ID A0A1I5KDG4_9RHOB Unreviewed; 316 AA. AC A0A1I5KDG4; DT 22-NOV-2017, integrated into UniProtKB/TrEMBL. DT 22-NOV-2017, sequence version 1. DT 13-FEB-2019, entry version 7. DE RecName: Full=4-hydroxy-3-methylbut-2-enyl diphosphate reductase {ECO:0000256|HAMAP-Rule:MF_00191, ECO:0000256|SAAS:SAAS01001099}; DE Short=HMBPP reductase {ECO:0000256|HAMAP-Rule:MF_00191}; DE EC=1.17.7.4 {ECO:0000256|HAMAP-Rule:MF_00191, ECO:0000256|SAAS:SAAS01001099}; 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 Rhodobacteraceae; 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)- CC butenyl 4-diphosphate (HMBPP) into a mixture of isopentenyl CC diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Acts in CC the terminal step of the DOXP/MEP pathway for isoprenoid precursor CC biosynthesis. {ECO:0000256|HAMAP-Rule:MF_00191, CC ECO:0000256|SAAS:SAAS01001098}. CC -!- CATALYTIC ACTIVITY: CC Reaction=H2O + isopentenyl diphosphate + 2 oxidized [2Fe-2S]- CC [ferredoxin] = (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 CC H(+) + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:24488, CC Rhea:RHEA-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 ECO:0000256|SAAS:SAAS01125179}; CC -!- CATALYTIC ACTIVITY: CC Reaction=dimethylallyl diphosphate + H2O + 2 oxidized [2Fe-2S]- CC [ferredoxin] = (2E)-4-hydroxy-3-methylbut-2-enyl diphosphate + 2 CC H(+) + 2 reduced [2Fe-2S]-[ferredoxin]; Xref=Rhea:RHEA:24825, CC Rhea:RHEA-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 ECO:0000256|SAAS:SAAS01125177}; 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- CC Rule:MF_00191, ECO:0000256|SAAS:SAAS01001092}. 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:0000256|HAMAP- CC Rule:MF_00191, ECO:0000256|SAAS:SAAS01001076}. CC -!- SIMILARITY: Belongs to the IspH family. {ECO:0000256|HAMAP- CC Rule:MF_00191, ECO:0000256|SAAS:SAAS01001094}. 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 BioCyc; GCF_900115595:BM162_RS00185-MONOMER; -. 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|HAMAP-Rule:MF_00191, KW ECO:0000256|SAAS:SAAS01001097}; KW Complete proteome {ECO:0000313|Proteomes:UP000199356}; KW Iron {ECO:0000256|HAMAP-Rule:MF_00191, ECO:0000256|SAAS:SAAS00772206}; KW Iron-sulfur {ECO:0000256|HAMAP-Rule:MF_00191, KW ECO:0000256|SAAS:SAAS00772258}; KW Isoprene biosynthesis {ECO:0000256|HAMAP-Rule:MF_00191, KW ECO:0000256|SAAS:SAAS01001084}; KW Metal-binding {ECO:0000256|HAMAP-Rule:MF_00191, KW ECO:0000256|SAAS:SAAS00772260}; KW Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_00191, KW ECO:0000256|SAAS:SAAS01001093}; KW Reference proteome {ECO:0000313|Proteomes:UP000199356}. FT REGION 228 230 Substrate binding. {ECO:0000256|HAMAP- FT Rule:MF_00191}. FT ACT_SITE 131 131 Proton donor. {ECO:0000256|HAMAP-Rule: FT MF_00191}. FT METAL 17 17 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP- FT Rule:MF_00191}. FT METAL 101 101 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP- FT Rule:MF_00191}. FT METAL 200 200 Iron-sulfur (4Fe-4S). {ECO:0000256|HAMAP- FT Rule:MF_00191}. FT BINDING 46 46 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00191}. FT BINDING 79 79 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00191}. FT BINDING 129 129 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00191}. FT BINDING 170 170 Substrate. {ECO:0000256|HAMAP-Rule: FT MF_00191}. FT BINDING 273 273 Substrate. {ECO:0000256|HAMAP-Rule: FT 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 //