Skip Header

 
Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot A8IBL6 (ISPDF_AZOC5)

Last modified November 3, 2009. Version 13. 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: AZC_3089
OrganismAzorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / ORS 571) [Complete proteome] [HAMAP]
Taxonomic identifier438753 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesXanthobacteraceaeAzorhizobium

Protein attributes

Sequence length391 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 – 391391Bifunctional enzyme ispD/ispF HAMAP MF_01520
PRO_1000073538

Regions

Region1 – 2302302-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
Region231 – 3911612-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520

Sites

Metal binding2371Divalent metal cation By similarity
Metal binding2391Divalent metal cation By similarity
Metal binding2711Divalent metal cation By similarity
Site151Transition state stabilizer By similarity
Site221Transition state stabilizer By similarity
Site1531Positions MEP for the nucleophilic attack By similarity
Site2101Positions MEP for the nucleophilic attack By similarity
Site2631Transition state stabilizer By similarity
Site3621Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
A8IBL6-1 [UniParc].

Last modified December 4, 2007. Version 1.
Checksum: 5EBE02911016E0E3

FASTA39140,845
        10         20         30         40         50         60 
MACAVLIVAA GRGTRAGGAV PKQYHRLGGE SVLRRTLLRF AECAAIDVIQ VVTHPDDAPL 

        70         80         90        100        110        120 
YEQAVAGLTK VLPQVAGGAT RQQSVRAGLE ALAAYGPERV LVQDGARPFT PPEVIARAIA 

       130        140        150        160        170        180 
ALDGNTAAIP VLPVTDTIKH VDAAGHVTGT VDRAMLRAVQ TPQAFRFAEL LAAHRAAADA 

       190        200        210        220        230        240 
RVADLTDDAS VMEWAGHTVA TFAGDSENVK LTSAEDLARA ARMLADLPDV RTGTGFDVHA 

       250        260        270        280        290        300 
FGPGDHVMLG GVAIPFDRGL DGHSDADVGL HALTDAVLGA LADGDIGAHF PPSDPQWKGA 

       310        320        330        340        350        360 
TSDRFLAFAI ERVRERGGIV AHLDLTLICE APKVGPHRDA IRAEIARICD LPLGRVSVKA 

       370        380        390 
TTTEKLGFTG RREGIAAMAS ATIRLPLEIG A 

« Hide

References

[1]"Complete genome sequence of the nitrogen-fixing bacterium Azorhizobium caulinodans ORS571."
Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T., Kaneko T., Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B., Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M., Oyaizu H.
Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases

AP009384 Genomic DNA. Translation: BAF89087.1.
RefSeqYP_001526005.1.

3D structure databases

ModBaseSearch...

Genome annotation databases

GeneID5688538.
GenomeReviewsGene locus AZC_3089 in contig AP009384_GR.
KEGGazc:AZC_3089.

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]
PfamPF01128. IspD. 1 hit.
PF02542. YgbB. 1 hit.
[Graphical view]
TIGRFAMsTIGR00453. ispD. 1 hit.
TIGR00151. ispF. 1 hit.
PROSITEPS01295. ISPD. False negative.
PS01350. ISPF. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameISPDF_AZOC5
AccessionPrimary (citable) accession number: A8IBL6
Entry history
Integrated into UniProtKB/Swiss-Prot: February 26, 2008
Last sequence update: December 4, 2007
Last modified: November 3, 2009
This is version 13 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