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O58466 (RIBL_PYRHO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 77. 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:PH0735
OrganismPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) [Complete proteome] [HAMAP]
Taxonomic identifier70601 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus

Protein attributes

Sequence length148 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 – 148148FAD synthase HAMAP-Rule MF_02115
PRO_0000406281

Regions

Nucleotide binding14 – 152ATP By similarity
Nucleotide binding19 – 224ATP By similarity
Nucleotide binding98 – 1014ATP By similarity

Sequences

Sequence LengthMass (Da)Tools
O58466 [UniParc].

Last modified August 1, 1998. Version 1.
Checksum: 07F566C19188FE38

FASTA14816,737
        10         20         30         40         50         60 
MGSDRKIRVV VGGVFDIIHA GHVHFLKMAK ELGDELIVIV AHDETVKKRK GRPPINPAED 

        70         80         90        100        110        120 
RAEVLKAIRY VDDVVIGKPG EISLDLIKRL KPDVIALGPD QDFDCEDLKR KLKSIGLNVE 

       130        140 
VIRLPYLYKK DRAKTSKIIE RITEIFCD 

« Hide

References

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
BA000001 Genomic DNA. Translation: BAA29826.1.
PIRH71120.
RefSeqNP_142678.1. NC_000961.1.

3D structure databases

ProteinModelPortalO58466.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING70601.PH0735.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaBAA29826; BAA29826; BAA29826.
GeneID1443066.
KEGGpho:PH0735.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0615.
HOGENOMHOG000284153.
KOK14656.
OMAVAHDETV.
ProtClustDBCLSK253517.

Enzyme and pathway databases

BioCycPHOR70601:GJWR-732-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_PYRHO
AccessionPrimary (citable) accession number: O58466
Entry history
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: August 1, 1998
Last modified: February 19, 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