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Q979C2 (RIBL_THEVO) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 70. 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:TV1239
ORF Names:TVG1279046
OrganismThermoplasma volcanium (strain ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1) [Complete proteome] [HAMAP]
Taxonomic identifier273116 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma

Protein attributes

Sequence length142 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 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 142142FAD synthase HAMAP-Rule MF_02115
PRO_0000406287

Regions

Nucleotide binding9 – 102ATP HAMAP-Rule MF_02115
Nucleotide binding14 – 174ATP HAMAP-Rule MF_02115
Nucleotide binding91 – 944ATP HAMAP-Rule MF_02115

Sites

Binding site1201ATP; via amide nitrogen

Secondary structure

..................... 142
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Q979C2 [UniParc].

Last modified October 1, 2001. Version 1.
Checksum: B9A106F982D0022E

FASTA14216,009
        10         20         30         40         50         60 
MIRVMATGVF DILHLGHIHY LKESKKLGDE LVVVVARDST ARNNGKIPIF DENSRLALIS 

        70         80         90        100        110        120 
ELKVVDRAIL GHEGDMMKTV IEVKPDIITL GYDQKFDEAE LQSKINKLGI TVKIVRISKY 

       130        140 
DGQLNSSSSV RKKIMELIGE RY 

« Hide

References

« Hide 'large scale' references
[1]"Archaeal adaptation to higher temperatures revealed by genomic sequence of Thermoplasma volcanium."
Kawashima T., Amano N., Koike H., Makino S., Higuchi S., Kawashima-Ohya Y., Watanabe K., Yamazaki M., Kanehori K., Kawamoto T., Nunoshiba T., Yamamoto Y., Aramaki H., Makino K., Suzuki M.
Proc. Natl. Acad. Sci. U.S.A. 97:14257-14262(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 51530 / DSM 4299 / JCM 9571 / NBRC 15438 / GSS1.
[2]"The crystal structure of the lipopolysaccharide core biosynthesis protein from Thermoplasma volcanium GSS1."
Midwest center for structural genomics (MCSG)
Submitted (MAY-2009) to the PDB data bank
Cited for: X-RAY CRYSTALLOGRAPHY (1.99 ANGSTROMS) IN COMPLEX WITH AMP.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000011 Genomic DNA. Translation: BAB60381.1.
RefSeqNP_111734.1. NC_002689.2.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3GLVX-ray1.99A/B1-142[»]
ProteinModelPortalQ979C2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273116.TVN1215.

Protocols and materials databases

DNASU1441355.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAB60381; BAB60381; BAB60381.
GeneID1441355.
KEGGtvo:TVN1215.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0615.
KOK14656.
OMAIVLGHDQ.

Enzyme and pathway databases

BioCycTVOL273116:GC31-1257-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...

Other

EvolutionaryTraceQ979C2.

Entry information

Entry nameRIBL_THEVO
AccessionPrimary (citable) accession number: Q979C2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: October 1, 2001
Last modified: May 14, 2014
This is version 70 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