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Reviewed, UniProtKB/Swiss-Prot P44815 (ISPF_HAEIN)

Last modified June 16, 2009. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
    2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase
      Short name=MECPS
      Short name=MECDP-synthase
    EC=4.6.1.12
Gene names
Name: ispF
Ordered Locus Names: HI0671
OrganismHaemophilus influenzae [Complete proteome] [HAMAP]
Taxonomic identifier727 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length158 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Converts 4-diphosphocytidyl-2-C-methyl-D-erythritol 2-phosphate into 2-C-methyl-D-erythritol 2,4-cyclodiphosphate (MECDP) and CMP By similarity.

Catalytic activity

2-phospho-4-(cytidine 5'-diphospho)-2-C-methyl-D-erythritol = 2-C-methyl-D-erythritol 2,4-cyclodiphosphate + CMP. HAMAP MF_00107

Cofactor

Binds 1 divalent metal cation per subunit. HAMAP MF_00107

Pathway

Isoprenoid biosynthesis; isopentenyl-PP biosynthesis via DXP pathway; isopentenyl-PP from 1-deoxy-D-xylulose 5-phosphate: step 4/6. HAMAP MF_00107

Subunit structure

Homotrimer. HAMAP MF_00107

Sequence similarities

Belongs to the ispF family.

Ontologies

Keywords
   Biological processIsoprene biosynthesis
   LigandMetal-binding
   Molecular functionLyase
   Technical term3D-structure
Complete proteome
Gene Ontology (GO)
   Biological processterpenoid biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Molecular function2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase activity

Inferred from electronic annotation. Source: HAMAP

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 1581582-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase HAMAP MF_00107
PRO_0000189472

Sites

Metal binding91Divalent metal cation HAMAP MF_00107
Metal binding111Divalent metal cation HAMAP MF_00107
Metal binding431Divalent metal cation HAMAP MF_00107
Site351Transition state stabilizer By similarity
Site1341Transition state stabilizer By similarity

Secondary structure

........................ 158
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P44815-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: DC34BF347DEC2EFF

FASTA15817,194
        10         20         30         40         50         60 
MIRIGHGFDV HAFGEDRPLI IGGVEVPYHT GFIAHSDGDV ALHALTDAIL GAAALGDIGK 

        70         80         90        100        110        120 
LFPDTDMQYK NADSRGLLRE AFRQVQEKGY KIGNVDITII AQAPKMRPHI DAMRAKIAED 

       130        140        150 
LQCDIEQVNV KATTTEKLGF TGRQEGIACE AVALLIRQ 

« Hide

References

« Hide 'large scale' references
[1]"Whole-genome random sequencing and assembly of Haemophilus influenzae Rd."
Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. expand/collapse author list , Glodek A., Kelley J.M., Weidman J.F., Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R., Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D., Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A., Small K.V., Fraser C.M., Smith H.O., Venter J.C.
Science 269:496-512(1995) [PubMed: 7542800] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51907 / DSM 11121 / KW20 / Rd.
[2]"Reference map of the low molecular mass proteins of Haemophilus influenzae."
Fountoulakis M., Juranville J.-F., Roeder D., Evers S., Berndt P., Langen H.
Electrophoresis 19:1819-1827(1998) [PubMed: 9719565] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
[3]"Structure of 2C-methyl-D-erythrol-2,4-cyclodiphosphate synthase from Haemophilus influenzae: activation by conformational transition."
Lehmann C., Lim K., Toedt J., Krajewski W., Howard A., Eisenstein E., Herzberg O.
Proteins 49:135-138(2002) [PubMed: 12211023] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).

Cross-references

Sequence databases

L42023 Genomic DNA. Translation: AAC22331.1.
PIRF64156.
RefSeqNP_438831.1.

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1JN1X-ray2.90A/B/C1-158[»]
1VH8X-ray2.35A/B/C/D/E/F2-158[»]
1VHAX-ray2.35A/B/C/D/E/F2-158[»]
ModBaseSearch...

Genome annotation databases

GeneID950633.
GenomeReviewsGene locus HI0671 in contig L42023_GR.
KEGGhin:HI0671.
NMPDRfig|71421.1.peg.641.
TIGRHI0671.

Phylogenomic databases

HOGENOMP44815.
OMAP44815. HAICDAL.

Enzyme and pathway databases

BioCycHINF71421:HI_0671-MON.
BRENDA4.6.1.12. 109.

Family and domain databases

HAMAPMF_00107.
[Tree]
InterProIPR003526. MECDP_synthase_core.
[Graphical view]
Gene3DG3DSA:3.30.1330.50. MECDP_synthase_core. 1 hit.
PfamPF02542. YgbB. 1 hit.
[Graphical view]
TIGRFAMsTIGR00151. ispF. 1 hit.
PROSITEPS01350. ISPF. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameISPF_HAEIN
AccessionPrimary (citable) accession number: P44815
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 16, 2009
This is version 71 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

Haemophilus influenzae

Haemophilus influenzae (strain Rd): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

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