ISPH_FRATT
ID ISPH_FRATT Reviewed; 318 AA.
AC Q5NGK4;
DT 19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
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=FTT_0833;
OS Francisella tularensis subsp. tularensis (strain SCHU S4 / Schu 4).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Thiotrichales;
OC Francisellaceae; Francisella.
OX NCBI_TaxID=177416;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SCHU S4 / Schu 4;
RX PubMed=15640799; DOI=10.1038/ng1499;
RA Larsson P., Oyston P.C.F., Chain P., Chu M.C., Duffield M., Fuxelius H.-H.,
RA Garcia E., Haelltorp G., Johansson D., Isherwood K.E., Karp P.D.,
RA Larsson E., Liu Y., Michell S., Prior J., Prior R., Malfatti S.,
RA Sjoestedt A., Svensson K., Thompson N., Vergez L., Wagg J.K., Wren B.W.,
RA Lindler L.E., Andersson S.G.E., Forsman M., Titball R.W.;
RT "The complete genome sequence of Francisella tularensis, the causative
RT agent of tularemia.";
RL Nat. Genet. 37:153-159(2005).
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}.
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; AJ749949; CAG45466.1; -; Genomic_DNA.
DR RefSeq; WP_003020788.1; NZ_CP010290.1.
DR RefSeq; YP_169838.1; NC_006570.2.
DR AlphaFoldDB; Q5NGK4; -.
DR SMR; Q5NGK4; -.
DR STRING; 177416.FTT_0833; -.
DR DNASU; 3190808; -.
DR EnsemblBacteria; CAG45466; CAG45466; FTT_0833.
DR KEGG; ftu:FTT_0833; -.
DR eggNOG; COG0761; Bacteria.
DR OMA; HNKYVVD; -.
DR UniPathway; UPA00056; UER00097.
DR UniPathway; UPA00059; UER00105.
DR Proteomes; UP000001174; 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..318
FT /note="4-hydroxy-3-methylbut-2-enyl diphosphate reductase"
FT /id="PRO_0000128818"
FT ACT_SITE 126
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 41
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT BINDING 74
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT BINDING 96
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT BINDING 124
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT BINDING 167
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT BINDING 197
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT BINDING 225..227
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
FT BINDING 269
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00191"
SQ SEQUENCE 318 AA; 35152 MW; 0ECD0079A2D4BC3C CRC64;
MKILLANPRG FCAGVSRAVE TVEKVLEVEK SPVYVRHEVV HNKVVVDSLK KKGVVFVKEV
DEVPDDAVCI FSAHGVSLKV EEAAAKKNLV LYDATCPLVT KVHRGVRLAS NNDAECILIG
HKGHPEVQGT MGQYRSKKGA IYLIESEEDL NKLTIKDPDN LYYATQTTLS VDETQGIIQA
LKDKYPNIKG PKKEDICYAT QNRQTAIKAM LKHIDVLVVV GSQNSSNSNR LKELATLEGI
DAYLVDNPKD VDKLWFDNKK VCGVSAGASA PEYLVQQIIS QISKVCSTEV EEFEGIKEEV
YFPLPRLLKQ KIGTGKVE
