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A6X0N1 (ISPDF_OCHA4) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 35. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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=MECPS
    EC=4.6.1.12
Gene names
Name:ispDF
Ordered Locus Names:Oant_2069
OrganismOchrobactrum anthropi (strain ATCC 49188 / DSM 6882 / NCTC 12168) [Complete proteome] [HAMAP]
Taxonomic identifier439375 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Alphaproteobacteria › Rhizobiales › Brucellaceae › Ochrobactrum

Protein attributes

Sequence length407 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 – 407407Bifunctional enzyme IspD/IspF HAMAP MF_01520
PRO_0000315554

Regions

Region1 – 2462462-C-methyl-D-erythritol 4-phosphate cytidylyltransferase HAMAP MF_01520
Region247 – 4071612-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_01520

Sites

Metal binding2531Divalent metal cation By similarity
Metal binding2551Divalent metal cation By similarity
Metal binding2871Divalent metal cation By similarity
Site251Transition state stabilizer By similarity
Site341Transition state stabilizer By similarity
Site1651Positions MEP for the nucleophilic attack By similarity
Site2221Positions MEP for the nucleophilic attack By similarity
Site2791Transition state stabilizer By similarity
Site3781Transition state stabilizer By similarity

Sequences

Sequence LengthMass (Da)Tools
A6X0N1 [UniParc].

Last modified August 21, 2007. Version 1.
Checksum: B681EE7DBDFD3E5F

FASTA40743,721
        10         20         30         40         50         60 
MQPLAEATTI SKIAAVIVAA GRGERAGQSI EGPKQYRRIG GEAVLARTLR AFIDCPLVDS 

        70         80         90        100        110        120 
IVVVIHPDDH VLYERALQEN CDTILVVNGG ATRQESTRLG LLALRDYAPQ YVMIHDGVRP 

       130        140        150        160        170        180 
FVSQDLLKRI VENLAPDEGV LPALAVSDTL KQSATDGTVK TTVPRVGLFA AQTPQAFPYT 

       190        200        210        220        230        240 
PILDAHEKAF AISRSDFTDD AAIAEWQSIA VRIIEGSADN TKLTWAKDIE MADKRLRQDH 

       250        260        270        280        290        300 
VSFPDIRTGN GYDVHSFEPG DHVTLCGVKI PHEAKLNGHS DADVGLHALT DALLATRGAG 

       310        320        330        340        350        360 
DIGTHFPPSD PQWKGAASRI FIEHAANIVR EAGGRIANVD VTFISEAPKI GPHRAAMTEA 

       370        380        390        400 
LCDMLGIAAD RVSIKATTNE KLGFVGRREG IAAIATATVI YPGEVPE

« Hide

References

[1]"Complete sequence of chromosome 1 of Ochrobactrum anthropi ATCC 49188."
Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E., Tice H., Pitluck S., Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Garcia E., Richardson P.
Submitted (JUL-2007) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 49188 / DSM 6882 / NCTC 12168.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CP000758 Genomic DNA. Translation: ABS14785.1.
RefSeqYP_001370614.1. NC_009667.1.

3D structure databases

ProteinModelPortalA6X0N1.
ModBaseSearch...

Protein-protein interaction databases

STRINGA6X0N1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID5379672.
GenomeReviewsGene locus Oant_2069 in contig CP000758_GR.
KEGGoan:Oant_2069.
PATRIC20469357. VBIOchAnt73124_2175.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG1211.
HOGENOMHBG672839.
OMAIVLIHDA.
ProtClustDBPRK09382.

Enzyme and pathway databases

BioCycOANT439375:OANT_2069-MONOMER.

Family and domain databases

HAMAPMF_01520. IspDF.
[Tree]
InterProIPR023423. IpsF_dom.
IPR001228. ISPD_synthase.
IPR018294. ISPD_synthase_CS.
IPR003526. MECDP_synthase.
IPR020555. MECDP_synthase_CS.
[Graphical view]
Gene3DG3DSA:3.30.1330.50. MECDP_synthase_core. 1 hit.
KOK12506.
PfamPF01128. IspD. 1 hit.
PF02542. YgbB. 1 hit.
[Graphical view]
SUPFAMSSF69765. YgbB_synth. 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_OCHA4
AccessionPrimary (citable) accession number: A6X0N1
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: August 21, 2007
Last modified: January 25, 2012
This is version 35 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

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