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Reviewed, UniProtKB/Swiss-Prot A8ER37 (ISPDF_ARCB4)

Last modified November 3, 2009. Version 15. 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: Abu_0126
OrganismArcobacter butzleri (strain RM4018) [Complete proteome] [HAMAP]
Taxonomic identifier367737 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeArcobacter

Protein attributes

Sequence length374 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 – 374374Bifunctional enzyme ispD/ispF HAMAP MF_01520
PRO_1000068624

Regions

Region1 – 2132132-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
Region214 – 3741612-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520

Sites

Metal binding2201Divalent metal cation By similarity
Metal binding2221Divalent metal cation By similarity
Metal binding2541Divalent metal cation By similarity
Site161Transition state stabilizer By similarity
Site231Transition state stabilizer By similarity
Site1411Positions MEP for the nucleophilic attack By similarity
Site1931Positions MEP for the nucleophilic attack By similarity
Site2461Transition state stabilizer By similarity
Site3451Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
A8ER37-1 [UniParc].

Last modified November 13, 2007. Version 1.
Checksum: 2F2D9827E7597246

FASTA37441,907
        10         20         30         40         50         60 
MLDVTLIVLC AGNSTRFEHK TKKQWIRVED EPLWLNVTKR ISSFAKFDKI IVTSHQDELN 

        70         80         90        100        110        120 
YMKNFSDDFT FVKGGETRQL SILNSLQFVT TKYVMITDVA RACVPQSVIE NLLNEKSSAD 

       130        140        150        160        170        180 
CIVPILNVTD TVVYENDTID RSNVKLIQTP QLSSTQVLRD ALNTPIEFTD ESSAIKAIDG 

       190        200        210        220        230        240 
KIKYIQGSTF SKKLTLGDEL DELPCLKAPS NNFFTGTGFD IHAFEEIKDM YLGGVKLPYE 

       250        260        270        280        290        300 
YGFKAHSDGD VLIHSVIDAL LGACGAGDIG EFFPDTDDKY KGIDSKLLLG QIVNFINNVG 

       310        320        330        340        350        360 
YEIVNVDLTI IAQKPKINPF KDEIKKSMAK LLRIEKQFVN VKATTAEKLG FIGRAEGVAV 

       370 
QSIATLKYYN WKKR 

« Hide

References

[1]"The complete genome sequence and analysis of the Epsilonproteobacterium Arcobacter butzleri."
Miller W.G., Parker C.T., Rubenfield M., Mendz G.L., Woesten M.M.S.M., Ussery D.W., Stolz J.F., Binnewies T.T., Hallin P.F., Wang G., Malek J.A., Rogosin A., Stanker L.H., Mandrell R.E.
PLoS ONE 2:E1358-E1358(2007) [PubMed: 18159241] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

CP000361 Genomic DNA. Translation: ABV66411.1.
RefSeqYP_001489080.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGA8ER37.

Genome annotation databases

GeneID5624435.
GenomeReviewsGene locus Abu_0126 in contig CP000361_GR.
KEGGabu:Abu_0126.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMAIVLIHDA.

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]
TIGRFAMsTIGR00151. ispF. 1 hit.
PROSITEPS01295. ISPD. False negative.
PS01350. ISPF. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameISPDF_ARCB4
AccessionPrimary (citable) accession number: A8ER37
Entry history
Integrated into UniProtKB/Swiss-Prot: February 5, 2008
Last sequence update: November 13, 2007
Last modified: November 3, 2009
This is version 15 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