ID N6UI18_9RHIZ Unreviewed; 341 AA. AC N6UI18; DT 26-JUN-2013, integrated into UniProtKB/TrEMBL. DT 26-JUN-2013, sequence version 1. DT 13-NOV-2013, entry version 4. DE RecName: Full=4-hydroxy-3-methylbut-2-enyl diphosphate reductase; DE EC=1.17.1.2; GN Name=ispH; ORFNames=BBbe_03790; OS Bartonella bovis 91-4. OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhizobiales; OC Bartonellaceae; Bartonella. OX NCBI_TaxID=1094491; RN [1] RP NUCLEOTIDE SEQUENCE. RC STRAIN=91-4; RX PubMed=23555299; 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 RT hold the keys to the explosive radiation of the emerging pathogen RT bartonella."; RL PLoS Genet. 9:E1003393-E1003393(2013). CC -!- FUNCTION: Converts 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate CC into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate CC (DMAPP) (By similarity). CC -!- CATALYTIC ACTIVITY: Dimethylallyl diphosphate + NAD(P)(+) + H(2)O CC = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H. CC -!- CATALYTIC ACTIVITY: Isopentenyl diphosphate + NAD(P)(+) + H(2)O = CC (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H. CC -!- COFACTOR: Binds 1 3Fe-4S cluster per subunit (By similarity). CC -!- PATHWAY: Isoprenoid biosynthesis; dimethylallyl diphosphate CC biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3- CC methylbutenyl diphosphate: step 1/1. CC -!- PATHWAY: Isoprenoid biosynthesis; isopentenyl diphosphate CC biosynthesis via DXP pathway; isopentenyl diphosphate from 1- CC deoxy-D-xylulose 5-phosphate: step 6/6. CC -!- SIMILARITY: Belongs to the IspH family. CC -!- CAUTION: The sequence shown here is derived from an CC EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is CC preliminary data. 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 EnsemblBacteria; ENN92074; ENN92074; BBbe_03790. DR UniPathway; UPA00056; UER00097. DR UniPathway; UPA00059; UER00105. DR GO; GO:0051538; F:3 iron, 4 sulfur cluster binding; IEA:UniProtKB-HAMAP. DR GO; GO:0051745; F:4-hydroxy-3-methylbut-2-en-1-yl diphosphate reductase activity; IEA:UniProtKB-HAMAP. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0050992; P:dimethylallyl diphosphate biosynthetic process; IEA:UniProtKB-UniPathway. DR GO; GO:0019288; P:isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway; IEA:UniProtKB-HAMAP. DR GO; GO:0016114; P:terpenoid biosynthetic process; IEA:UniProtKB-HAMAP. DR HAMAP; MF_00191; IspH; 1; -. DR InterPro; IPR003451; LytB. DR Pfam; PF02401; LYTB; 1. DR TIGRFAMs; TIGR00216; ispH_lytB; 1. PE 3: Inferred from homology; KW 3Fe-4S; Iron; Iron-sulfur; Isoprene biosynthesis; Metal-binding; NADP; KW Oxidoreductase. FT REGION 232 234 Substrate binding (By similarity). FT METAL 18 18 Iron-sulfur (3Fe-4S) (By similarity). FT METAL 105 105 Iron-sulfur (3Fe-4S) (By similarity). FT METAL 204 204 Iron-sulfur (3Fe-4S) (By similarity). FT BINDING 47 47 Substrate (By similarity). FT BINDING 83 83 Substrate (By similarity). FT BINDING 133 133 Substrate (By similarity). FT BINDING 174 174 Substrate (By similarity). FT BINDING 277 277 Substrate (By similarity). 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 //