Skip Header

Contribute Send feedback
Read comments (?) or add your own

Q5H2D9 (ISPH_XANOR) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 56. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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
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:XOO1628
OrganismXanthomonas oryzae pv. oryzae (strain KACC10331 / KXO85) [Complete proteome] [HAMAP]
Taxonomic identifier291331 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Gammaproteobacteria › Xanthomonadales › Xanthomonadaceae › Xanthomonas ›

Protein attributes

Sequence length316 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-Rule MF_00191

Catalytic activity

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

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

Cofactor

Binds 1 3Fe-4S cluster per subunit By similarity.

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

Sequence similarities

Belongs to the IspH family.

Sequence caution

The sequence AAW74882.1 differs from that shown. Reason: Erroneous initiation.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3163164-hydroxy-3-methylbut-2-enyl diphosphate reductase HAMAP-Rule MF_00191
PRO_0000128900

Regions

Region227 – 2293Substrate binding By similarity

Sites

Metal binding121Iron-sulfur (3Fe-4S) By similarity
Metal binding961Iron-sulfur (3Fe-4S) By similarity
Metal binding1991Iron-sulfur (3Fe-4S) By similarity
Binding site411Substrate By similarity
Binding site741Substrate By similarity
Binding site1241Substrate By similarity
Binding site1691Substrate By similarity
Binding site2711Substrate By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5H2D9 [UniParc].

Last modified July 19, 2005. Version 2.
Checksum: 7874BA547183E0D8

FASTA31634,716
        10         20         30         40         50         60 
MYVLLANPRG FCAGVDRAIE IVKRAIETLG APIYVRHEVV HNRFVVDDLK QRGAIFVEEL 

        70         80         90        100        110        120 
DEVPDDATVI FSAHGVPQAV RQEAERRGLK VFDATCPLVT KVHFEVARHC RAGRDVVLIG 

       130        140        150        160        170        180 
HAGHPEVEGT MGQWSRERGP GTIYLVEDIE QVATLDVRQP ENLAYTTQTT LSVDDTMGII 

       190        200        210        220        230        240 
EALRARYPAM QGPRHDDICY ATQNRQDAVR DLARQCDLVL VVGSPNSSNS NRLSELARRD 

       250        260        270        280        290        300 
GVESYLIDNA SEIDPAWIVG KQHIGLTAGA SAPQVLVDGV LARLRELGAS GVSELEGEPE 

       310 
SMVFALPKEL RLRLVG

« Hide

References

[1]"The genome sequence of Xanthomonas oryzae pathovar oryzae KACC10331, the bacterial blight pathogen of rice."
Lee B.-M., Park Y.-J., Park D.-S., Kang H.-W., Kim J.-G., Song E.-S., Park I.-C., Yoon U.-H., Hahn J.-H., Koo B.-S., Lee G.-B., Kim H., Park H.-S., Yoon K.-O., Kim J.-H., Jung C.-H., Koh N.-H., Seo J.-S., Go S.-J.
Nucleic Acids Res. 33:577-586(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: KACC10331 / KXO85.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE013598 Genomic DNA. Translation: AAW74882.1. Different initiation.
RefSeqYP_200267.2. NC_006834.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING291331.XOO1628.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAW74882; AAW74882; XOO1628.
GeneID3262536.
KEGGxoo:XOO1628.
PATRIC24102333. VBIXanOry111333_1805.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0761.
HOGENOMHOG000220192.
KOK03527.
OMAQDAMFSL.
ProtClustDBPRK01045.

Enzyme and pathway databases

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...

Entry information

Entry nameISPH_XANOR
AccessionPrimary (citable) accession number: Q5H2D9
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2005
Last sequence update: July 19, 2005
Last modified: May 1, 2013
This is version 56 of the entry and version 2 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

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents