (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H. CC {ECO:0000255|HAMAP-Rule:MF_00191}. CC -!- CATALYTIC ACTIVITY: Dimethylallyl diphosphate + NAD(P)(+) + H(2)O CC = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H. CC {ECO:0000255|HAMAP-Rule:MF_00191}. CC -!- COFACTOR: CC Name=[3Fe-4S] cluster; Xref=ChEBI:CHEBI:21137; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00191}; CC Note=Binds 1 [3Fe-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- CC Rule:MF_00191}. CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate CC biosynthesis via DXP pathway; isopentenyl diphosphate from 1- CC deoxy-D-xylulose 5-phosphate: step 6/6. {ECO:0000255|HAMAP- CC 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; YP_001021882.1; NC_008825.1. DR STRING; 420662.Mpe_A2693; -. DR EnsemblBacteria; ABM95647; ABM95647; Mpe_A2693. DR GeneID; 4783595; -. DR KEGG; mpt:Mpe_A2693; -. DR eggNOG; COG0761; -. DR HOGENOM; HOG000220192; -. DR KO; K03527; -. DR OMA; IIGPRKD; -. DR OrthoDB; EOG6HF624; -. DR BioCyc; MPET420662:GHBE-2726-MONOMER; -. DR UniPathway; UPA00056; UER00097. DR UniPathway; UPA00059; UER00105. DR Proteomes; UP000000366; Chromosome. DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP. DR GO; GO:0051745; F:4-hydroxy-3-methylbut-2-en-1-yl diphosphate reductase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0050992; P:dimethylallyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-HAMAP. DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00191; IspH; 1. DR InterPro; IPR003451; LytB/IspH. DR Pfam; PF02401; LYTB; 1. DR TIGRFAMs; TIGR00216; ispH_lytB; 1. PE 3: Inferred from homology; KW 3Fe-4S; Complete proteome; Iron; Iron-sulfur; Isoprene biosynthesis; KW Metal-binding; NADP; Oxidoreductase; Reference proteome. FT CHAIN 1 329 4-hydroxy-3-methylbut-2-enyl diphosphate FT reductase. FT /FTId=PRO_1000098957. FT REGION 237 239 Substrate binding. {ECO:0000255|HAMAP- FT Rule:MF_00191}. FT METAL 27 27 Iron-sulfur (3Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00191}. FT METAL 111 111 Iron-sulfur (3Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00191}. FT METAL 209 209 Iron-sulfur (3Fe-4S). {ECO:0000255|HAMAP- FT Rule:MF_00191}. FT BINDING 56 56 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00191}. FT BINDING 89 89 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00191}. FT BINDING 139 139 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00191}. FT BINDING 179 179 Substrate. {ECO:0000255|HAMAP- FT Rule:MF_00191}. FT BINDING 281 281 Substrate. {ECO:0000255|HAMAP- FT 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 //