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Q5JHT4 (RIBL_THEKO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 60. 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:TK2274
OrganismThermococcus kodakaraensis (strain ATCC BAA-918 / JCM 12380 / KOD1) (Pyrococcus kodakaraensis (strain KOD1)) [Reference proteome] [HAMAP]
Taxonomic identifier69014 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaeThermococcus

Protein attributes

Sequence length149 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 – 149149FAD synthase HAMAP-Rule MF_02115
PRO_0000406282

Regions

Nucleotide binding15 – 162ATP By similarity
Nucleotide binding20 – 234ATP By similarity
Nucleotide binding99 – 1024ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5JHT4 [UniParc].

Last modified February 15, 2005. Version 1.
Checksum: 5D0C81C1322844C3

FASTA14917,304
        10         20         30         40         50         60 
MEEKRKKIRV LVGGVFDILH VGHIHFLKQA KELGDELVVI VAHDETVRMQ KRREPINPAE 

        70         80         90        100        110        120 
DRAELLRAIR YVDEVYIGTP GTIDMELVKR IDPDVIAIGP DQFFNCEKLK EELRKHGINA 

       130        140 
EVIRIPYLYK SDRAKTSKII QRIVETFCE 

« Hide

References

[1]"Complete genome sequence of the hyperthermophilic archaeon Thermococcus kodakaraensis KOD1 and comparison with Pyrococcus genomes."
Fukui T., Atomi H., Kanai T., Matsumi R., Fujiwara S., Imanaka T.
Genome Res. 15:352-363(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC BAA-918 / JCM 12380 / KOD1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AP006878 Genomic DNA. Translation: BAD86463.1.
RefSeqYP_184687.1. NC_006624.1.

3D structure databases

ProteinModelPortalQ5JHT4.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING69014.TK2274.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAD86463; BAD86463; TK2274.
GeneID3234716.
KEGGtko:TK2274.

Phylogenomic databases

eggNOGCOG0615.
HOGENOMHOG000284153.
KOK14656.
OMAVAHDETV.
ProtClustDBCLSK253517.

Enzyme and pathway databases

BioCycTKOD69014:GH72-2326-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_THEKO
AccessionPrimary (citable) accession number: Q5JHT4
Entry history
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: February 15, 2005
Last modified: February 19, 2014
This is version 60 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