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Q6L0A7 (RIBL_PICTO) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 55. 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:PTO1010
OrganismPicrophilus torridus (strain ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828) [Complete proteome] [HAMAP]
Taxonomic identifier263820 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaThermoplasmataThermoplasmatalesPicrophilaceaePicrophilus

Protein attributes

Sequence length139 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 – 139139FAD synthase HAMAP-Rule MF_02115
PRO_0000406278

Regions

Nucleotide binding8 – 92ATP By similarity
Nucleotide binding13 – 164ATP By similarity
Nucleotide binding90 – 934ATP By similarity

Sites

Binding site1191ATP; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q6L0A7 [UniParc].

Last modified July 5, 2004. Version 1.
Checksum: D3B26EECB2F0ADB7

FASTA13916,169
        10         20         30         40         50         60 
MKIMATGVFD ILHPGHIHYL SESKKLGDYL IVIIATDKTA GSHGKKLIFN EEQRRFMVSQ 

        70         80         90        100        110        120 
LRMVDEAIIG HEDDIFKTVY EVRPDIITLG YDQHFNDSEI EKKCRDLGLN TRVVRISKYD 

       130 
GEIKSSSDIR RRIIELYNR 

« Hide

References

[1]"Genome sequence of Picrophilus torridus and its implications for life around pH 0."
Fuetterer O., Angelov A., Liesegang H., Gottschalk G., Schleper C., Schepers B., Dock C., Antranikian G., Liebl W.
Proc. Natl. Acad. Sci. U.S.A. 101:9091-9096(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 700027 / DSM 9790 / JCM 10055 / NBRC 100828.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE017261 Genomic DNA. Translation: AAT43595.1.
RefSeqYP_023788.1. NC_005877.1.

3D structure databases

ProteinModelPortalQ6L0A7.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING263820.PTO1010.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAT43595; AAT43595; PTO1010.
GeneID2844853.
KEGGpto:PTO1010.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0615.
HOGENOMHOG000284153.
KOK14656.
OMAVAHDETV.
ProtClustDBCLSK227867.

Enzyme and pathway databases

BioCycPTOR263820:GHA3-1052-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_PICTO
AccessionPrimary (citable) accession number: Q6L0A7
Entry history
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: July 5, 2004
Last modified: February 19, 2014
This is version 55 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