ID A0A1I5KDG4_9RHOB Unreviewed; 316 AA. AC A0A1I5KDG4; DT 22-NOV-2017, integrated into UniProtKB/TrEMBL. DT 22-NOV-2017, sequence version 1. DT 03-AUG-2022, entry version 15. 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=ispH {ECO:0000256|HAMAP-Rule:MF_00191}; GN ORFNames=SAMN04488047_10137 {ECO:0000313|EMBL:SFO83028.1}; OS Tranquillimonas alkanivorans. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales; OC Roseobacteraceae; Tranquillimonas. OX NCBI_TaxID=441119 {ECO:0000313|EMBL:SFO83028.1, ECO:0000313|Proteomes:UP000199356}; RN [1] {ECO:0000313|EMBL:SFO83028.1, ECO:0000313|Proteomes:UP000199356} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=DSM 19547 {ECO:0000313|EMBL:SFO83028.1, RC ECO:0000313|Proteomes:UP000199356}; RA de Groot N.N.; RL Submitted (OCT-2016) 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:0000256|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:0000256|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: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; FOXA01000001; SFO83028.1; -; Genomic_DNA. DR STRING; 441119.SAMN04488047_10137; -. DR EnsemblBacteria; SFO83028; SFO83028; SAMN04488047_10137. DR UniPathway; UPA00056; UER00097. DR UniPathway; UPA00059; UER00105. DR Proteomes; UP000199356; Unassembled WGS sequence. 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 {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:UP000199356}. FT REGION 228..230 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT ACT_SITE 131 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 17 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 46 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 79 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 101 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 129 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 170 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 200 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 273 FT /ligand="substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" SQ SEQUENCE 316 AA; 34137 MW; D4C06A17C9EA8339 CRC64; MTKPPLTLYL AAPRGFCAGV DRAIKIVEMA LEKWGAPVYV RHEIVHNRYV VDGLREKGAV FVEELDECPD DRPVIFSAHG VPKAVPAEAA KREMVYVDAT CPLVSKVHIE AERHHENGLQ MIMIGHAGHP ETVGTMGQLP AGEVLLVETD EDVAGLDVRD PDKLAFITQT TLSVDDTAGI VAALQARFPN IVGPHKEDIC YATTNRQAAV KAMAPHADAM LVIGAPNSSN SKRLVEVGRG AGCGYAQLVQ RADDIDWRAL EGIGSIGITA GASAPEVLVN EVLDAFRDRF DVTVEQVETA QENVEFKVPR VLRVPA //