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Protein

4-hydroxy-3-methylbut-2-enyl diphosphate reductase

Gene

ispH

Organism
Aquifex aeolicus (strain VF5)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Converts 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP).

Catalytic activityi

Isopentenyl diphosphate + NAD(P)+ + H2O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H.1 Publication
Dimethylallyl diphosphate + NAD(P)+ + H2O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H.1 Publication

Cofactori

[3Fe-4S] cluster1 PublicationNote: Binds 1 [3Fe-4S] cluster per subunit.1 Publication

Enzyme regulationi

Highly sensitive to dioxygen.1 Publication

Kineticsi

  1. KM=590 µM for 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate1 Publication

    pH dependencei

    Optimum pH is 7.0-7.5.1 Publication

    Temperature dependencei

    Optimum temperature is 60 degrees Celsius.1 Publication

    Pathway:idimethylallyl diphosphate biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate.
    Proteins known to be involved in this subpathway in this organism are:
    1. 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (ispH)
    This subpathway is part of the pathway dimethylallyl diphosphate biosynthesis, which is itself part of Isoprenoid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate, the pathway dimethylallyl diphosphate biosynthesis and in Isoprenoid biosynthesis.

    Pathway:iisopentenyl diphosphate biosynthesis via DXP pathway

    This protein is involved in step 6 of the subpathway that synthesizes isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate.
    Proteins known to be involved in the 6 steps of the subpathway in this organism are:
    1. 1-deoxy-D-xylulose 5-phosphate reductoisomerase (dxr)
    2. 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase (ispD)
    3. 4-diphosphocytidyl-2-C-methyl-D-erythritol kinase (ispE)
    4. 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase (ispF)
    5. 4-hydroxy-3-methylbut-2-en-1-yl diphosphate synthase (flavodoxin) (ispG)
    6. 4-hydroxy-3-methylbut-2-enyl diphosphate reductase (ispH)
    This subpathway is part of the pathway isopentenyl diphosphate biosynthesis via DXP pathway, which is itself part of Isoprenoid biosynthesis.
    View all proteins of this organism that are known to be involved in the subpathway that synthesizes isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate, the pathway isopentenyl diphosphate biosynthesis via DXP pathway and in Isoprenoid biosynthesis.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi13 – 131Iron-sulfur (3Fe-4S)1 Publication
    Binding sitei42 – 421SubstrateBy similarity
    Binding sitei74 – 741SubstrateBy similarity
    Metal bindingi96 – 961Iron-sulfur (3Fe-4S)1 Publication
    Binding sitei124 – 1241SubstrateBy similarity
    Binding sitei165 – 1651SubstrateBy similarity
    Metal bindingi193 – 1931Iron-sulfur (3Fe-4S)1 Publication
    Binding sitei265 – 2651SubstrateBy similarity

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Oxidoreductase

    Keywords - Biological processi

    Isoprene biosynthesis

    Keywords - Ligandi

    3Fe-4S, Iron, Iron-sulfur, Metal-binding, NADP

    Enzyme and pathway databases

    BioCyciAAEO224324:GJBH-1242-MONOMER.
    BRENDAi1.17.1.2. 396.
    UniPathwayiUPA00056; UER00097.
    UPA00059; UER00105.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    4-hydroxy-3-methylbut-2-enyl diphosphate reductase (EC:1.17.1.2)
    Gene namesi
    Name:ispH
    Synonyms:lytB
    Ordered Locus Names:aq_1739
    OrganismiAquifex aeolicus (strain VF5)
    Taxonomic identifieri224324 [NCBI]
    Taxonomic lineageiBacteriaAquificaeAquificalesAquificaceaeAquifex
    ProteomesiUP000000798 Componenti: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 2892894-hydroxy-3-methylbut-2-enyl diphosphate reductasePRO_0000128766Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi224324.aq_1739.

    Structurei

    Secondary structure

    1
    289
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 64Combined sources
    Helixi14 – 2613Combined sources
    Turni27 – 293Combined sources
    Beta strandi34 – 385Combined sources
    Beta strandi40 – 423Combined sources
    Helixi44 – 5310Combined sources
    Beta strandi55 – 573Combined sources
    Beta strandi68 – 714Combined sources
    Helixi78 – 869Combined sources
    Beta strandi90 – 934Combined sources
    Helixi97 – 11115Combined sources
    Beta strandi115 – 1206Combined sources
    Helixi125 – 13612Combined sources
    Beta strandi141 – 1466Combined sources
    Helixi147 – 1559Combined sources
    Beta strandi157 – 1637Combined sources
    Helixi169 – 18214Combined sources
    Beta strandi183 – 1897Combined sources
    Helixi195 – 20612Combined sources
    Helixi207 – 2093Combined sources
    Beta strandi210 – 2178Combined sources
    Helixi222 – 23413Combined sources
    Beta strandi236 – 2438Combined sources
    Helixi244 – 2463Combined sources
    Helixi249 – 2524Combined sources
    Beta strandi256 – 2627Combined sources
    Helixi268 – 28013Combined sources

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3DNFX-ray1.65A/B1-289[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiO67625.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni221 – 2233Substrate bindingBy similarity

    Sequence similaritiesi

    Belongs to the IspH family.Curated

    Phylogenomic databases

    eggNOGiCOG0761.
    HOGENOMiHOG000220193.
    InParanoidiO67625.
    KOiK03527.
    OMAiDDLTFMT.
    OrthoDBiEOG6HF624.

