Skip Header

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

Q07J28 (Q07J28_RHOP5) Unreviewed, UniProtKB/TrEMBL

Last modified May 1, 2013. Version 55. Feed History...

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

Names and origin

Protein namesRecommended name:
4-hydroxy-3-methylbut-2-enyl diphosphate reductase HAMAP-Rule MF_00191
EC=1.17.1.2 HAMAP-Rule MF_00191
Gene names
Name:ispH HAMAP-Rule MF_00191
Ordered Locus Names:RPE_4130 EMBL ABJ08056.1
OrganismRhodopseudomonas palustris (strain BisA53) [Complete proteome] [HAMAP] EMBL ABJ08056.1
Taxonomic identifier316055 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Bradyrhizobiaceae › Rhodopseudomonas ›

Protein attributes

Sequence length320 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
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. SAAS SAAS003451 HAMAP-Rule MF_00191

Catalytic activity

Dimethylallyl diphosphate + NAD(P)+ + H2O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H. SAAS SAAS003451 HAMAP-Rule MF_00191

Isopentenyl diphosphate + NAD(P)+ + H2O = (E)-4-hydroxy-3-methylbut-2-en-1-yl diphosphate + NAD(P)H. SAAS SAAS003451 HAMAP-Rule MF_00191

Cofactor

Binds 1 3Fe-4S cluster per subunit By similarity. SAAS SAAS003451 HAMAP-Rule MF_00191

Pathway

Isoprenoid biosynthesis; dimethylallyl diphosphate biosynthesis; dimethylallyl diphosphate from (2E)-4-hydroxy-3-methylbutenyl diphosphate: step 1/1. HAMAP-Rule MF_00191 SAAS SAAS003451

Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 6/6. SAAS SAAS003451 HAMAP-Rule MF_00191

Sequence similarities

Belongs to the IspH family. HAMAP-Rule MF_00191

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2525 Potential EMBL ABJ08056.1
Chain26 – 320295 Potential
PRO_5000133898

Regions

Region230 – 2323Substrate binding By similarity HAMAP-Rule MF_00191

Sites

Metal binding181Iron-sulfur (3Fe-4S) By similarity HAMAP-Rule MF_00191
Metal binding1031Iron-sulfur (3Fe-4S) By similarity HAMAP-Rule MF_00191
Metal binding2021Iron-sulfur (3Fe-4S) By similarity HAMAP-Rule MF_00191
Binding site471Substrate By similarity HAMAP-Rule MF_00191
Binding site811Substrate By similarity HAMAP-Rule MF_00191
Binding site1311Substrate By similarity HAMAP-Rule MF_00191
Binding site1721Substrate By similarity HAMAP-Rule MF_00191
Binding site2751Substrate By similarity HAMAP-Rule MF_00191

Sequences

Sequence LengthMass (Da)Tools
Q07J28 [UniParc].

Last modified October 31, 2006. Version 1.
Checksum: 70602656132C48E6

FASTA32034,754
        10         20         30         40         50         60 
MQTKPPLKIL LCSPRGFCAG VVRAIDTVER ALSLYGAPVY VRHEIVHNKY VVDSLRAKGA 

        70         80         90        100        110        120 
IFVEELSEIP ETDAPVVFSA HGVPKDVPEE AHRRKFFSLD ATCPLVTKVH REAAIHFKRG 

       130        140        150        160        170        180 
REILLIGHSH HPEVVGTLGQ LPDGAVSLIE TAADASAYQP KDPDNLAFVT QTTLSIDDTS 

       190        200        210        220        230        240 
GIVSILRKRF PNISGPHKED ICYATTNRQA AVKKVAPIVD AMIVVGAPNS SNSQRLREVA 

       250        260        270        280        290        300 
EREGCKIAVL AQRASDIDLK QFEGVTSLGL TAGASAPEVI VEEIMGAFAE YYDLKVETVS 

       310        320 
AAEENEFFPL PRALRPDAAE

« Hide

References

[1]"Complete sequence of Rhodopseudomonas palustris BisA53."
US DOE Joint Genome Institute
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Pelletier D.A., Kyrpides N., Kim E., Harwood C.S., Oda Y., Richardson P.
Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: BisA53 EMBL ABJ08056.1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000463 Genomic DNA. Translation: ABJ08056.1.
RefSeqYP_783036.1. NC_008435.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRING316055.RPE_4130.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABJ08056; ABJ08056; RPE_4130.
GeneID4361823.
KEGGrpe:RPE_4130.
PATRIC23262906. VBIRhoPal93214_4182.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0761.
HOGENOMHOG000220192.
KOK03527.
OMAPNISGPH.
ProtClustDBPRK01045.

Enzyme and pathway databases

BioCycRPAL316055:GHR9-4184-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...

Entry information

Entry nameQ07J28_RHOP5
AccessionPrimary (citable) accession number: Q07J28
Entry history
Integrated into UniProtKB/TrEMBL: October 31, 2006
Last sequence update: October 31, 2006
Last modified: May 1, 2013
This is version 55 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info