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Q8FQP0 (ISPH_COREF) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 47. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

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

EC=1.17.1.2
Gene names
Name:ispH
Ordered Locus Names:CE1079
OrganismCorynebacterium efficiens [Complete proteome] [HAMAP]
Taxonomic identifier152794 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length336 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

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

Catalytic activity

Isopentenyl diphosphate + NAD(P)+ + H2O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H. HAMAP MF_00191

Dimethylallyl diphosphate + NAD(P)+ + H2O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H. HAMAP MF_00191

Cofactor

Binds 1 3Fe-4S cluster By similarity. HAMAP MF_00191

Pathway

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

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

Sequence similarities

Belongs to the IspH family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3363364-hydroxy-3-methylbut-2-enyl diphosphate reductase HAMAP MF_00191
PRO_0000128807

Sequences

Sequence LengthMass (Da)Tools
Q8FQP0 [UniParc].

Last modified March 1, 2003. Version 1.
Checksum: C47E456FEEB82AC7

FASTA33636,430
        10         20         30         40         50         60 
MFGQRLDTLG AMSSSVSSPS PETGKKILLA APRGYCAGVD RAVETVERAL EEYGAPIYVR 

        70         80         90        100        110        120 
KEIVHNRYVV DTLAEKGVIF VEEASEAPEG AHMVFSAHGV SPAVKEEAAA KNLQAIDAAC 

       130        140        150        160        170        180 
PLVTKVHNEV KRFDKQGFHI LFIGHEGHEE VEGTMGHSLD RTHLVDGIES IPGLPAFLAD 

       190        200        210        220        230        240 
EPNLIWLSQT TLSVDETMEI VRELKKVYPQ LQDPPSDDIC YATQNRQVAV KAIAERCDLM 

       250        260        270        280        290        300 
IVVGSTNSSN SVRLVEVALQ AGAKNAYLVD YAHQIDEAWL DGVQTIGISS GASVPEILVT 

       310        320        330 
GVLERLAGYG FDDVEEVTTA AEKIVFALPR VLRPAR 

« Hide

References

[1]"Comparative complete genome sequence analysis of the amino acid replacements responsible for the thermostability of Corynebacterium efficiens."
Nishio Y., Nakamura Y., Kawarabayasi Y., Usuda Y., Kimura E., Sugimoto S., Matsui K., Yamagishi A., Kikuchi H., Ikeo K., Gojobori T.
Genome Res. 13:1572-1579(2003) [PubMed: 12840036] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000035 Genomic DNA. Translation: BAC17889.1.
RefSeqNP_737689.1. NC_004369.1.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID1033260.
GenomeReviewsGene locus CE1079 in contig BA000035_GR.
KEGGcef:CE1079.
NMPDRfig|196164.1.peg.1079.
PATRIC21488296. VBICorEff9312_1082.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG335228.
OMAAMAPECD.
PhylomeDBQ8FQP0.
ProtClustDBPRK01045.

Enzyme and pathway databases

BioCycCEFF196164:CE1079-MONOMER.

Family and domain databases

HAMAPMF_00191. IspH.
[Tree]
InterProIPR003451. LytB.
[Graphical view]
KOK03527.
PfamPF02401. LYTB. 1 hit.
[Graphical view]
TIGRFAMsTIGR00216. IspH_lytB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameISPH_COREF
AccessionPrimary (citable) accession number: Q8FQP0
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: March 1, 2003
Last modified: January 25, 2012
This is version 47 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families