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Reviewed, UniProtKB/Swiss-Prot O68249 (RIBB_DEHMU)

Last modified February 9, 2010. Version 50. 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
OrganismDehalospirillum multivorans
Taxonomic identifier66821 [NCBI]
Taxonomic lineageBacteriaProteobacteriaEpsilonproteobacteriaCampylobacteralesCampylobacteraceaeSulfurospirillum

Protein attributes

Sequence length356 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. HAMAP MF_00180

Pathway

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

Sequence similarities

In the N-terminal section; belongs to the DHBP synthase family.

In the C-terminal section; belongs to the GTP cyclohydrolase II family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 3563563,4-dihydroxy-2-butanone 4-phosphate synthase HAMAP MF_00180
PRO_0000151796

Regions

Region1 – 211211DHBP synthase HAMAP MF_00180
Region38 – 392Substrate binding By similarity
Region150 – 1545Substrate binding By similarity
Region212 – 356145GTP cyclohydrolase II-like HAMAP MF_00180

Sites

Metal binding391Magnesium or manganese 1 By similarity
Metal binding391Magnesium or manganese 2 By similarity
Metal binding1531Magnesium or manganese 2 By similarity
Binding site431Substrate By similarity
Binding site1741Substrate By similarity
Site1361Essential for catalytic activity By similarity
Site1741Essential for catalytic activity By similarity

Sequences

Sequence LengthMass (Da)Tools
O68249-1 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 851685138C2F6512

FASTA35639,358
        10         20         30         40         50         60 
MNAILSDQKT FQAIIRVNQA IEDIRQGKMV VMVDDEDREN EGDLVYAASF STPQKVNFMA 

        70         80         90        100        110        120 
SHAKGLICVA ISKKIANRLQ LEPMVKKNDS SYETAFTITV DARTAATGIS AGERDMTIKI 

       130        140        150        160        170        180 
LADGGSHESE LVRPGHIFPL IAKEGGALVR IGHTEGSVDL CRLAGQGDSA VICEIMKEDG 

       190        200        210        220        230        240 
TMARRPDLDI FCAKHELNIV YISDIVEYRM MNESLIRVIA ESTTQFLGKD ARRYDFVDHN 

       250        260        270        280        290        300 
DNHHIAYAFG NIKNRSAVKF HSIMPDNELL ADTKKYNSLI QAIHYLQKSG GVLIFMDNGT 

       310        320        330        340        350 
QDMSKIREYG IGAQIIKHLG IENIELLSDS KNKEFVGISG FGLSVIKSTN VNETVA 

« Hide

References

[1]"Tetrachloroethene dehalogenase from Dehalospirillum multivorans: cloning, sequencing of the encoding genes, and expression of the pceA gene in Escherichia coli."
Neumann A., Wohlfarth G., Diekert G.
J. Bacteriol. 180:4140-4145(1998) [PubMed: 9696761] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF022812 Genomic DNA. Translation: AAC60785.1.

3D structure databases

SMRO68249. Positions 15-210, 223-349.
ModBaseSearch...

Enzyme and pathway databases

BRENDA4.1.99.12. 229899.

Family and domain databases

HAMAPMF_00180. RibB. Fused.
[Tree]
InterProIPR017945. DHBP_synth_RibB-like_a/b_dom.
IPR000422. DHBP_synthase_RibB.
IPR000926. GTP_CycHdrlase_II.
IPR016299. Riboflavin_synth_RibA.
[Graphical view]
Gene3DG3DSA:3.90.870.10. DHBP_synth_RibB-like_a/b_dom. 1 hit.
PfamPF00926. DHBP_synthase. 1 hit.
PF00925. GTP_cyclohydro2. 1 hit.
[Graphical view]
PIRSFPIRSF001259. RibA. 1 hit.
TIGRFAMsTIGR00506. ribB. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRIBB_DEHMU
AccessionPrimary (citable) accession number: O68249
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: August 1, 1998
Last modified: February 9, 2010
This is version 50 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