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Reviewed, UniProtKB/Swiss-Prot Q57D18 (ISPDF_BRUAB)

Last modified November 3, 2009. Version 25. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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: BruAb1_1126
OrganismBrucella abortus [Complete proteome] [HAMAP]
Taxonomic identifier235 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length390 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 – 390390Bifunctional enzyme ispD/ispF HAMAP MF_01520
PRO_0000075659

Regions

Region1 – 2292292-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
Region230 – 3901612-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520

Sites

Metal binding2361Divalent metal cation By similarity
Metal binding2381Divalent metal cation By similarity
Metal binding2701Divalent metal cation By similarity
Site81Transition state stabilizer By similarity
Site171Transition state stabilizer By similarity
Site1481Positions MEP for the nucleophilic attack By similarity
Site2051Positions MEP for the nucleophilic attack By similarity
Site2621Transition state stabilizer By similarity
Site3611Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q57D18-1 [UniParc].

Last modified May 10, 2005. Version 1.
Checksum: 05AB0A2FBA03DEDB

FASTA39041,840
        10         20         30         40         50         60 
MAAGRGERAG QSAEGPKQYR LIGAEAVLAR TLRAFTDCPL IGTIAVVIHP DDHALYRRAV 

        70         80         90        100        110        120 
PEKHENVILV TGGPTRQEST RLGLLALKDE APQYVLIHDG VRPFIGQDLL ERIIANLTPD 

       130        140        150        160        170        180 
NGVLPALAVS DTLKRAAADG MVETTISRTG LFAAQTPQAF PYAPILDAHE KAFAINRTDF 

       190        200        210        220        230        240 
TDDAAIAEWQ EIAVRIIEGS ADNTKLTWAK DIEMADKRLR QDHAVFPDIR TGNGYDVHSF 

       250        260        270        280        290        300 
EPGDHVTLCG VKIPHEAKLN GHSDADVALH ALTDALLATR GAGDIGTHFP PSDPQWKGAA 

       310        320        330        340        350        360 
SRIFIEHAAK IVREAGGRIA NVDVTLISEA PKIGPHRAAM TQALCDMLGI AADRVSIKAT 

       370        380        390 
TNEKLGFVGR REGIAAIATA TVIYPGEVPE 

« Hide

References

[1]"Completion of the genome sequence of Brucella abortus and comparison to the highly similar genomes of Brucella melitensis and Brucella suis."
Halling S.M., Peterson-Burch B.D., Bricker B.J., Zuerner R.L., Qing Z., Li L.-L., Kapur V., Alt D.P., Olsen S.C.
J. Bacteriol. 187:2715-2726(2005) [PubMed: 15805518] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 9-941 / Biovar 1.

Cross-references

Sequence databases

AE017223 Genomic DNA. Translation: AAX74466.1.
RefSeqYP_221827.2.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3340471.
GenomeReviewsGene locus BruAb1_1126 in contig AE017223_GR.
KEGGbmb:BruAb1_1126.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ57D18.
OMAIVLIHDA.

Enzyme and pathway databases

BioCycBABO262698:BRUAB1_1126-MON.
BRENDA2.7.7.60. 575.
4.6.1.12. 575.

Family and domain databases

HAMAPMF_01520.
[Tree]
InterProIPR001228. ISPD_synthase.
IPR018294. ISPD_synthase_CS.
IPR003526. MECDP_synthase_core.
IPR020555. MECDP_synthase_CS.
[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. 1 hit.
PS01350. ISPF. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameISPDF_BRUAB
AccessionPrimary (citable) accession number: Q57D18
Entry history
Integrated into UniProtKB/Swiss-Prot: August 30, 2005
Last sequence update: May 10, 2005
Last modified: November 3, 2009
This is version 25 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

Brucella abortus strain 9-941

Brucella abortus (strain 9-941): entries and gene names

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