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Reviewed, UniProtKB/Swiss-Prot Q1R6T4 (RIBB_ECOUT)

Last modified June 16, 2009. Version 21. 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:
    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.
Sequence processingThe displayed sequence is not processed.
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.

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; 3,4-dihydroxy-2-butanone 4-phosphate from D-ribulose 5-phosphate: step 1/1. HAMAP MF_00180

Subunit structure

Homodimer By similarity.

Sequence similarities

Belongs to the DHBP synthase family.

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
Q1R6T4-1 [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].

Cross-references

Sequence databases

CP000243 Genomic DNA. Translation: ABE08930.1.
RefSeqYP_542461.1.

3D structure databases

SMRQ1R6T4. Positions 4-217.
ModBaseSearch...

Genome annotation databases

GeneID3993889.
GenomeReviewsGene locus UTI89_C3483 in contig CP000243_GR.
KEGGeci:UTI89_C3483.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMQ1R6T4.
OMAQ1R6T4. YGSGIVC.

Enzyme and pathway databases

BioCycECOL364106:UTI89_C3483-MON.

Family and domain databases

HAMAPMF_00180.
[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.
PfamPF00926. DHBP_synthase. 1 hit.
[Graphical view]
ProDomPD003034. DHBP_synthase. 1 hit.
[Graphical view] [Entries sharing at least one domain]
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: June 16, 2009
This is version 21 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