ID ISPH_SYNY3 Reviewed; 379 AA. AC Q55643; Q55066; DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2000, sequence version 2. DT 27-MAR-2024, entry version 137. 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}; Synonyms=lytB; GN OrderedLocusNames=slr0348; OS Synechocystis sp. (strain PCC 6803 / Kazusa). OC Bacteria; Cyanobacteriota; Cyanophyceae; Synechococcales; Merismopediaceae; OC Synechocystis. OX NCBI_TaxID=1111708; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX PubMed=9305771; DOI=10.1016/s0378-1119(97)00165-0; RA Cassier-Chauvat C., Poncelet M., Chauvat F.; RT "Three insertion sequences from the cyanobacterium Synechocystis PCC6803 RT support the occurrence of horizontal DNA transfer among bacteria."; RL Gene 195:257-266(1997). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 27184 / PCC 6803 / N-1; RX PubMed=8590279; DOI=10.1093/dnares/2.4.153; RA Kaneko T., Tanaka A., Sato S., Kotani H., Sazuka T., Miyajima N., RA Sugiura M., Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. I. Sequence features in the 1 Mb region RT from map positions 64% to 92% of the genome."; RL DNA Res. 2:153-166(1995). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=PCC 6803 / Kazusa; RX PubMed=8905231; DOI=10.1093/dnares/3.3.109; RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y., RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T., RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S., RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.; RT "Sequence analysis of the genome of the unicellular cyanobacterium RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire RT genome and assignment of potential protein-coding regions."; RL DNA Res. 3:109-136(1996). RN [4] RP PATHWAY. RX PubMed=11004185; DOI=10.1128/jb.182.20.5841-5848.2000; RA Cunningham F.X. Jr., Lafond T.P., Gantt E.; RT "Evidence of a role for LytB in the nonmevalonate pathway of isoprenoid RT biosynthesis."; RL J. Bacteriol. 182:5841-5848(2000). 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 ECO:0000269|PubMed:11004185}. 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 ECO:0000269|PubMed:11004185}. CC -!- SIMILARITY: Belongs to the IspH family. {ECO:0000255|HAMAP- CC Rule:MF_00191}. CC -!- SEQUENCE CAUTION: CC Sequence=BAA10159.1; Type=Erroneous initiation; Evidence={ECO:0000305}; 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; U38915; AAB72119.1; -; Genomic_DNA. DR EMBL; BA000022; BAA10159.1; ALT_INIT; Genomic_DNA. DR PIR; S76307; S76307. DR AlphaFoldDB; Q55643; -. DR SMR; Q55643; -. DR IntAct; Q55643; 4. DR STRING; 1148.gene:10499652; -. DR PaxDb; 1148-1001532; -. DR EnsemblBacteria; BAA10159; BAA10159; BAA10159. DR KEGG; syn:slr0348; -. DR eggNOG; COG0761; Bacteria. DR InParanoid; Q55643; -. DR PhylomeDB; Q55643; -. DR UniPathway; UPA00056; UER00097. DR UniPathway; UPA00059; UER00105. DR Proteomes; UP000001425; 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 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 PANTHER; PTHR31619; 4-HYDROXY-3-METHYLBUT-2-ENYL DIPHOSPHATE REDUCTASE, CHLOROPLASTIC; 1. DR PANTHER; PTHR31619:SF5; 4-HYDROXY-3-METHYLBUT-2-ENYL DIPHOSPHATE REDUCTASE, CHLOROPLASTIC; 1. DR Pfam; PF02401; LYTB; 1. PE 3: Inferred from homology; KW 4Fe-4S; Iron; Iron-sulfur; Isoprene biosynthesis; Metal-binding; KW Oxidoreductase; Reference proteome. FT CHAIN 1..379 FT /note="4-hydroxy-3-methylbut-2-enyl diphosphate reductase" FT /id="PRO_0000128880" FT ACT_SITE 160 FT /note="Proton donor" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 39 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 69 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 130 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 158 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 223 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 261 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 290..292 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" FT BINDING 352 FT /ligand="substrate" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191" SQ SEQUENCE 379 AA; 42415 MW; 4CD0167AF5D4957E CRC64; MGVMNTEYQS HLIQEIRQNN YRLERGDVTI LLAEAFGFCW GVERAVAMAY ETRQHFPGDR LWITNEIIHN PSVNQRLREM EVNFIDVVNG EKDFSGVAKG DVVILPAFGA SVEEMQLLND RECTIVDTTC PWVSKVWNSV EKHKKKEHTS IIHGKYNHEE TIATSSFAGT YLIVLNMAEA QKVCDYILHG GDRQEFLDYF ANAHSAGFDP DQDLVRLGVA NQTTMLKSET EMIGKLFEKT LLQKYGPIEL NNHFMSFNTI CDATQERQDA MFDLVEEDLS LMVVIGGFNS SNTTHLQEIA VEHGIPSVHI DSGDRIGPGN RVEHKPLGKD LEVLEPWLPA GKITVGVTSG ASTPDKVVEE VMKKILAIKE AQPVLEIAG //