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Q8YHD8 (ISPDF_BRUME) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 84. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Bifunctional enzyme IspD/IspF

Including the following 2 domains:

  1. 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. 2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
    Short name=MECDP-synthase
    Short name=MECPP-synthase
    Short name=MECPS
    EC=4.6.1.12
Gene names
Name:ispDF
Ordered Locus Names:BMEI0863
OrganismBrucella melitensis biotype 1 (strain 16M / ATCC 23456 / NCTC 10094) [Complete proteome] [HAMAP]
Taxonomic identifier224914 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBrucellaceaeBrucella

Protein attributes

Sequence length390 AA.
Sequence statusComplete.
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 catalyzes the conversion of 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate (CDP-ME2P) to 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (ME-CPP) with a corresponding release of cytidine 5-monophosphate (CMP) (IspF) By similarity. HAMAP-Rule MF_01520

Catalytic activity

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

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

Cofactor

Divalent metal cations By similarity. HAMAP-Rule MF_01520

Pathway

Isoprenoid biosynthesis; isopentenyl diphosphate biosynthesis via DXP pathway; isopentenyl diphosphate from 1-deoxy-D-xylulose 5-phosphate: step 2/6. HAMAP-Rule 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-Rule MF_01520
PRO_0000075660

Regions

Region1 – 2292292-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP-Rule MF_01520
Region230 – 3901612-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP-Rule MF_01520
Region236 – 2383Substrate binding By similarity
Region262 – 2632Substrate binding By similarity
Region266 – 2749Substrate binding By similarity
Region284 – 2863Substrate binding By similarity
Region359 – 3635Substrate binding By similarity

Sites

Metal binding2361Divalent metal cation By similarity
Metal binding2381Divalent metal cation By similarity
Metal binding2701Divalent metal cation By similarity
Binding site2931Substrate; via carbonyl oxygen By similarity
Binding site3671Substrate; via carbonyl oxygen By similarity
Binding site3701Substrate 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
Q8YHD8 [UniParc].

Last modified March 1, 2002. 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 

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE008917 Genomic DNA. Translation: AAL52044.1.
PIRAI3359.

3D structure databases

ProteinModelPortalQ8YHD8.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING224914.BMEI0863.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAL52044; AAL52044; BMEI0863.
PATRIC17851934. VBIBruMel92729_0970.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000252034.
OMACGAGDIG.
OrthoDBEOG6J48RZ.
ProtClustDBPRK09382.

Enzyme and pathway databases

BioCycBMEL224914:GCJ0-890-MONOMER.
UniPathwayUPA00056; UER00093.
UPA00056; UER00095.

Family and domain databases

Gene3D3.30.1330.50. 1 hit.
HAMAPMF_00107. IspF.
MF_00108. IspD.
MF_01520. IspDF.
InterProIPR001228. IspD.
IPR026596. IspD/F.
IPR018294. ISPD_synthase_CS.
IPR003526. MECDP_synthase.
IPR020555. MECDP_synthase_CS.
[Graphical view]
PfamPF01128. IspD. 1 hit.
PF02542. YgbB. 1 hit.
[Graphical view]
SUPFAMSSF69765. SSF69765. 1 hit.
TIGRFAMsTIGR00453. ispD. 1 hit.
TIGR00151. ispF. 1 hit.
PROSITEPS01295. ISPD. 1 hit.
PS01350. ISPF. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameISPDF_BRUME
AccessionPrimary (citable) accession number: Q8YHD8
Entry history
Integrated into UniProtKB/Swiss-Prot: June 6, 2002
Last sequence update: March 1, 2002
Last modified: February 19, 2014
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PATHWAY comments

Index of metabolic and biosynthesis pathways

Brucella melitensis

Brucella melitensis (strain 16M): entries and gene names