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Q8TXT2 (RIBL_METKA) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 59. 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:MK0578
OrganismMethanopyrus kandleri (strain AV19 / DSM 6324 / JCM 9639 / NBRC 100938) [Reference proteome] [HAMAP]
Taxonomic identifier190192 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanopyriMethanopyralesMethanopyraceaeMethanopyrus

Protein attributes

Sequence length150 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 – 150150FAD synthase HAMAP-Rule MF_02115
PRO_0000406265

Regions

Nucleotide binding10 – 112ATP By similarity
Nucleotide binding15 – 184ATP By similarity
Nucleotide binding95 – 984ATP By similarity

Sites

Binding site1241ATP; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q8TXT2 [UniParc].

Last modified June 1, 2002. Version 1.
Checksum: 4E8C5D1817051216

FASTA15017,107
        10         20         30         40         50         60 
MGKRVLAGGV FDILHPGHVA FLEEARKIAG KNGELVVVVA RDETVRRLKR TPIVPEEQRV 

        70         80         90        100        110        120 
RMVSALKPVD RAILGHPRDF SITLKTVKPD VVVLGPDQDI DEKEVERWAE RAGVDCEVRR 

       130        140        150 
IEKYERCPLD STIKIVKRVI ELWKRGELRV 

« Hide

References

[1]"The complete genome of hyperthermophile Methanopyrus kandleri AV19 and monophyly of archaeal methanogens."
Slesarev A.I., Mezhevaya K.V., Makarova K.S., Polushin N.N., Shcherbinina O.V., Shakhova V.V., Belova G.I., Aravind L., Natale D.A., Rogozin I.B., Tatusov R.L., Wolf Y.I., Stetter K.O., Malykh A.G., Koonin E.V., Kozyavkin S.A.
Proc. Natl. Acad. Sci. U.S.A. 99:4644-4649(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: AV19 / DSM 6324 / JCM 9639 / NBRC 100938.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AE009439 Genomic DNA. Translation: AAM01793.1.
RefSeqNP_613863.1. NC_003551.1.

3D structure databases

ProteinModelPortalQ8TXT2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING190192.MK0578.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaAAM01793; AAM01793; MK0578.
GeneID1476679.
KEGGmka:MK0578.

Phylogenomic databases

eggNOGCOG0615.
HOGENOMHOG000284153.
KOK14656.
OMAVAHDETV.

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_METKA
AccessionPrimary (citable) accession number: Q8TXT2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: June 1, 2002
Last modified: February 19, 2014
This is version 59 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