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Q9HJ34 (RIBL_THEAC) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 62. 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:Ta1139
OrganismThermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165) [Reference proteome] [HAMAP]
Taxonomic identifier273075 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesThermoplasmataceaeThermoplasma

Protein attributes

Sequence length142 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 142142FAD synthase HAMAP-Rule MF_02115
PRO_0000406286

Regions

Nucleotide binding9 – 102ATP By similarity
Nucleotide binding14 – 174ATP By similarity
Nucleotide binding91 – 944ATP By similarity

Sites

Binding site1201ATP; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q9HJ34 [UniParc].

Last modified March 1, 2001. Version 1.
Checksum: C047A9F91F4F595B

FASTA14216,196
        10         20         30         40         50         60 
MVRVMATGVF DIIHLGHIHY LRESKKLGDE LVVVVARDST ARKNGKVPIF DENSRLKLVS 

        70         80         90        100        110        120 
ELKPVDRAIL GHEDDMMKTV VEVMPDIITL GYDQKFDEAD LKRKLDQIGV NSRIVRISKY 

       130        140 
DGNLNSSSMV RKKIMELIGE RF 

« Hide

References

[1]"The genome sequence of the thermoacidophilic scavenger Thermoplasma acidophilum."
Ruepp A., Graml W., Santos-Martinez M.-L., Koretke K.K., Volker C., Mewes H.-W., Frishman D., Stocker S., Lupas A.N., Baumeister W.
Nature 407:508-513(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AL445066 Genomic DNA. Translation: CAC12265.1.
RefSeqNP_394596.1. NC_002578.1.

3D structure databases

ProteinModelPortalQ9HJ34.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING273075.Ta1139.

Proteomic databases

PRIDEQ9HJ34.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAC12265; CAC12265; CAC12265.
GeneID1456643.
KEGGtac:Ta1139.

Phylogenomic databases

eggNOGCOG0615.
HOGENOMHOG000284153.
KOK14656.
OMAVAHDETV.
ProtClustDBCLSK227867.

Enzyme and pathway databases

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_THEAC
AccessionPrimary (citable) accession number: Q9HJ34
Entry history
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: March 1, 2001
Last modified: February 19, 2014
This is version 62 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