SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

O67625

- ISPH_AQUAE

UniProt

O67625 - ISPH_AQUAE

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

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

Gene
ispH, lytB, aq_1739
Organism
Aquifex aeolicus (strain VF5)
Status
Reviewed - 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).UniRule annotation

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.

Temperature dependencei

Optimum temperature is 60 degrees Celsius.

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi13 – 131Iron-sulfur (3Fe-4S)
Binding sitei42 – 421Substrate By similarity
Binding sitei74 – 741Substrate By similarity
Metal bindingi96 – 961Iron-sulfur (3Fe-4S)
Binding sitei124 – 1241Substrate By similarity
Binding sitei165 – 1651Substrate By similarity
Metal bindingi193 – 1931Iron-sulfur (3Fe-4S)
Binding sitei265 – 2651Substrate By 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
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.
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 reductaseUniRule annotationPRO_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[»]

Miscellaneous databases

EvolutionaryTraceiO67625.

Family & Domainsi

Region

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

Sequence similaritiesi

Belongs to the IspH family.

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

« 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: September 3, 2014
This is version 90 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