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Q5PAE7 (ISPH_ANAMM) 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

EC=1.17.1.2
Gene names
Name:ispH
Synonyms:lytB
Ordered Locus Names:AM804
OrganismAnaplasma marginale (strain St. Maries) [Complete proteome] [HAMAP]
Taxonomic identifier234826 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRickettsialesAnaplasmataceaeAnaplasma

Protein attributes

Sequence length342 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 – 3423424-hydroxy-3-methylbut-2-enyl diphosphate reductase HAMAP MF_00191
PRO_0000128764

Sequences

Sequence LengthMass (Da)Tools
Q5PAE7 [UniParc].

Last modified January 4, 2005. Version 1.
Checksum: E8C59A841DEED1CC

FASTA34237,671
        10         20         30         40         50         60 
MEAVQQNHSV CRGYCGVMLR SRSGGFFRRG FMLGNVEVIL ARPRGFCAGV ERAVRTLESV 

        70         80         90        100        110        120 
ASRYAGTREV YALHEIVHNL HVVNSFKKMG VKFVSALHEV PEGAVLVFSA HGVSQQVKEE 

       130        140        150        160        170        180 
SRRKGLTVVD ATCPLVTKVH LEIQRYDKSG YQVILVGHKG HREVEGSMGQ VSNPVVLVQN 

       190        200        210        220        230        240 
VQDVQSIKIP SAAKLAYVTQ TTLSMDDTAE IISALKLRFP RIVGPDLRDI CYATQNRQTA 

       250        260        270        280        290        300 
VKAMSQMVDV VLAIGSKNSS NSNRLLDLAK AQNARAYLID SYRNIDLEWL IGARRIGITA 

       310        320        330        340 
GASAPEILVQ EVIDYLGLHA NLKVRTMDGV SENITFKLPE LD 

« Hide

References

[1]"Complete genome sequencing of Anaplasma marginale reveals that the surface is skewed to two superfamilies of outer membrane proteins."
Brayton K.A., Kappmeyer L.S., Herndon D.R., Dark M.J., Tibbals D.L., Palmer G.H., McGuire T.C., Knowles D.P. Jr.
Proc. Natl. Acad. Sci. U.S.A. 102:844-849(2005) [PubMed: 15618402] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: St. Maries.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000030 Genomic DNA. Translation: AAV86733.1.
RefSeqYP_153988.1. NC_004842.2.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGQ5PAE7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3171942.
GenomeReviewsGene locus AM804 in contig CP000030_GR.
KEGGama:AM804.
PATRIC20947557. VBIAnaMar46146_0694.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0761.
HOGENOMHBG335228.
OMAIVHNTYV.
PhylomeDBQ5PAE7.
ProtClustDBPRK01045.

Enzyme and pathway databases

BioCycAMAR234826:AM804-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_ANAMM
AccessionPrimary (citable) accession number: Q5PAE7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: January 4, 2005
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