ID N6UI18_9HYPH Unreviewed; 341 AA. AC N6UI18; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 29-SEP-2021, entry version 43. 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 ECO:0000313|EMBL:ENN92074.1}; GN ORFNames=BBbe_03790 {ECO:0000313|EMBL:ENN92074.1}; OS Bartonella bovis 91-4. OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales; OC Bartonellaceae; Bartonella. OX NCBI_TaxID=1094491 {ECO:0000313|EMBL:ENN92074.1, ECO:0000313|Proteomes:UP000014038}; RN [1] {ECO:0000313|EMBL:ENN92074.1, ECO:0000313|Proteomes:UP000014038} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=91-4 {ECO:0000313|EMBL:ENN92074.1, RC ECO:0000313|Proteomes:UP000014038}; RX PubMed=23555299; DOI=10.1371/journal.pgen.1003393; RA Guy L., Nystedt B., Toft C., Zaremba-Niedzwiedzka K., Berglund E.C., RA Granberg F., Naslund K., Eriksson A.S., Andersson S.G.; RT "A gene transfer agent and a dynamic repertoire of secretion systems hold RT the keys to the explosive radiation of the emerging pathogen Bartonella."; RL PLoS Genet. 9:E1003393-E1003393(2013). 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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:ENN92074.1}. 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; AGWA01000006; ENN92074.1; -; Genomic_DNA. DR RefSeq; WP_010700941.1; NZ_CM001844.1. DR STRING; 1094491.BBbe_03790; -. DR EnsemblBacteria; ENN92074; ENN92074; BBbe_03790. DR PATRIC; fig|1094491.5.peg.415; -. DR eggNOG; COG0761; Bacteria. DR HOGENOM; CLU_027486_1_0_5; -. DR OrthoDB; 1311145at2; -. DR UniPathway; UPA00056; UER00097. DR UniPathway; UPA00059; UER00105. DR Proteomes; UP000014038; 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 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}. FT REGION 232..234 FT /note="Substrate binding" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT ACT_SITE 135 FT /note="Proton donor" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT METAL 18 FT /note="Iron-sulfur (4Fe-4S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT METAL 105 FT /note="Iron-sulfur (4Fe-4S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT METAL 204 FT /note="Iron-sulfur (4Fe-4S)" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 47 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 83 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 133 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 174 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" FT BINDING 277 FT /note="Substrate" FT /evidence="ECO:0000256|HAMAP-Rule:MF_00191" SQ SEQUENCE 341 AA; 37787 MW; 8E1350C224E2A53E CRC64; MCLLPPLTMR LCSPRGFCAG VDRAIQIVVL ALKKYGTPVY VRHEIVHNRY VVEGLQQRGA IFIEELNEIP EEHRGQPVVF SAHGVPKSVP EEAHHYNLFY IDATCPLVSK VHKQAIRHQR HGRHVILIGH SGHPEVIGTM GQLEKGAVTL IETVEDAWRY KPENPKKLGF VTQTTLSVEN TAEILDVLQK RFPALETPAA ESICYATTNR QEAVKAAALG SDLFLIVGAP NSSNSRRLVE VAERFGAQRS ILVQCADEID FDNLGVLSVV SLSAGASAPE IIVDEIIAAF HKRYDVKIEL AETVLETETF LVNRGLRDVV LTPQDMAFVN GYAKDTNKRK L //