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Q59263 (RIBF_CORAM) Reviewed, UniProtKB/Swiss-Prot

Last modified January 22, 2014. Version 71. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Riboflavin biosynthesis protein RibF

Including the following 2 domains:

  1. Riboflavin kinase
    EC=2.7.1.26
    Alternative name(s):
    Flavokinase
  2. FMN adenylyltransferase
    EC=2.7.7.2
    Alternative name(s):
    FAD pyrophosphorylase
    FAD synthase
Gene names
Name:ribF
OrganismCorynebacterium ammoniagenes (Brevibacterium ammoniagenes)
Taxonomic identifier1697 [NCBI]
Taxonomic lineageBacteriaActinobacteriaActinobacteridaeActinomycetalesCorynebacterineaeCorynebacteriaceaeCorynebacterium

Protein attributes

Sequence length338 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Catalytic activity

ATP + riboflavin = ADP + FMN.

ATP + FMN = diphosphate + FAD.

Enzyme regulation

Higher divalent cation concentrations lead to decrease in the turnover of riboflavin and the 5'-phosphotransferase activity, while the adenylyltransferase activity increases. With magnesium ions the highest turnover of riboflavin is observed between pH 6 and 7.5, while that of FAD is between 7.0 and 9.0. With zinc ions a steady increase in riboflavin turnover is observed between pH 4.5 and 10, while FAD is the major product at pH 7.0 and decreases rapidly above pH 8.0.

Pathway

Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1.

Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin (ATP route): step 1/1.

Sequence similarities

Belongs to the RibF family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 338338Riboflavin biosynthesis protein RibF
PRO_0000194136

Secondary structure

............................................................ 338
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q59263 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: B714FD885412CC68

FASTA33836,844
        10         20         30         40         50         60 
MDIWYGTAAV PKDLDNSAVT IGVFDGVHRG HQKLINATVE KAREVGAKAI MVTFDPHPVS 

        70         80         90        100        110        120 
VFLPRRAPLG ITTLAERFAL AESFGIDGVL VIDFTRELSG TSPEKYVEFL LEDTLHASHV 

       130        140        150        160        170        180 
VVGANFTFGE NAAGTADSLR QICQSRLTVD VIDLLDDEGV RISSTTVREF LSEGDVARAN 

       190        200        210        220        230        240 
WALGRHFYVT GPVVRGAGRG GKELGFPTAN QYFHDTVALP ADGVYAGWLT ILPTEAPVSG 

       250        260        270        280        290        300 
NMEPEVAYAA AISVGTNPTF GDEQRSVESF VLDRDADLYG HDVKVEFVDH VRAMEKFDSV 

       310        320        330 
EQLLEVMAKD VQKTRTLLAQ DVQAHKMAPE TYFLQAES 

« Hide

References

[1]"Nucleotide sequence of the FAD synthetase gene from Corynebacterium ammoniagenes and its expression in Escherichia coli."
Nakagawa S., Igarashi A., Ohta T., Hagihara T., Fujio T., Aisaka K.
Biosci. Biotechnol. Biochem. 59:694-702(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Strain: ATCC 6872 / DSM 20305 / KCTC 1019 / NCTC 2399.
[2]"Purification and characterization of FAD synthetase from Brevibacterium ammoniagenes."
Manstein D.J., Pai E.F.
J. Biol. Chem. 261:16169-16173(1986) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 1-18, CHARACTERIZATION.
Strain: ATCC 6872 / DSM 20305 / KCTC 1019 / NCTC 2399.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D37967 Genomic DNA. Translation: BAA07182.1.
PIRJC4008.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2X0KX-ray1.95A/B1-338[»]
3ZUGX-ray2.05A/B1-338[»]
ProteinModelPortalQ59263.
ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

BRENDA2.7.7.2. 1639.
UniPathwayUPA00276; UER00406.
UPA00277; UER00407.

Family and domain databases

Gene3D2.40.30.30. 1 hit.
3.40.50.620. 1 hit.
InterProIPR015864. FAD_synthase.
IPR023468. Riboflavin_kinase.
IPR002606. Riboflavin_kinase_bac.
IPR015865. Riboflavin_kinase_bac/euk.
IPR023465. Riboflavin_kinase_domain.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PANTHERPTHR22749. PTHR22749. 1 hit.
PfamPF06574. FAD_syn. 1 hit.
PF01687. Flavokinase. 1 hit.
[Graphical view]
PIRSFPIRSF004491. FAD_Synth. 1 hit.
SMARTSM00904. Flavokinase. 1 hit.
[Graphical view]
SUPFAMSSF82114. SSF82114. 1 hit.
TIGRFAMsTIGR00083. ribF. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceQ59263.

Entry information

Entry nameRIBF_CORAM
AccessionPrimary (citable) accession number: Q59263
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1996
Last modified: January 22, 2014
This is version 71 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

PATHWAY comments

Index of metabolic and biosynthesis pathways