    Family and domain databases

    HAMAPiMF_00191. IspH.
    InterProiIPR003451. LytB/IspH.
    [Graphical view]
    PfamiPF02401. LYTB. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00216. ispH_lytB. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    O67625-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MVDIIIAEHA GFCFGVKRAV KLAEESLKES QGKVYTLGPI IHNPQEVNRL
    60 70 80 90 100
    KNLGVFPSQG EEFKEGDTVI IRSHGIPPEK EEALRKKGLK VIDATCPYVK
    110 120 130 140 150
    AVHEAVCQLT REGYFVVLVG EKNHPEVIGT LGYLRACNGK GIVVETLEDI
    160 170 180 190 200
    GEALKHERVG IVAQTTQNEE FFKEVVGEIA LWVKEVKVIN TICNATSLRQ
    210 220 230 240 250
    ESVKKLAPEV DVMIIIGGKN SGNTRRLYYI SKELNPNTYH IETAEELQPE
    260 270 280
    WFRGVKRVGI SAGASTPDWI IEQVKSRIQE ICEGQLVSS
    Length:289
    Mass (Da):32,104
    Last modified:August 1, 1998 - v1
    Checksum:iA9D910C41727E9F4
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE000657 Genomic DNA. Translation: AAC07596.1.
    PIRiG70449.
    RefSeqiNP_214191.1. NC_000918.1.
    WP_010881128.1. NC_000918.1.

    Genome annotation databases

    EnsemblBacteriaiAAC07596; AAC07596; aq_1739.
    GeneIDi1193340.
    KEGGiaae:aq_1739.
    PATRICi20960466. VBIAquAeo85532_1338.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    AE000657 Genomic DNA. Translation: AAC07596.1.
    PIRiG70449.
    RefSeqiNP_214191.1. NC_000918.1.
    WP_010881128.1. NC_000918.1.

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    3DNFX-ray1.65A/B1-289[»]
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi224324.aq_1739.

    Chemistry

    ChEMBLiCHEMBL2242741.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiAAC07596; AAC07596; aq_1739.
    GeneIDi1193340.
    KEGGiaae:aq_1739.
    PATRICi20960466. VBIAquAeo85532_1338.

    Phylogenomic databases

    eggNOGiCOG0761.
    HOGENOMiHOG000220193.
    InParanoidiO67625.
    KOiK03527.
    OMAiDDLTFMT.
    OrthoDBiEOG6HF624.

    Enzyme and pathway databases

    UniPathwayiUPA00056; UER00097.
    UPA00059; UER00105.
    BioCyciAAEO224324:GJBH-1242-MONOMER.
    BRENDAi1.17.1.2. 396.

    Miscellaneous databases

    EvolutionaryTraceiO67625.

    Family and domain databases

    HAMAPiMF_00191. IspH.
    InterProiIPR003451. LytB/IspH.
    [Graphical view]
    PfamiPF02401. LYTB. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR00216. ispH_lytB. 1 hit.
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: VF5.
    2. "LytB protein catalyzes the terminal step of the 2-C-methyl-D-erythritol-4-phosphate pathway of isoprenoid biosynthesis."
      Altincicek B., Duin E.C., Reichenberg A., Hedderich R., Kollas A.-K., Hintz M., Wagner S., Wiesner J., Beck E., Jomaa H.
      FEBS Lett. 532:437-440(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, PRESENCE OF AN IRON-SULFUR CLUSTER, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES.
    3. "Structure of (E)-4-hydroxy-3-methyl-but-2-enyl diphosphate reductase, the terminal enzyme of the non-mevalonate pathway."
      Rekittke I., Wiesner J., Roehrich R., Demmer U., Warkentin E., Xu W., Troschke K., Hintz M., No J.H., Duin E.C., Oldfield E., Jomaa H., Ermler U.
      J. Am. Chem. Soc. 130:17206-17207(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.65 ANGSTROMS) IN COMPLEX WITH IRON-SULFUR (3FE-4S), COFACTOR, SUBUNIT.

    Entry informationi

    Entry nameiISPH_AQUAE
    AccessioniPrimary (citable) accession number: O67625
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: August 1, 1998
    Last modified: July 22, 2015
    This is version 98 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3

    Similar proteinsi

    Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
    100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
    90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
    50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.