Skip Header

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

Q1R6T4 (RIBB_ECOUT) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
3,4-dihydroxy-2-butanone 4-phosphate synthase

Short name=DHBP synthase
EC=4.1.99.12
Gene names
Name:ribB
Ordered Locus Names:UTI89_C3483
OrganismEscherichia coli (strain UTI89 / UPEC) [Complete proteome] [HAMAP]
Taxonomic identifier364106 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia

Protein attributes

Sequence length217 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the conversion of D-ribulose 5-phosphate to formate and 3,4-dihydroxy-2-butanone 4-phosphate By similarity. HAMAP MF_00180

Catalytic activity

D-ribulose 5-phosphate = formate + L-3,4-dihydroxybutan-2-one 4-phosphate. HAMAP MF_00180

Cofactor

Binds 2 divalent metal cations per subunit. Magnesium or manganese By similarity.

Pathway

Cofactor biosynthesis; riboflavin biosynthesis; 2-hydroxy-3-oxobutyl phosphate from D-ribulose 5-phosphate: step 1/1. HAMAP MF_00180

Subunit structure

Homodimer By similarity. HAMAP MF_00180

Sequence similarities

Belongs to the DHBP synthase family.

Ontologies

Keywords
   Biological processRiboflavin biosynthesis
   LigandMagnesium
Manganese
Metal-binding
   Molecular functionLyase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processriboflavin biosynthetic process

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular function3,4-dihydroxy-2-butanone-4-phosphate synthase activity

Inferred from electronic annotation. Source: EC

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 – 2172173,4-dihydroxy-2-butanone 4-phosphate synthase HAMAP MF_00180
PRO_1000040607

Regions

Region37 – 382Substrate binding By similarity
Region150 – 1545Substrate binding By similarity

Sites

Metal binding381Magnesium or manganese 1 By similarity
Metal binding381Magnesium or manganese 2 By similarity
Metal binding1531Magnesium or manganese 2 By similarity
Binding site421Substrate By similarity
Binding site1741Substrate By similarity
Site1361Essential for catalytic activity By similarity
Site1741Essential for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q1R6T4 [UniParc].

Last modified May 16, 2006. Version 1.
Checksum: C8220A407A342609

FASTA21723,339
        10         20         30         40         50         60 
MNQTLLSSFG TPFERVENAL AALREGRGVM VLDDEDRENE GDMIFPAETM TVEQMALTIR 

        70         80         90        100        110        120 
HGSGIVCLCI TDDRRKQLDL PMMVENNTSA YGTGFTVTIE AAEGVTTGVS AADRITTVRA 

       130        140        150        160        170        180 
AIADGAKPSD LNRPGHVFPL RAQAGGVLTR GGHTEATIDL MTLAGFKPAG VLCELTNDDG 

       190        200        210 
TMARAPECIE FANKHNMALV TIEDLVAYRQ AHERKAS 

« Hide

References

[1]"Identification of genes subject to positive selection in uropathogenic strains of Escherichia coli: a comparative genomics approach."
Chen S.L., Hung C.-S., Xu J., Reigstad C.S., Magrini V., Sabo A., Blasiar D., Bieri T., Meyer R.R., Ozersky P., Armstrong J.R., Fulton R.S., Latreille J.P., Spieth J., Hooton T.M., Mardis E.R., Hultgren S.J., Gordon J.I.
Proc. Natl. Acad. Sci. U.S.A. 103:5977-5982(2006) [PubMed: 16585510] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: UTI89 / UPEC.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000243 Genomic DNA. Translation: ABE08930.1.
RefSeqYP_542461.1. NC_007946.1.

3D structure databases

ProteinModelPortalQ1R6T4.
SMRQ1R6T4. Positions 1-217.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ1R6T4.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBESCT00000068642; EBESCP00000066120; EBESCG00000067689.
GeneID3993889.
GenomeReviewsGene locus UTI89_C3483 in contig CP000243_GR.
KEGGeci:UTI89_C3483.
PATRIC18456466. VBIEscCol42261_3450.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0108.
GeneTreeEBGT00050000011873.
HOGENOMHBG735778.
OMAGDMIFAA.
ProtClustDBPRK03353.

Enzyme and pathway databases

BioCycECOL364106:UTI89_C3483-MONOMER.

Family and domain databases

HAMAPMF_00180. RibB.
[Tree]
InterProIPR017945. DHBP_synth_RibB-like_a/b_dom.
IPR000422. DHBP_synthase_RibB.
[Graphical view]
Gene3DG3DSA:3.90.870.10. DHBP_synth_RibB-like_a/b_dom. 1 hit.
KOK02858.
PfamPF00926. DHBP_synthase. 1 hit.
[Graphical view]
SUPFAMSSF55821. DHBP_synth_RibB-like_a/b_dom. 1 hit.
TIGRFAMsTIGR00506. RibB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRIBB_ECOUT
AccessionPrimary (citable) accession number: Q1R6T4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: May 16, 2006
Last modified: January 25, 2012
This is version 39 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