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Q629Z7 (ISPH1_BURMA) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 48. 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 1
EC=1.17.1.2
Gene names
Name:ispH1
Synonyms:ispH-1
Ordered Locus Names:BMAA1962
OrganismBurkholderia mallei (Pseudomonas mallei) [Complete proteome] [HAMAP]
Taxonomic identifier13373 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Burkholderiaceae › Burkholderia › pseudomallei group

Protein attributes

Sequence length313 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 – 3133134-hydroxy-3-methylbut-2-enyl diphosphate reductase 1 HAMAP MF_00191
PRO_0000128791

Sequences

Sequence LengthMass (Da)Tools
Q629Z7 [UniParc].

Last modified October 25, 2004. Version 1.
Checksum: 944BC58A7CBE079B

FASTA31333,769
        10         20         30         40         50         60 
MRVILAQPRG FCAGVVRAIE IVERALQQNG APVYVRHEIV HNRHVVENLR NKGARFVEEL 

        70         80         90        100        110        120 
DEVPHGAVAI FSAHGVAQTV EQDAQARGLD VLDATCPLVT KVHVQGRQYV AAGRRLILIG 

       130        140        150        160        170        180 
HAGHPEVEGT IGQIPAEVIL VQSEAEVDTL TLPADTPVAY VTQTTLSVDD TRGIIEALQR 

       190        200        210        220        230        240 
RFTDIVGPDT RDICYATQNR QAAVRELSEQ VDVLLVVGAT NSSNSNRLRE IGTESGVPSY 

       250        260        270        280        290        300 
LVADGSEVRA EWFANARTVG LTAGASAPEE MVEDVIAALR ALGPLEVATM SGREEKVEFK 

       310 
LPAKLTQAVA REV

« Hide

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000011 Genomic DNA. Translation: AAU45677.1.
RefSeqYP_106485.1. NC_006349.2.

3D structure databases

ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3086216.
GenomeReviewsGene locus BMAA1962 in contig CP000011_GR.
KEGGbma:BMAA1962.
PATRIC19126202. VBIBurMal55007_5581.
TIGRBMAA1962.

Phylogenomic databases

HOGENOMHBG335228.
OMAHNQGKRY.
PhylomeDBQ629Z7.
ProtClustDBPRK01045.

Enzyme and pathway databases

BioCycBMAL243160:BMA_A1962-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 nameISPH1_BURMA
AccessionPrimary (citable) accession number: Q629Z7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: October 25, 2004
Last modified: January 25, 2012
This is version 48 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

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