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Reviewed, UniProtKB/Swiss-Prot Q1QM99 (ISPDF_NITHX)

Last modified February 9, 2010. Version 23. 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: Nham_1834
OrganismNitrobacter hamburgensis (strain X14 / DSM 10229) [Complete proteome] [HAMAP]
Taxonomic identifier323097 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeNitrobacter

Protein attributes

Sequence length403 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 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. HAMAP MF_01520

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. HAMAP MF_01520

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 – 403403Bifunctional enzyme ispD/ispF HAMAP MF_01520
PRO_0000292856

Regions

Region1 – 2342342-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
Region235 – 4031692-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520

Sites

Metal binding2411Divalent metal cation By similarity
Metal binding2431Divalent metal cation By similarity
Metal binding2751Divalent metal cation By similarity
Site191Transition state stabilizer By similarity
Site261Transition state stabilizer By similarity
Site1561Positions MEP for the nucleophilic attack By similarity
Site2131Positions MEP for the nucleophilic attack By similarity
Site2671Transition state stabilizer By similarity
Site3661Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1QM99-1 [UniParc].

Last modified June 26, 2007. Version 2.
Checksum: C18698298DDC8335

FASTA40342,798
        10         20         30         40         50         60 
MPTSKRTAAI IVAAGRGLRA GTGGPKQYRT IAGRTVIARA MEAFCDHPDV FAVQPVLNPD 

        70         80         90        100        110        120 
DLAMFNQAVA GFRYRPPANG GATRQASVHA GLEALAADAP DIVLIHDAAR PFATPALIRR 

       130        140        150        160        170        180 
AIEATDITGA AVPVIPVTDT IKQVDASGAV NATPDRAKLR IAQTPQAFRF DVILDAHRRA 

       190        200        210        220        230        240 
ARDGRDDFTD DAALAEWVGL TVATFEGDAA NMKLTTPEDF VREEARLAAM LGDIRTGTGY 

       250        260        270        280        290        300 
DVHAFGDGDH VMLCGVKVPH NRGFLAHSDG DVGLHALVDA ILGALADGDI GSHFPPSDPQ 

       310        320        330        340        350        360 
WKGAASDKFL KYAVDRVAAR GGRIANLEVT MICERPKIGP LRDTMRARIA EITGVAISRI 

       370        380        390        400 
AVKATTSERL GFTGREEGIA TTASATVRLP WNDSDQEDKG WST 

« Hide

References

[1]"Complete sequence of chromosome of Nitrobacter hamburgensis X14."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M. expand/collapse author list , Hauser L., Kyrpides N., Ivanova N., Ward B., Arp D., Klotz M., Stein L., O'Mullan G., Starkenburg S., Sayavedra L., Poret-Peterson A.T., Gentry M.E., Bruce D., Richardson P.
Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000319 Genomic DNA. Translation: ABE62648.1. Different initiation.
RefSeqYP_577108.1.

3D structure databases

SMRQ1QM99. Positions 6-391.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1QM99.

Genome annotation databases

GeneID4033011.
GenomeReviewsGene locus Nham_1834 in contig CP000319_GR.
KEGGnha:Nham_1834.
NMPDRfig|323097.3.peg.3209.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1211.
HOGENOMHBG672839.

Enzyme and pathway databases

BioCycNHAM323097:NHAM_1834-MONOMER.

Family and domain databases

HAMAPMF_01520. IspDF.
[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. 1 hit.
PS01350. ISPF. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameISPDF_NITHX
AccessionPrimary (citable) accession number: Q1QM99
Entry history
Integrated into UniProtKB/Swiss-Prot: June 26, 2007
Last sequence update: June 26, 2007
Last modified: February 9, 2010
This is version 23 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