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Q4QMD5 (RIBB_HAEI8) Reviewed, UniProtKB/Swiss-Prot

Last modified January 25, 2012. Version 40. 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:NTHI0925
OrganismHaemophilus influenzae (strain 86-028NP) [Complete proteome] [HAMAP]
Taxonomic identifier281310 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPasteurellalesPasteurellaceaeHaemophilus

Protein attributes

Sequence length215 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 – 2152153,4-dihydroxy-2-butanone 4-phosphate synthase HAMAP MF_00180
PRO_1000040610

Regions

Region38 – 392Substrate binding By similarity
Region151 – 1555Substrate binding By similarity

Sites

Metal binding391Magnesium or manganese 1 By similarity
Metal binding391Magnesium or manganese 2 By similarity
Metal binding1541Magnesium or manganese 2 By similarity
Binding site431Substrate By similarity
Binding site1751Substrate By similarity
Site1371Essential for catalytic activity By similarity
Site1751Essential for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
Q4QMD5 [UniParc].

Last modified July 19, 2005. Version 1.
Checksum: D64A5C8BD9FBAF2A

FASTA21523,281
        10         20         30         40         50         60 
MNQSILSPFG NTAEERVLNA INAFKHGTGV LVLDDEDREN EGDLIFPAET ITSEQMAKLI 

        70         80         90        100        110        120 
RYGSGIVCLC ITDERCQQLD LPPMVEHNNS VNKTAFTVTI EAAKGVSTGV SAADRVTTIQ 

       130        140        150        160        170        180 
TAIADNAVPT DLHRPGHVFP LRAANGGVLT RRGHTEASVD LARLAGFKEA GVICEITNDD 

       190        200        210 
GTMARTPEIV EFAKKFGYSV LTIEDLVEYR LAHNI 

« Hide

References

[1]"Genomic sequence of an otitis media isolate of nontypeable Haemophilus influenzae: comparative study with H. influenzae serotype d, strain KW20."
Harrison A., Dyer D.W., Gillaspy A., Ray W.C., Mungur R., Carson M.B., Zhong H., Gipson J., Gipson M., Johnson L.S., Lewis L., Bakaletz L.O., Munson R.S. Jr.
J. Bacteriol. 187:4627-4636(2005) [PubMed: 15968074] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: 86-028NP.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000057 Genomic DNA. Translation: AAX87812.1.
RefSeqYP_248472.1. NC_007146.2.

3D structure databases

HSSPHSSP built from PDB template 1G58 based on UniProtKB P0A7J0.
ProteinModelPortalQ4QMD5.
SMRQ4QMD5. Positions 1-213.
ModBaseSearch...

Protein-protein interaction databases

STRINGQ4QMD5.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID3430234.
GenomeReviewsGene locus NTHI0925 in contig CP000057_GR.
KEGGhit:NTHI0925.
PATRIC20182027. VBIHaeInf100748_0858.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0108.
HOGENOMHBG735778.
OMAGDMIFAA.
PhylomeDBQ4QMD5.
ProtClustDBPRK01792.

Enzyme and pathway databases

BioCycHINF281310:NTHI0925-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_HAEI8
AccessionPrimary (citable) accession number: Q4QMD5
Entry history
Integrated into UniProtKB/Swiss-Prot: January 15, 2008
Last sequence update: July 19, 2005
Last modified: January 25, 2012
This is version 40 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