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O67625

- ISPH_AQUAE

UniProt

O67625 - ISPH_AQUAE

Protein

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

Gene

ispH

Organism
Aquifex aeolicus (strain VF5)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 91 (01 Oct 2014)
      Sequence version 1 (01 Aug 1998)
      Previous versions | rss
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    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

    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

    Pathwayi

    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

    1. 3 iron, 4 sulfur cluster binding Source: UniProtKB-HAMAP
    2. 4-hydroxy-3-methylbut-2-en-1-yl diphosphate reductase activity Source: UniProtKB-HAMAP
    3. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. dimethylallyl diphosphate biosynthetic process Source: UniProtKB-UniPathway
    2. isopentenyl diphosphate biosynthetic process, methylerythritol 4-phosphate pathway Source: UniProtKB-HAMAP
    3. terpenoid biosynthetic process Source: UniProtKB-HAMAP

    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.
    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: 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 – 64
    Helixi14 – 2613
    Turni27 – 293
    Beta strandi34 – 385
    Beta strandi40 – 423
    Helixi44 – 5310
    Beta strandi55 – 573
    Beta strandi68 – 714
    Helixi78 – 869
    Beta strandi90 – 934
    Helixi97 – 11115
    Beta strandi115 – 1206
    Helixi125 – 13612
    Beta strandi141 – 1466
    Helixi147 – 1559
    Beta strandi157 – 1637
    Helixi169 – 18214
    Beta strandi183 – 1897
    Helixi195 – 20612
    Helixi207 – 2093
    Beta strandi210 – 2178
    Helixi222 – 23413
    Beta strandi236 – 2438
    Helixi244 – 2463
    Helixi249 – 2524
    Beta strandi256 – 2627
    Helixi268 – 28013

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    KOiK03527.
    OMAiLEMYGAP.
    OrthoDBiEOG6HF624.

    Family and domain databases

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

    Sequencei

    Sequence statusi: Complete.

    O67625-1 [UniParc]FASTAAdd to Basket

    « Hide

    MVDIIIAEHA GFCFGVKRAV KLAEESLKES QGKVYTLGPI IHNPQEVNRL    50
    KNLGVFPSQG EEFKEGDTVI IRSHGIPPEK EEALRKKGLK VIDATCPYVK 100
    AVHEAVCQLT REGYFVVLVG EKNHPEVIGT LGYLRACNGK GIVVETLEDI 150
    GEALKHERVG IVAQTTQNEE FFKEVVGEIA LWVKEVKVIN TICNATSLRQ 200
    ESVKKLAPEV DVMIIIGGKN SGNTRRLYYI SKELNPNTYH IETAEELQPE 250
    WFRGVKRVGI SAGASTPDWI IEQVKSRIQE ICEGQLVSS 289
    Length:289
    Mass (Da):32,104
    Last modified:August 1, 1998 - v1
    Checksum:iA9D910C41727E9F4
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AE000657 Genomic DNA. Translation: AAC07596.1 .
    PIRi G70449.
    RefSeqi NP_214191.1. NC_000918.1.
    WP_010881128.1. NC_000918.1.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3DNF X-ray 1.65 A/B 1-289 [» ]
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 224324.aq_1739.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC07596 ; AAC07596 ; aq_1739 .
    GeneIDi 1193340.
    KEGGi aae:aq_1739.
    PATRICi 20960466. VBIAquAeo85532_1338.

    Phylogenomic databases

    eggNOGi COG0761.
    HOGENOMi HOG000220193.
    KOi K03527.
    OMAi LEMYGAP.
    OrthoDBi EOG6HF624.

    Enzyme and pathway databases

    UniPathwayi UPA00056 ; UER00097 .
    UPA00059 ; UER00105 .
    BioCyci AAEO224324:GJBH-1242-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei O67625.

    Family and domain databases

    HAMAPi MF_00191. IspH.
    InterProi IPR003451. LytB.
    [Graphical view ]
    Pfami PF02401. LYTB. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00216. ispH_lytB. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 91 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