ID A5U856_MYCTA Unreviewed; 329 AA. AC A5U856; DT 10-JUL-2007, integrated into UniProtKB/TrEMBL. DT 10-JUL-2007, sequence version 1. DT 02-SEP-2026, entry version 112. 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=lytB1 {ECO:0000313|EMBL:ABQ75206.1}; GN Synonyms=ispH {ECO:0000256|HAMAP-Rule:MF_00191}; GN OrderedLocusNames=MRA_3422 {ECO:0000313|EMBL:ABQ75206.1}; OS Mycobacterium tuberculosis (strain ATCC 25177 / H37Ra). OC Bacteria; Bacillati; Actinomycetota; Actinomycetes; Mycobacteriales; OC Mycobacteriaceae; Mycobacterium; Mycobacterium tuberculosis complex. OX NCBI_TaxID=419947 {ECO:0000313|EMBL:ABQ75206.1, ECO:0000313|Proteomes:UP000001988}; RN [1] {ECO:0000313|EMBL:ABQ75206.1, ECO:0000313|Proteomes:UP000001988} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 25177 / H37Ra {ECO:0000313|Proteomes:UP000001988}; RX PubMed=18584054; DOI=10.1371/journal.pone.0002375; RA Zheng H., Lu L., Wang B., Pu S., Zhang X., Zhu G., Shi W., Zhang L., RA Wang H., Wang S., Zhao G., Zhang Y.; RT "Genetic basis of virulence attenuation revealed by comparative genomic RT analysis of Mycobacterium tuberculosis strain H37Ra versus H37Rv."; RL PLoS ONE 3:E2375-E2375(2008). 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; CP000611; ABQ75206.1; -; Genomic_DNA. DR RefSeq; WP_003417912.1; NC_009525.1. DR AlphaFoldDB; A5U856; -. DR SMR; A5U856; -. DR KEGG; mra:MRA_3422; -. DR eggNOG; COG0761; Bacteria. DR HOGENOM; CLU_027486_1_1_11; -. DR UniPathway; UPA00056; UER00097. DR UniPathway; UPA00059; UER00105. DR Proteomes; UP000001988; 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: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; 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}; Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00191}; KW Reference proteome {ECO:0000313|Proteomes:UP000001988}. FT ACT_SITE 147 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 29 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 58 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 58 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 58 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 95 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 95 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 95 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 117 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 145 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 145 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 145 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 185 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 215 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 243 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 243 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 243 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 244 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 244 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 244 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 245 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 245 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 245 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 287 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 287 FT /ligand="dimethylallyl diphosphate" FT /ligand_id="ChEBI:CHEBI:57623" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 287 FT /ligand="isopentenyl diphosphate" FT /ligand_id="ChEBI:CHEBI:128769" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" SQ SEQUENCE 329 AA; 34666 MW; 00540C5C87B2AB6B CRC64; MAEVFVGPVA QGYASGEVTV LLASPRSFCA GVERAIETVK RVLDVAEGPV YVRKQIVHNT VVVAELRDRG AVFVEDLDEI PDPPPPGAVV VFSAHGVSPA VRAGADERGL QVVDATCPLV AKVHAEAARF AARGDTVVFI GHAGHEETEG TLGVAPRSTL LVQTPADVAA LNLPEGTQLS YLTQTTLALD ETADVIDALR ARFPTLGQPP SEDICYATTN RQRALQSMVG ECDVVLVIGS CNSSNSRRLV ELAQRSGTPA YLIDGPDDIE PEWLSSVSTI GVTAGASAPP RLVGQVIDAL RGYASITVVE RSIATETVRF GLPKQVRAQ //