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Q9UZ37 (RIBL_PYRAB) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 69. 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:PYRAB13170
ORF Names:PAB1507
OrganismPyrococcus abyssi (strain GE5 / Orsay) [Complete proteome] [HAMAP]
Taxonomic identifier272844 [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_0000406279

Regions

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

Sequences

Sequence LengthMass (Da)Tools
Q9UZ37 [UniParc].

Last modified May 1, 2000. Version 1.
Checksum: 262B17E43AE43E0D

FASTA14816,833
        10         20         30         40         50         60 
MAGNRRIRVV VGGVFDILHV GHIHFLKMAK ELGDELIVIV AHDETVKKRK GRPPINPAED 

        70         80         90        100        110        120 
RAEVLRAIRY VDDVVIGEPG EISLELIKKL KPDVIALGPD QDFDCRTLKE KLRSIGLKVE 

       130        140 
VIRLPYLYKE DRAKTSKIIK RITEIFCD 

« Hide

References

« Hide 'large scale' references
[1]"An integrated analysis of the genome of the hyperthermophilic archaeon Pyrococcus abyssi."
Cohen G.N., Barbe V., Flament D., Galperin M., Heilig R., Lecompte O., Poch O., Prieur D., Querellou J., Ripp R., Thierry J.-C., Van der Oost J., Weissenbach J., Zivanovic Y., Forterre P.
Mol. Microbiol. 47:1495-1512(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: GE5 / Orsay.
[2]"Re-annotation of two hyperthermophilic archaea Pyrococcus abyssi GE5 and Pyrococcus furiosus DSM 3638."
Gao J., Wang J.
Curr. Microbiol. 64:118-129(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: GENOME REANNOTATION.
Strain: GE5 / Orsay.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AJ248287 Genomic DNA. Translation: CAB50222.1.
HE613800 Genomic DNA. Translation: CCE70758.1.
PIRA75041.
RefSeqNP_126992.1. NC_000868.1.

3D structure databases

ProteinModelPortalQ9UZ37.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING272844.PAB1507.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaCAB50222; CAB50222; PAB1507.
GeneID1496704.
KEGGpab:PAB1507.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0615.
HOGENOMHOG000284153.
KOK14656.
OMAIVLGHDQ.

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_PYRAB
AccessionPrimary (citable) accession number: Q9UZ37
Secondary accession number(s): G8ZHC1
Entry history
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: May 1, 2000
Last modified: May 14, 2014
This is version 69 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