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Q2NHB2 (RIBL_METST) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 52. 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:Msp_0390
OrganismMethanosphaera stadtmanae (strain ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3) [Complete proteome] [HAMAP]
Taxonomic identifier339860 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanosphaera

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_0000406271

Regions

Nucleotide binding5 – 62ATP By similarity
Nucleotide binding10 – 134ATP By similarity
Nucleotide binding90 – 934ATP By similarity

Sites

Binding site1191ATP; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2NHB2 [UniParc].

Last modified February 7, 2006. Version 1.
Checksum: 73288E85B05EA011

FASTA14816,744
        10         20         30         40         50         60 
MASGTFDIIH PGHGFYLSES KKLGGDNAIL MVVVATDKTV KNHKRVPIVG EKQRCEMVSM 

        70         80         90        100        110        120 
LKGVDEAYVG DEKDPFKIVK EKKPDIITIG PDQNFNPDSL HKSLLKKGLD IKVVKINDYK 

       130        140 
KFELDSSCKI IRKIKQTDFD MDYLENCQ 

« Hide

References

[1]"The genome sequence of Methanosphaera stadtmanae reveals why this human intestinal archaeon is restricted to methanol and H2 for methane formation and ATP synthesis."
Fricke W.F., Seedorf H., Henne A., Kruer M., Liesegang H., Hedderich R., Gottschalk G., Thauer R.K.
J. Bacteriol. 188:642-658(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 43021 / DSM 3091 / JCM 11832 / MCB-3.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000102 Genomic DNA. Translation: ABC56791.1.
RefSeqYP_447434.1. NC_007681.1.

3D structure databases

ProteinModelPortalQ2NHB2.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING339860.Msp_0390.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABC56791; ABC56791; Msp_0390.
GeneID3855755.
KEGGmst:Msp_0390.

Organism-specific databases

CMRSearch...

Phylogenomic databases

eggNOGCOG0615.
HOGENOMHOG000284153.
KOK14656.
OMAIVLGHDQ.

Enzyme and pathway databases

BioCycMSTA339860:GJEZ-390-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_METST
AccessionPrimary (citable) accession number: Q2NHB2
Entry history
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: February 7, 2006
Last modified: May 14, 2014
This is version 52 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