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D9PX81 (RIBL_METTM) Reviewed, UniProtKB/Swiss-Prot

Last modified May 14, 2014. Version 26. 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:MTBMA_c12410
OrganismMethanothermobacter marburgensis (strain DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum) [Complete proteome] [HAMAP]
Taxonomic identifier79929 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter

Protein attributes

Sequence length161 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 – 161161FAD synthase HAMAP-Rule MF_02115
PRO_0000406274

Regions

Nucleotide binding19 – 202ATP By similarity
Nucleotide binding24 – 274ATP By similarity
Nucleotide binding104 – 1074ATP By similarity

Sites

Binding site1331ATP; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
D9PX81 [UniParc].

Last modified October 5, 2010. Version 1.
Checksum: 60C2822CE8D830C1

FASTA16118,664
        10         20         30         40         50         60 
MKRFSDKRTQ IKTVMATGTF DIIHPGHGFF LEEAKKLGGE NARLVVVLAR DSTVRARKRT 

        70         80         90        100        110        120 
PIIGEKQRLE VVMMLKPVDE AYLGSETDMF EIVHRLKPDI IAIGPDQKFD IDELRDELRR 

       130        140        150        160 
RGLECEVKRV GKYRRSELDS TCKIIKKIRK MEFDEDALKN C 

« Hide

References

[1]"Complete genome sequence of Methanothermobacter marburgensis, a methanoarchaeon model organism."
Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H., Gottschalk G., Thauer R.K.
J. Bacteriol. 192:5850-5851(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP001710 Genomic DNA. Translation: ADL58829.1.
RefSeqYP_003850142.1. NC_014408.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaADL58829; ADL58829; MTBMA_c12410.
GeneID9704949.
KEGGmmg:MTBMA_c12410.

Organism-specific databases

CMRSearch...

Phylogenomic databases

HOGENOMHOG000284153.
KOK14656.
OMAIVLGHDQ.

Enzyme and pathway databases

BioCycMMAR79929:GH5J-1244-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_METTM
AccessionPrimary (citable) accession number: D9PX81
Entry history
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: October 5, 2010
Last modified: May 14, 2014
This is version 26 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