Skip Header

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

Q7NQC4 (RIBB_CHRVO) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 54. 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
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:CV_4216
OrganismChromobacterium violaceum [Complete proteome] [HAMAP]
Taxonomic identifier536 [NCBI]
Taxonomic lineageBacteria › Proteobacteria › Betaproteobacteria › Neisseriales › Neisseriaceae › Chromobacterium

Protein attributes

Sequence length210 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 – 2102103,4-dihydroxy-2-butanone 4-phosphate synthase HAMAP MF_00180
PRO_0000151795

Regions

Region33 – 342Substrate binding By similarity
Region146 – 1505Substrate binding By similarity

Sites

Metal binding341Magnesium or manganese 1 By similarity
Metal binding341Magnesium or manganese 2 By similarity
Metal binding1491Magnesium or manganese 2 By similarity
Binding site381Substrate By similarity
Binding site1701Substrate By similarity
Site1321Essential for catalytic activity By similarity
Site1701Essential for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q7NQC4 [UniParc].

Last modified December 15, 2003. Version 1.
Checksum: 7CDF2DC4F10708E7

FASTA21022,524
        10         20         30         40         50         60 
MNANTDILSL RVHAALDALR RGLPVIVADD ADRENEADLI LAADTLTVPE MARMIRDGSG 

        70         80         90        100        110        120 
IVCLCLTPER AERLQLPPMA AENGSRYGTA FTVAIEAAQG VTTGVSAADR TTTIRAAIHP 

       130        140        150        160        170        180 
DAKPGDLVRP GHVYPIVARA GGVRERRGHT EASVELARLA GFSPAGVLCE LMNPDGTMMR 

       190        200        210 
GQQVQDYAER HDLPQLSVAE LAEWLQREPA

« Hide

References

[1]"The complete genome sequence of Chromobacterium violaceum reveals remarkable and exploitable bacterial adaptability."
Vasconcelos A.T.R., de Almeida D.F., Hungria M., Guimaraes C.T., Antonio R.V., Almeida F.C., de Almeida L.G.P., de Almeida R., Alves-Gomes J.A., Andrade E.M., Araripe J., de Araujo M.F.F., Astolfi-Filho S., Azevedo V., Baptista A.J., Bataus L.A.M., Batista J.S., Belo A. expand/collapse author list , van den Berg C., Bogo M., Bonatto S., Bordignon J., Brigido M.M., Brito C.A., Brocchi M., Burity H.A., Camargo A.A., Cardoso D.D.P., Carneiro N.P., Carraro D.M., Carvalho C.M.B., Cascardo J.C.M., Cavada B.S., Chueire L.M.O., Creczynski-Pasa T.B., Cunha-Junior N.C., Fagundes N., Falcao C.L., Fantinatti F., Farias I.P., Felipe M.S.S., Ferrari L.P., Ferro J.A., Ferro M.I.T., Franco G.R., Freitas N.S.A., Furlan L.R., Gazzinelli R.T., Gomes E.A., Goncalves P.R., Grangeiro T.B., Grattapaglia D., Grisard E.C., Hanna E.S., Jardim S.N., Laurino J., Leoi L.C.T., Lima L.F.A., Loureiro M.F., Lyra M.C.C.P., Madeira H.M.F., Manfio G.P., Maranhao A.Q., Martins W.S., di Mauro S.M.Z., de Medeiros S.R.B., Meissner R.V., Moreira M.A.M., Nascimento F.F., Nicolas M.F., Oliveira J.G., Oliveira S.C., Paixao R.F.C., Parente J.A., Pedrosa F.O., Pena S.D.J., Pereira J.O., Pereira M., Pinto L.S.R.C., Pinto L.S., Porto J.I.R., Potrich D.P., Ramalho-Neto C.E., Reis A.M.M., Rigo L.U., Rondinelli E., Santos E.B.P., Santos F.R., Schneider M.P.C., Seuanez H.N., Silva A.M.R., da Silva A.L.C., Silva D.W., Silva R., Simoes I.C., Simon D., Soares C.M.A., Soares R.B.A., Souza E.M., Souza K.R.L., Souza R.C., Steffens M.B.R., Steindel M., Teixeira S.R., Urmenyi T., Vettore A., Wassem R., Zaha A., Simpson A.J.G.
Proc. Natl. Acad. Sci. U.S.A. 100:11660-11665(2003) [PubMed: 14500782] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 12472 / DSM 30191 / JCM 1249 / NBRC 12614 / NCIMB 9131 / NCTC 9757.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AE016825 Genomic DNA. Translation: AAQ61876.1.
RefSeqNP_903886.1. NC_005085.1.

3D structure databases

ProteinModelPortalQ7NQC4.
SMRQ7NQC4. Positions 10-207.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID2549626.
GenomeReviewsGene locus CV_4216 in contig AE016825_GR.
KEGGcvi:CV_4216.
NMPDRfig|243365.1.peg.4216.
PATRIC21443277. VBIChrVio67196_4133.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHBG735778.
OMAGDMIFAA.
PhylomeDBQ7NQC4.

Enzyme and pathway databases

BioCycCVIO243365:CV_4216-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_CHRVO
AccessionPrimary (citable) accession number: Q7NQC4
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: December 15, 2003
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

PATHWAY comments

Index of metabolic and biosynthesis pathways

SIMILARITY comments

Index of protein domains and families

to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·Documents