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D3RZA9 (RIBL_FERPA) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 29. 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:
FAD synthase

EC=2.7.7.2
Alternative name(s):
FMN adenylyltransferase
Flavin adenine dinucleotide synthase
Gene names
Name:ribL
Ordered Locus Names:Ferp_1676
OrganismFerroglobus placidus (strain DSM 10642 / AEDII12DO) [Complete proteome] [HAMAP]
Taxonomic identifier589924 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaArchaeoglobiArchaeoglobalesArchaeoglobaceaeFerroglobus

Protein attributes

Sequence length152 AA.
Sequence statusComplete.
Protein existenceInferred from homology

General annotation (Comments)

Function

Catalyzes the transfer of the AMP portion of ATP to flavin mononucleotide (FMN) to produce flavin adenine dinucleotide (FAD) coenzyme By similarity. HAMAP-Rule MF_02115

Catalytic activity

ATP + FMN = diphosphate + FAD. HAMAP-Rule MF_02115

Cofactor

Divalent metal cations By similarity. HAMAP-Rule MF_02115

Pathway

Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1. HAMAP-Rule MF_02115

Subunit structure

Homodimer By similarity. HAMAP-Rule MF_02115

Sequence similarities

Belongs to the archaeal FAD synthase family.

Ontologies

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 152152FAD synthase HAMAP-Rule MF_02115
PRO_0000406234

Regions

Nucleotide binding9 – 102ATP By similarity
Nucleotide binding14 – 174ATP By similarity
Nucleotide binding90 – 934ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
D3RZA9 [UniParc].

Last modified April 20, 2010. Version 1.
Checksum: BF5DD18B8AB76D78

FASTA15217,696
        10         20         30         40         50         60 
MKKVVATGTF DIIHPGHVRF LEEAKKLGDY LVVIVAREKN VKHKPKPIMP EEQRRRVVEA 

        70         80         90        100        110        120 
LKPVDEAILG DEEDIFKPIE KIKPDVIALG YDQHFDEEWL REELRKRGIK AEVVRIRAKE 

       130        140        150 
DCELCSSAKI IERIVTLASS RLKDFQERKE KL 

« Hide

References

[1]"Complete sequence of Ferroglobus placidus DSM 10642."
US DOE Joint Genome Institute
Lucas S., Copeland A., Lapidus A., Cheng J.-F., Bruce D., Goodwin L., Pitluck S., Saunders E., Brettin T., Detter J.C., Han C., Tapia R., Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Holmes D. expand/collapse author list , Lovley D., Kyrpides N., Anderson I.J., Woyke T.
Submitted (FEB-2010) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 10642 / AEDII12DO.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001899 Genomic DNA. Translation: ADC65822.1.
RefSeqYP_003436097.1. NC_013849.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADC65822; ADC65822; Ferp_1676.
GeneID8779201.
KEGGfpl:Ferp_1676.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000284153.
KOK14656.
OMAIVLGHDQ.

Enzyme and pathway databases

BioCycFPLA589924:GHX0-1711-MONOMER.
UniPathwayUPA00277; UER00407.

Family and domain databases

Gene3D3.40.50.620. 1 hit.
HAMAPMF_02115. FAD_synth_arch.
InterProIPR004821. Cyt_trans-like.
IPR024902. FAD_synth_RibL.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamPF01467. CTP_transf_2. 1 hit.
[Graphical view]
TIGRFAMsTIGR00125. cyt_tran_rel. 1 hit.
ProtoNetSearch...

Entry information

Entry nameRIBL_FERPA
AccessionPrimary (citable) accession number: D3RZA9
Entry history
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: April 20, 2010
Last modified: May 14, 2014
This is version 29 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

PATHWAY comments

Index of metabolic and biosynthesis pathways