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Q58579 (RIBL_METJA) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 77. 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:
FAD synthase

EC=2.7.7.2
Alternative name(s):
FMN adenylyltransferase
Flavin adenine dinucleotide synthase
Gene names
Name:ribL
Ordered Locus Names:MJ1179
OrganismMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii) [Reference proteome] [HAMAP]
Taxonomic identifier243232 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus

Protein attributes

Sequence length149 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Catalyzes the transfer of the AMP portion of ATP to flavin mononucleotide (FMN) to produce flavin adenine dinucleotide (FAD) coenzyme. To a lesser extent, is also able to utilize other nucleotides such as CTP and GTP as substrates, producing the modified coenzymes, flavin cytosine dinucleotide (FCD) and flavin guanine dinucleotide (FGD), respectively. Does not catalyze the reverse reaction to produce FMN and ATP from FAD and PPi. Does not function as a glycerol-3-phosphate cytidylyltransferase, as previously annotated in the complete genome. Ref.2

Catalytic activity

ATP + FMN = diphosphate + FAD. Ref.2

Cofactor

Divalent metal cations. The best activity is observed with Co2+, where the activity is 4 and 2.5 times greater than that with Mg2+ and Mn2+, respectively. Ref.2

Enzyme regulation

Is inhibited by the product PPi. Ref.2

Pathway

Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step 1/1. Ref.2

Subunit structure

Homodimer. Ref.2

Miscellaneous

Alkylation of both Cys-126 and Cys-143 results in complete loss of enzymatic activity.

Sequence similarities

Belongs to the archaeal FAD synthase family.

Biophysicochemical properties

Kinetic parameters:

KM=25 µM for ATP Ref.2

KM=63 µM for FMN

KM=480 µM for CTP

Vmax=14 nmol/min/mg enzyme with ATP and FMN as substrates

Vmax=10 nmol/min/mg enzyme with CTP and FMN as substrates

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 149149FAD synthase HAMAP-Rule MF_02115
PRO_0000107202

Regions

Nucleotide binding10 – 112ATP By similarity
Nucleotide binding15 – 184ATP By similarity
Nucleotide binding93 – 964ATP By similarity

Sites

Binding site1231ATP; via amide nitrogen By similarity

Experimental info

Mutagenesis1261C → S: 2-fold increase in activity with Mg(2+) but loss of activity with Co(2+) as cofactor. Ref.2
Mutagenesis1431C → S: Nearly no change in activity with Mg(2+) but loss of activity with Co(2+) as cofactor. Ref.2

Sequences

Sequence LengthMass (Da)Tools
Q58579 [UniParc].

Last modified November 1, 1996. Version 1.
Checksum: 55FD11671ED94594

FASTA14917,288
        10         20         30         40         50         60 
MKKRVVTAGT FDILHPGHYE ILKFAKSLGD ELIVIVARDE TVKKLKGRKP IIPEEQRREM 

        70         80         90        100        110        120 
VEALKPVDKA ILGSLKNKLE PILELKPDII VLGPDQTTFD EETLKKELAK YNLYPEIVRF 

       130        140 
RGYKKCPFHS SFDIVKEIIR RFCNKEIKI 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
L77117 Genomic DNA. Translation: AAB99182.1.
PIRB64447.
RefSeqNP_248173.1. NC_000909.1.

3D structure databases

ProteinModelPortalQ58579.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING243232.MJ1179.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAB99182; AAB99182; MJ_1179.
GeneID1452077.
KEGGmja:MJ_1179.

Phylogenomic databases

eggNOGCOG0615.
KOK14656.
OMAFAKKHAD.
PhylomeDBQ58579.

Enzyme and pathway databases

BioCycMetaCyc:MONOMER-16487.
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_METJA
AccessionPrimary (citable) accession number: Q58579
Entry history
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: November 1, 1996
Last modified: July 9, 2014
This is version 77 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

Methanococcus jannaschii

Methanococcus jannaschii: entries and gene names