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Reviewed, UniProtKB/Swiss-Prot Q21YT7 (ISPDF_RHOFD)

Last modified June 16, 2009. Version 20. 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

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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: Rfer_1332
OrganismRhodoferax ferrireducens (strain DSM 15236 / ATCC BAA-621 / T118) [Complete proteome] [HAMAP]
Taxonomic identifier338969 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Burkholderiales › Comamonadaceae › Rhodoferax

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Protein attributes

Sequence length418 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceInferred from homology.

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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.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 418418Bifunctional enzyme ispD/ispF HAMAP MF_01520
PRO_0000296752

Regions

Region1 – 2612612-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
Region262 – 4181572-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520

Sites

Metal binding2681Divalent metal cation By similarity
Metal binding2701Divalent metal cation By similarity
Metal binding3021Divalent metal cation By similarity
Site291Transition state stabilizer By similarity
Site361Transition state stabilizer By similarity
Site1691Positions MEP for the nucleophilic attack By similarity
Site2221Positions MEP for the nucleophilic attack By similarity
Site2941Transition state stabilizer By similarity
Site3931Transition state stabilizer By similarity

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Sequences

Sequence LengthMass (Da)Tools
Q21YT7-1 [UniParc].

Last modified April 18, 2006. Version 1.
Checksum: D172268F7456D43F

FASTA41844,282
        10         20         30         40         50         60 
MADTPALIPQ SDTTPRCWAL IPCAGTGSRA GATGPKQYQL LAGKPMVLHT LAAFAAVPRI 

        70         80         90        100        110        120 
ARTLVVVAPD DAFFASQTLT DARFLVAACG GSTRAASVLN GLNFLLGQGA ARHDWVLVHD 

       130        140        150        160        170        180 
AARCLIRPDQ IDQLIDACWQ DDVGGLLALP LPDTLKRESL GRVAATLERA DKWLAQTPQM 

       190        200        210        220        230        240 
FRLGSLLDAL QVAGTTVTDE SSAMEAMGLS PKLVPGSAQN FKVTYPQDFC LAEAVLMTRS 

       250        260        270        280        290        300 
SGDSAPQQSA SEFKRASDMN FRIGEGWDIH ALVAGRKLLL GGVEIPYHLG LLGHSDADVL 

       310        320        330        340        350        360 
LHAITDALLG AAALGDIGTH FPDTDARFKG ADSLVLLTEA ARRVRAKGFE IGNVDSTVIA 

       370        380        390        400        410 
QAPKLMPYMA AMRAQIALAL ALEVDQVNVK AKTAEKMGPV GLGQAMEARA TVLLRKFI

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References

[1]"Complete sequence of chromosome of Rhodoferax ferrireducens DSM 15236."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Ivanova N., Richardson P.
Submitted (FEB-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

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Cross-references

Sequence databases

CP000267 Genomic DNA. Translation: ABD69066.1.
RefSeqYP_522597.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID3961363.
GenomeReviewsGene locus Rfer_1332 in contig CP000267_GR.
KEGGrfr:Rfer_1332.
NMPDRfig|338969.3.peg.2261.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ21YT7.
OMAQ21YT7. IVLIHDA.

Enzyme and pathway databases

BioCycRFER338969:RFER_1332-MON.

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. 1 hit.
PS01350. ISPF. 1 hit.
[Graphical view]
ProtoNetSearch...

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Entry information

Entry nameISPDF_RHOFD
AccessionPrimary (citable) accession number: Q21YT7
Entry history
Integrated into UniProtKB/Swiss-Prot: July 24, 2007
Last sequence update: April 18, 2006
Last modified: June 16, 2009
This is version 20 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)

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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