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O67625 (ISPH_AQUAE) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 88. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
4-hydroxy-3-methylbut-2-enyl diphosphate reductase

EC=1.17.1.2
Gene names
Name:ispH
Synonyms:lytB
Ordered Locus Names:aq_1739
OrganismAquifex aeolicus (strain VF5) [Reference proteome] [HAMAP]
Taxonomic identifier224324 [NCBI]
Taxonomic lineageBacteriaAquificaeAquificalesAquificaceaeAquifex

Protein attributes

Sequence length289 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Converts 1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). HAMAP-Rule MF_00191

Catalytic activity

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

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

Cofactor

Binds 1 3Fe-4S cluster per subunit. Ref.3

Enzyme regulation

Highly sensitive to dioxygen. Ref.2

Pathway

Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate: step 1/1. HAMAP-Rule MF_00191

Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 6/6. HAMAP-Rule MF_00191

Subunit structure

Homodimer. Ref.3

Sequence similarities

Belongs to the IspH family.

Biophysicochemical properties

Kinetic parameters:

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

pH dependence:

Optimum pH is 7.0-7.5.

Temperature dependence:

Optimum temperature is 60 degrees Celsius.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 2892894-hydroxy-3-methylbut-2-enyl diphosphate reductase HAMAP-Rule MF_00191
PRO_0000128766

Regions

Region221 – 2233Substrate binding By similarity

Sites

Metal binding131Iron-sulfur (3Fe-4S)
Metal binding961Iron-sulfur (3Fe-4S)
Metal binding1931Iron-sulfur (3Fe-4S)
Binding site421Substrate By similarity
Binding site741Substrate By similarity
Binding site1241Substrate By similarity
Binding site1651Substrate By similarity
Binding site2651Substrate By similarity

Secondary structure

................................................. 289
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O67625 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: A9D910C41727E9F4

FASTA28932,104
        10         20         30         40         50         60 
MVDIIIAEHA GFCFGVKRAV KLAEESLKES QGKVYTLGPI IHNPQEVNRL KNLGVFPSQG 

        70         80         90        100        110        120 
EEFKEGDTVI IRSHGIPPEK EEALRKKGLK VIDATCPYVK AVHEAVCQLT REGYFVVLVG 

       130        140        150        160        170        180 
EKNHPEVIGT LGYLRACNGK GIVVETLEDI GEALKHERVG IVAQTTQNEE FFKEVVGEIA 

       190        200        210        220        230        240 
LWVKEVKVIN TICNATSLRQ ESVKKLAPEV DVMIIIGGKN SGNTRRLYYI SKELNPNTYH 

       250        260        270        280 
IETAEELQPE WFRGVKRVGI SAGASTPDWI IEQVKSRIQE ICEGQLVSS 

« Hide

References

« Hide 'large scale' references
[1]"The complete genome of the hyperthermophilic bacterium Aquifex aeolicus."
Deckert G., Warren P.V., Gaasterland T., Young W.G., Lenox A.L., Graham D.E., Overbeek R., Snead M.A., Keller M., Aujay M., Huber R., Feldman R.A., Short J.M., Olsen G.J., Swanson R.V.
Nature 392:353-358(1998) [PubMed] [Europe PMC] [Abstract]
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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE000657 Genomic DNA. Translation: AAC07596.1.
PIRG70449.
RefSeqNP_214191.1. NC_000918.1.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3DNFX-ray1.65A/B1-289[»]
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224324.aq_1739.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAC07596; AAC07596; aq_1739.
GeneID1193340.
KEGGaae:aq_1739.
PATRIC20960466. VBIAquAeo85532_1338.

Phylogenomic databases

eggNOGCOG0761.
HOGENOMHOG000220193.
KOK03527.
OMAGKYNHEE.
OrthoDBEOG6HF624.
ProtClustDBCLSK2299815.

Enzyme and pathway databases

BioCycAAEO224324:GJBH-1242-MONOMER.
UniPathwayUPA00056; UER00097.
UPA00059; UER00105.

Family and domain databases

HAMAPMF_00191. IspH.
InterProIPR003451. LytB.
[Graphical view]
PfamPF02401. LYTB. 1 hit.
[Graphical view]
TIGRFAMsTIGR00216. ispH_lytB. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceO67625.

Entry information

Entry nameISPH_AQUAE
AccessionPrimary (citable) accession number: O67625
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: August 1, 1998
Last modified: February 19, 2014
This is version 88 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways