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Reviewed, UniProtKB/Swiss-Prot Q89LQ8 (ISPDF_BRAJA)

Last modified June 16, 2009. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Bifunctional enzyme ispD/ispF
Including the following 2 domains:
    1- Recommended name:
            2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase
              EC=2.7.7.60
        Alternative name(s):
            4-diphosphocytidyl-2C-methyl-D-erythritol synthase
            MEP cytidylyltransferase
              Short name=MCT
    2- Recommended name:
            2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
                Short name=MECPS
                Short name=MECDP-synthase
              EC=4.6.1.12
Gene names
Name: ispDF
Ordered Locus Names: bll4485
OrganismBradyrhizobium japonicum [Complete proteome] [HAMAP]
Taxonomic identifier375 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeBradyrhizobium

Protein attributes

Sequence length398 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

General annotation (Comments)

Function

Bifunctional enzyme that catalyzes the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from CTP and 2-C-methyl-D-erythritol 4-phosphate (MEP) (ispD), and converts 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate into 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (MECDP) and CMP (ispF) By similarity.

Catalytic activity

CTP + 2-C-methyl-D-erythritol 4-phosphate = diphosphate + 4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol. HAMAP MF_01520

2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol = 2-C-methyl-D-erythritol 2,4-cyclodiphosphate + CMP. HAMAP MF_01520

Cofactor

Divalent metal cations By similarity.

Pathway

Isoprenoid biosynthesis; isopentenyl-PP biosynthesis via DXP pathway; isopentenyl-PP from 1-deoxy-D-xylulose 5-phosphate: step 2/6. HAMAP MF_01520

Isoprenoid biosynthesis; isopentenyl-PP biosynthesis via DXP pathway; isopentenyl-PP from 1-deoxy-D-xylulose 5-phosphate: step 4/6.

Sequence similarities

In the N-terminal section; belongs to the ispD family.

In the C-terminal section; belongs to the ispF family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 398398Bifunctional enzyme ispD/ispF HAMAP MF_01520
PRO_0000075658

Regions

Region1 – 2342342-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
Region235 – 3981642-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520

Sites

Metal binding2411Divalent metal cation By similarity
Metal binding2431Divalent metal cation By similarity
Metal binding2751Divalent metal cation By similarity
Site191Transition state stabilizer By similarity
Site261Transition state stabilizer By similarity
Site1561Positions MEP for the nucleophilic attack By similarity
Site2131Positions MEP for the nucleophilic attack By similarity
Site2671Transition state stabilizer By similarity
Site3661Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q89LQ8-1 [UniParc].

Last modified June 1, 2003. Version 1.
Checksum: 93E0A201CB315B6A

FASTA39842,226
        10         20         30         40         50         60 
MAKSQRTAVV LVAAGRGLRA GAGGPKQYRE IGGQPVIYRA MEAFSRHPDV FAVQPVVNPD 

        70         80         90        100        110        120 
DSAMFTAAVA GLKHEPPTNG GATRQASVLA GLEALAKHQP DIVLIHDAAR PFVSDGVISR 

       130        140        150        160        170        180 
AIDAASRTGA AIPVVPVTDT IKLTGASGNV EDTPDRARLR IAQTPQSFRF DVILEAHRRA 

       190        200        210        220        230        240 
AKDGRSDFTD DAAIAEWAGL TVATFEGDVA NMKLTTPEDF VREEARLAAQ LGDIRTGTGY 

       250        260        270        280        290        300 
DVHAFGEGDH VMICGVRVPH SKGFLAHSDG DVGLHALVDA ILGALADGDI GSHFPPSDAK 

       310        320        330        340        350        360 
WKGASSDQFL KYAIERVAQR GGRVANLEVT MICERPKIGP LRDTMRARIA EISGVDISRV 

       370        380        390 
AVKATTSERL GFTGREEGIA ATASATIRLP FNEKTWSV 

« Hide

References

[1]"Complete genomic sequence of nitrogen-fixing symbiotic bacterium Bradyrhizobium japonicum USDA110."
Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S., Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M., Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.
DNA Res. 9:189-197(2002) [PubMed: 12597275] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: USDA 110.

Cross-references

Sequence databases

BA000040 Genomic DNA. Translation: BAC49750.1.
RefSeqNP_771125.1.

3D structure databases

HSSPHSSP built from PDB template 1JN1 based on UniProtKB P44815.
ModBaseSearch...

Genome annotation databases

GeneID1052654.
GenomeReviewsGene locus bll4485 in contig BA000040_GR.
KEGGbja:bll4485.
NMPDRfig|224911.1.peg.4485.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ89LQ8.
OMAQ89LQ8. IVLIHDA.

Enzyme and pathway databases

BioCycBJAP224911:BLL4485-MON.
BRENDA2.7.7.60. 280.
4.6.1.12. 280.

Family and domain databases

HAMAPMF_01520.
[Tree]
InterProIPR001228. ISPD_synthase.
IPR018294. ISPD_synthase_CS.
IPR003526. MECDP_synthase_core.
[Graphical view]
PfamPF01128. IspD. 1 hit.
PF02542. YgbB. 1 hit.
[Graphical view]
TIGRFAMsTIGR00453. ispD. 1 hit.
TIGR00151. ispF. 1 hit.
PROSITEPS01295. ISPD. 1 hit.
PS01350. ISPF. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameISPDF_BRAJA
AccessionPrimary (citable) accession number: Q89LQ8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: June 1, 2003
Last modified: June 16, 2009
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents