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Reviewed, UniProtKB/Swiss-Prot Q6G3Z8 (ISPDF_BARHE)

Last modified September 22, 2009. Version 36. 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: BH05820
OrganismBartonella henselae (Rochalimaea henselae) [Complete proteome] [HAMAP]
Taxonomic identifier38323 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBartonellaceaeBartonella

Protein attributes

Sequence length397 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 diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6. HAMAP MF_01520

Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate 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 – 397397Bifunctional enzyme ispD/ispF HAMAP MF_01520
PRO_0000075656

Regions

Region1 – 2362362-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
Region237 – 3971612-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520

Sites

Metal binding2431Divalent metal cation By similarity
Metal binding2451Divalent metal cation By similarity
Metal binding2771Divalent metal cation By similarity
Site151Transition state stabilizer By similarity
Site241Transition state stabilizer By similarity
Site1551Positions MEP for the nucleophilic attack By similarity
Site2121Positions MEP for the nucleophilic attack By similarity
Site2691Transition state stabilizer By similarity
Site3681Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6G3Z8-1 [UniParc].

Last modified June 26, 2007. Version 2.
Checksum: 1488BE631F41E982

FASTA39744,057
        10         20         30         40         50         60 
MSIAAVILAA GRGKRAGSLP KKPKQYRLLG QEPVICHTVR CFCQNPAITT IILVIHPEDR 

        70         80         90        100        110        120 
QICEQAIADF KEQLIIVEGG NTRQKSTLRG LQALRKFKPK YVHIHDGARP FVENKLLEQI 

       130        140        150        160        170        180 
HTTVTPQEGV LPVLAVCDTL KRINSTHHVL ETIPRTHLYS AQTPQCFPFE RILAAHEKAI 

       190        200        210        220        230        240 
KTCKKEFTDD SAIAEWFGIS MRTIPGSPHN IKITWHEDLN TAHLYLQKKM QMFPDIRTGN 

       250        260        270        280        290        300 
GYDVHSFEEG NSLILCGIKI PFHKKLNGHS DADVALHALT DALLATRGAG DIGTHFPPSD 

       310        320        330        340        350        360 
PQWQNVSSEI FLRHALDIVK QAGGRIANVD ITLIAEEPKI GPYRHAMVGN LMNMLTILPD 

       370        380        390 
RISIKATTNE KLGFIGRGEG IAAFATANVL YPGEIPK 

« 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: ATCC 49882 / Houston 1.

Cross-references

Sequence databases

BX897699 Genomic DNA. Translation: CAF27390.1. Different initiation.

3D structure databases

ModBaseSearch...

Genome annotation databases

GenomeReviewsGene locus BH05820 in contig BX897699_GR.
KEGGbhe:BH05820.
NMPDRfig|283166.1.peg.544.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ6G3Z8.

Enzyme and pathway databases

BioCycBHEN283166:BH05820-MON.
BRENDA2.7.7.60. 277357.
4.6.1.12. 277357.

Family and domain databases

HAMAPMF_01520.
[Tree]
InterProIPR001228. ISPD_synthase.
IPR018294. ISPD_synthase_CS.
IPR003526. MECDP_synthase_core.
IPR020555. MECDP_synthase_CS.
[Graphical view]
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_BARHE
AccessionPrimary (citable) accession number: Q6G3Z8
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: June 26, 2007
Last modified: September 22, 2009
This is version 36 of the entry and version 2 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