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C1A293 (C1A293_RHOE4) Unreviewed, UniProtKB/TrEMBL

Last modified December 14, 2011. Version 15. Feed History...

Clusters with 100%, 90%, 50% identity | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
6,7-dimethyl-8-ribityllumazine synthase 2 HAMAP MF_00178
Short name=DMRL synthase 2 HAMAP MF_00178
Short name=Lumazine synthase 2 HAMAP MF_00178
EC=2.5.1.9 HAMAP MF_00178
Alternative name(s):
Riboflavin synthase beta chain 2 HAMAP MF_00178
Gene names
Name:ribH2 HAMAP MF_00178 EMBL BAH34728.1
Ordered Locus Names:RER_40200
OrganismRhodococcus erythropolis (strain PR4 / NBRC 100887) [Complete proteome] [HAMAP]
Taxonomic identifier234621 [NCBI]
Taxonomic lineageBacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Nocardiaceae › Rhodococcus

Protein attributes

Sequence length155 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Riboflavin synthase is a bifunctional enzyme complex catalyzing the formation of riboflavin from 5-amino-6-(1'-D)-ribityl-amino-2,4(1H,3H)-pyrimidinedione and L-3,4-dihydrohy-2-butanone-4-phosphate via 6,7-dimethyl-8-lumazine. The beta subunit catalyzes the condensation of 5-amino-6-(1'-D)-ribityl-amino-2,4(1H,3H)-pyrimidinedione with L-3,4-dihydrohy-2-butanone-4-phosphate yielding 6,7-dimethyl-8-lumazine By similarity. HAMAP MF_00178

Catalytic activity

2 6,7-dimethyl-8-(1-D-ribityl)lumazine = riboflavin + 4-(1-D-ribitylamino)-5-amino-2,6-dihydroxypyrimidine. HAMAP MF_00178 RuleBase RU003795

Pathway

Cofactor biosynthesis; riboflavin biosynthesis; riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-ribitylamino)uracil: step 2/2. HAMAP MF_00178 RuleBase RU003795

Sequence similarities

Belongs to the DMRL synthase family. HAMAP MF_00178 RuleBase RU003795

Sequences

Sequence LengthMass (Da)Tools
C1A293 [UniParc].

Last modified May 26, 2009. Version 1.
Checksum: 9D4AA42D61FAF143

FASTA15517,175
        10         20         30         40         50         60 
MVMSEIQGQR IAFIQATWHR NIVDRARDGF TDAIVELGYP KDTVDFFEVP GAFEIPLHAR 

        70         80         90        100        110        120 
RLAKTGRYQA IVAAGLVVDG GIYRHDFVAT AVIDGLMRVQ LDTDVPVFSV VLTPHNFHEH 

       130        140        150 
AEHVDYFSTH FVKKGAEAAR AVDATVKSLK ALPTS

« Hide

References

[1]"Comparison of the complete genome sequences of Rhodococcus erythropolis PR4 and Rhodococcus opacus B4."
Takarada H., Sekine M., Hosoyama A., Yamada R., Fujisawa T., Omata S., Shimizu A., Tsukatani N., Tanikawa S., Fujita N., Harayama S.
Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: PR4 / NBRC 100887.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AP008957 Genomic DNA. Translation: BAH34728.1.
RefSeqYP_002767467.1. NC_012490.1.

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

STRINGC1A293.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID7711530.
GenomeReviewsGene locus RER_40200 in contig AP008957_GR.
KEGGrer:RER_40200.
PATRIC23194581. VBIRhoEry66701_4553.

Organism-specific databases

CMRSearch...

Phylogenomic databases

OMARRYTAIV.
ProtClustDBPRK12419.

Family and domain databases

HAMAPMF_00178. Lumazine_synth.
[Tree]
InterProIPR002180. DMRL_synthase.
[Graphical view]
Gene3DG3DSA:3.40.50.960. DMRL_synthase. 1 hit.
KOK00794.
PANTHERPTHR21058. DMRL_synthase. 1 hit.
PfamPF00885. DMRL_synthase. 1 hit.
[Graphical view]
SUPFAMSSF52121. DMRL_synthase. 1 hit.
TIGRFAMsTIGR00114. Lumazine-synth. 1 hit.
ProtoNetSearch...

Entry information

Entry nameC1A293_RHOE4
AccessionPrimary (citable) accession number: C1A293
Entry history
Integrated into UniProtKB/TrEMBL: May 26, 2009
Last sequence update: May 26, 2009
Last modified: December 14, 2011
This is version 15 of the entry and version 1 of the sequence. [Complete history]
Entry statusUnreviewed (UniProtKB/TrEMBL)
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