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Q8KA55 (RIBB_BUCAP) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 54. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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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:BUsg_056
OrganismBuchnera aphidicola subsp. Schizaphis graminum (strain Sg) [Complete proteome] [HAMAP]
Taxonomic identifier198804 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeBuchnera

Protein attributes

Sequence length213 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 – 2132133,4-dihydroxy-2-butanone 4-phosphate synthase HAMAP MF_00180
PRO_0000151792

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
Q8KA55 [UniParc].

Last modified October 1, 2002. Version 1.
Checksum: 0A867A837CAA7A0D

FASTA21323,278
        10         20         30         40         50         60 
MNQTLLSEFG NPIERVKKAI SALQLGEGII ILDDEKRENE GDLVFSSETM TVEQMALTIR 

        70         80         90        100        110        120 
YGSGIVCLCI TESKRKKLNL PMMVKHNTST YRTGFTVTIE ASKGVSTGVS AKDRLTTIKT 

       130        140        150        160        170        180 
ATADDAQPSD LNRPGHVFPL RANGGGILAR AGHTEAAIEI VSLAGFKPYG VICELTNKDG 

       190        200        210 
SMSRTPEIIK FSKSKKMKIL TIKDLILYVQ NKK 

« Hide

References

[1]"50 million years of genomic stasis in endosymbiotic bacteria."
Tamas I., Klasson L., Canbaeck B., Naeslund A.K., Eriksson A.-S., Wernegreen J.J., Sandstroem J.P., Moran N.A., Andersson S.G.E.
Science 296:2376-2379(2002) [PubMed: 12089438] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: Sg.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE013218 Genomic DNA. Translation: AAM67627.1.
RefSeqNP_660416.1. NC_004061.1.

3D structure databases

ProteinModelPortalQ8KA55.
SMRQ8KA55. Positions 1-210.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaEBBUCT00000000258; EBBUCP00000000258; EBBUCG00000000258.
GeneID1005872.
GenomeReviewsGene locus BUsg_056 in contig AE013218_GR.
KEGGbas:BUsg056.
PATRIC21246877. VBIBucAph100086_0056.

Organism-specific databases

CMRSearch...

Phylogenomic databases

GeneTreeEBGT00050000007959.
HOGENOMHBG735778.
OMAGDMIFAA.
ProtClustDBPRK03353.

Enzyme and pathway databases

BioCycBAPH198804:BUSG056-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_BUCAP
AccessionPrimary (citable) accession number: Q8KA55
Entry history
Integrated into UniProtKB/Swiss-Prot: November 8, 2002
Last sequence update: October 1, 2002
Last modified: January 25, 2012
This is version 54 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Buchnera aphidicola (subsp. Schizaphis graminum)

Buchnera aphidicola (subsp. Schizaphis graminum): entries and gene names

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families