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Reviewed, UniProtKB/Swiss-Prot Q6G164 (ISPDF_BARQU)

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: BQ04980
OrganismBartonella quintana (Rochalimaea quintana) [Complete proteome] [HAMAP]
Taxonomic identifier803 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

Protein attributes

Sequence length391 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 – 391391Bifunctional enzyme ispD/ispF HAMAP MF_01520
PRO_0000075657

Regions

Region1 – 2302302-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
Region231 – 3911612-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520

Sites

Metal binding2371Divalent metal cation By similarity
Metal binding2391Divalent metal cation By similarity
Metal binding2711Divalent metal cation By similarity
Site91Transition state stabilizer By similarity
Site181Transition state stabilizer By similarity
Site1491Positions MEP for the nucleophilic attack By similarity
Site2061Positions MEP for the nucleophilic attack By similarity
Site2631Transition state stabilizer By similarity
Site3621Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6G164-1 [UniParc].

Last modified July 19, 2004. Version 1.
Checksum: E81E1DC69C3B2B75

FASTA39143,792
        10         20         30         40         50         60 
MLAAGRGKRA GSLQKNPKQY RLLGQKPVIC HTVRCFCQHP AITTIILVIH PEDRQICEQA 

        70         80         90        100        110        120 
ITDFKEHLII VEGGNTRQIS TLRGLHALKK FKPKYVHIHD GARPFIENKL LEKIHTTVNH 

       130        140        150        160        170        180 
QEGVLPVLPV SDTLKRVNST HRVLETIPHT HLYSAQTPQC FPFERILAAH ERAMQTCKKE 

       190        200        210        220        230        240 
FTDDSAIAEW FGIPMHTIPG DSHNIKITWH EDFDTAHLYL KKKMQMFPDI RTGNGYDVHS 

       250        260        270        280        290        300 
FEEGTSLILC GIKIPFHKKL KGHSDADVAF HALTDALLAT QGAGDIGTHF LPSDPQWKNA 

       310        320        330        340        350        360 
PSEIFLRHAL EIIKQAGGRI ANVDITLIAE TPKIGPYRHT MTENLMNILS LSLDRISIKA 

       370        380        390 
TTNEKLGFIG REEGIAALAT ATVLYPGEIP K 

« Hide

References

[1]"The louse-borne human pathogen Bartonella quintana is a genomic derivative of the zoonotic agent Bartonella henselae."
Alsmark U.C.M., Frank A.C., Karlberg E.O., Legault B.-A., Ardell D.H., Canbaeck B., Eriksson A.-S., Naeslund A.K., Handley S.A., Huvet M., La Scola B., Holmberg M., Andersson S.G.E.
Proc. Natl. Acad. Sci. U.S.A. 101:9716-9721(2004) [PubMed: 15210978] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Toulouse.

Cross-references

Sequence databases

BX897700 Genomic DNA. Translation: CAF25997.1.
RefSeqYP_032176.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID2866390.
GenomeReviewsGene locus BQ04980 in contig BX897700_GR.
KEGGbqu:BQ04980.
NMPDRfig|283165.1.peg.446.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ6G164.
OMAQ6G164. IVLIHDA.

Enzyme and pathway databases

BioCycBQUI283165:BQ04980-MON.
BRENDA2.7.7.60. 292235.
4.6.1.12. 292235.

Family and domain databases

HAMAPMF_01520.
[Tree]
InterProIPR001228. ISPD_synthase.
IPR018294. ISPD_synthase_CS.
IPR003526. MECDP_synthase_core.
[Graphical view]
Gene3DG3DSA:3.30.1330.50. MECDP_synthase_core. 1 hit.
PfamPF01128. IspD. 1 hit.
PF02542. YgbB. 1 hit.
[Graphical view]
TIGRFAMsTIGR00453. ispD. 1 hit.
TIGR00151. ispF. 1 hit.
PROSITEPS01295. ISPD. False negative.
PS01350. ISPF. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameISPDF_BARQU
AccessionPrimary (citable) accession number: Q6G164
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: July 19, 2004
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