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P61726 (RISB1_RHOPA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 1, 2013. Version 58. 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:
6,7-dimethyl-8-ribityllumazine synthase 1

Short name=DMRL synthase 1
Short name=LS 1
Short name=Lumazine synthase 1
EC=2.5.1.78
Gene names
Name:ribH1
Synonyms:ribE
Ordered Locus Names:RPA2728
OrganismRhodopseudomonas palustris (strain ATCC BAA-98 / CGA009) [Complete proteome] [HAMAP]
Taxonomic identifier258594 [NCBI]
Taxonomic lineageBacteriaProteobacteriaAlphaproteobacteriaRhizobialesBradyrhizobiaceaeRhodopseudomonas

Protein attributes

Sequence length163 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate. This is the penultimate step in the biosynthesis of riboflavin By similarity. HAMAP-Rule MF_00178

Catalytic activity

1-deoxy-L-glycero-tetrulose 4-phosphate + 5-amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(D-ribityl)lumazine + 2 H2O + phosphate. HAMAP-Rule MF_00178

Pathway

Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 1/2. HAMAP-Rule MF_00178

Sequence similarities

Belongs to the DMRL synthase family.

Ontologies

Keywords
   Biological processRiboflavin biosynthesis
   Molecular functionTransferase
   Technical termComplete proteome
Gene Ontology (GO)
   Biological_processriboflavin biosynthetic process

Inferred from electronic annotation. Source: HAMAP

   Cellular_componentriboflavin synthase complex

Inferred from electronic annotation. Source: InterPro

   Molecular_function6,7-dimethyl-8-ribityllumazine synthase activity

Inferred from electronic annotation. Source: HAMAP

transferase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 1631636,7-dimethyl-8-ribityllumazine synthase 1 HAMAP-Rule MF_00178
PRO_0000134798

Regions

Region58 – 6035-amino-6-(D-ribitylamino)uracil binding By similarity
Region87 – 8935-amino-6-(D-ribitylamino)uracil binding By similarity
Region92 – 9321-deoxy-L-glycero-tetrulose 4-phosphate binding By similarity

Sites

Active site951Proton donor Potential
Binding site2715-amino-6-(D-ribitylamino)uracil By similarity
Binding site12015-amino-6-(D-ribitylamino)uracil; via amide nitrogen and carbonyl oxygen By similarity
Binding site13411-deoxy-L-glycero-tetrulose 4-phosphate By similarity

Sequences

Sequence LengthMass (Da)Tools
P61726 [UniParc].

Last modified June 7, 2004. Version 1.
Checksum: 89187DD3C6655AB0

FASTA16317,088
        10         20         30         40         50         60 
MADARRAPLK DQTDVSGARV LIVEARFYDD IQDALLEGAV AELKAAGATH DVLTVPGALE 

        70         80         90        100        110        120 
IPAAVAIAID SAEAAGKPYD AAIALGCVVR GETIHFEIVS MESARALMDL SVARKFPLGN 

       130        140        150        160 
GIITVNTDEQ AWARAKPGDL NKGGDAARAA LAMLRIKRRL AKA 

« Hide

References

[1]"Complete genome sequence of the metabolically versatile photosynthetic bacterium Rhodopseudomonas palustris."
Larimer F.W., Chain P., Hauser L., Lamerdin J.E., Malfatti S., Do L., Land M.L., Pelletier D.A., Beatty J.T., Lang A.S., Tabita F.R., Gibson J.L., Hanson T.E., Bobst C., Torres y Torres J.L., Peres C., Harrison F.H., Gibson J., Harwood C.S.
Nat. Biotechnol. 22:55-61(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-98 / CGA009.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BX572601 Genomic DNA. Translation: CAE28170.1.
RefSeqNP_948071.1. NC_005296.1.

3D structure databases

ProteinModelPortalP61726.
ModBaseSearch...

Protein-protein interaction databases

STRING258594.RPA2728.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAE28170; CAE28170; RPA2728.
GeneID2693505.
KEGGrpa:RPA2728.
PATRIC23289873. VBIRhoPal84835_2864.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0054.
HOGENOMHOG000229250.
KOK00794.
OMAIVSMESA.
ProtClustDBPRK00061.

Enzyme and pathway databases

UniPathwayUPA00275; UER00404.

Family and domain databases

Gene3D3.40.50.960. 1 hit.
HAMAPMF_00178. Lumazine_synth.
InterProIPR002180. DMRL_synthase.
[Graphical view]
PANTHERPTHR21058. PTHR21058. 1 hit.
PfamPF00885. DMRL_synthase. 1 hit.
[Graphical view]
SUPFAMSSF52121. DMRL_synthase. 1 hit.
TIGRFAMsTIGR00114. lumazine-synth. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRISB1_RHOPA
AccessionPrimary (citable) accession number: P61726
Entry history
Integrated into UniProtKB/Swiss-Prot: June 7, 2004
Last sequence update: June 7, 2004
Last modified: May 1, 2013
This is version 58 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