ISPH_NITSB
ID ISPH_NITSB Reviewed; 275 AA.
AC A6Q2R7;
DT 15-JAN-2008, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 81.
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}; OrderedLocusNames=NIS_0662;
OS Nitratiruptor sp. (strain SB155-2).
OC Bacteria; Proteobacteria; Epsilonproteobacteria; Nautiliales;
OC Nitratiruptoraceae; Nitratiruptor; unclassified Nitratiruptor.
OX NCBI_TaxID=387092;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SB155-2;
RX PubMed=17615243; DOI=10.1073/pnas.0700687104;
RA Nakagawa S., Takaki Y., Shimamura S., Reysenbach A.-L., Takai K.,
RA Horikoshi K.;
RT "Deep-sea vent epsilon-proteobacterial genomes provide insights into
RT emergence of pathogens.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12146-12150(2007).
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 -!- 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 -!- SIMILARITY: Belongs to the IspH family. {ECO:0000255|HAMAP-
CC Rule:MF_00191}.
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DR EMBL; AP009178; BAF69776.1; -; Genomic_DNA.
DR RefSeq; WP_012082039.1; NC_009662.1.
DR AlphaFoldDB; A6Q2R7; -.
DR SMR; A6Q2R7; -.
DR STRING; 387092.NIS_0662; -.
DR EnsemblBacteria; BAF69776; BAF69776; NIS_0662.
DR KEGG; nis:NIS_0662; -.
DR eggNOG; COG0761; Bacteria.
DR HOGENOM; CLU_027486_0_1_7; -.
DR OMA; HNKYVVD; -.
DR OrthoDB; 1235756at2; -.
DR UniPathway; UPA00056; UER00097.
DR UniPathway; UPA00059; UER00105.
DR Proteomes; UP000001118; 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; Iron; Iron-sulfur; Isoprene biosynthesis; Metal-binding;
KW Oxidoreductase; Reference proteome.
FT CHAIN 1..275
FT /note="4-hydroxy-3-methylbut-2-enyl diphosphate reductase"
FT /id="PRO_1000021143"
FT ACT_SITE 122
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT BINDING 12
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT BINDING 36
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT BINDING 70
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT BINDING 92
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT BINDING 120
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT BINDING 157
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT BINDING 185
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT BINDING 213..215
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT BINDING 257
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
SQ SEQUENCE 275 AA; 31284 MW; CBBB85B50377F3CC CRC64;
MEIRLAKSYG FCFGVKRAIK IAEESPNSVT FGPLIHNKNE IDRLKEKYNV ELVEEIDEIQ
ENSRVVIRTH GIPKEKLALL KEKNVEVIDA TCPFVTKPQE IVSKMSEEGY SIVIFGDINH
PEIKGVMSYA TDPIVVLSVE ELEGKPLKEK VATVAQTTRK FEEYQKIVNY LMEHKKEVRV
FNTICNATFE NQDAARELSR EADIMIIIGG KNSSNTKQLF KICKENCPDS YLVENAKELE
KEWFEGKKVC GITAGASTPN WIIEEVIENI KKIQV
