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Q2FT79 (RIBL_METHJ) Reviewed, UniProtKB/Swiss-Prot

Last modified February 19, 2014. Version 48. 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:Mhun_2404
OrganismMethanospirillum hungatei JF-1 (strain ATCC 27890 / DSM 864 / NBRC 100397 / JF-1) [Reference proteome] [HAMAP]
Taxonomic identifier323259 [NCBI]
Taxonomic lineageArchaeaEuryarchaeotaMethanomicrobiaMethanomicrobialesMethanospirillaceaeMethanospirillum

Protein attributes

Sequence length156 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 – 156156FAD synthase HAMAP-Rule MF_02115
PRO_0000406273

Regions

Nucleotide binding9 – 102ATP By similarity
Nucleotide binding14 – 174ATP By similarity
Nucleotide binding90 – 934ATP By similarity

Sites

Binding site1191ATP; via amide nitrogen By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2FT79 [UniParc].

Last modified March 21, 2006. Version 1.
Checksum: 18DBDDCFBADE82DF

FASTA15617,822
        10         20         30         40         50         60 
MIRVVATGTF DILHPGHLWY LEESAKLGDE LYVIVARDAN IRHKPRPVIP EEQRLVMVAA 

        70         80         90        100        110        120 
LKPVTHAVLG DLEDMFRPIR EIKPDIITLG CNQHFDPETL QKALEKQNIR AQVVRISEHS 

       130        140        150 
SSPFTSSRDI VRKIAELTHQ RSQTRETKEQ RECGAV 

« Hide

References

[1]"Complete sequence of Methanospirillum hungatei JF-1."
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T., Hammon N., Israni S., Pitluck S., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Kiss H., Schmutz J., Larimer F., Land M. expand/collapse author list , Kyrpides N., Ivanova N., McInerney M.J., Brockman F., Culley D., Ferry J.G., Gunsalus R.P., Morrison M., Plugge C., Scholten J., Stams A.J.M., Boone D.R., Richardson P.
Submitted (JAN-2006) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Strain: ATCC 27890 / DSM 864 / NBRC 100397 / JF-1.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
CP000254 Genomic DNA. Translation: ABD42106.1.
RefSeqYP_503825.1. NC_007796.1.

3D structure databases

ProteinModelPortalQ2FT79.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING323259.Mhun_2404.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaABD42106; ABD42106; Mhun_2404.
GeneID3922391.
KEGGmhu:Mhun_2404.

Phylogenomic databases

eggNOGCOG0615.
HOGENOMHOG000284153.
KOK14656.
OMAVAHDETV.

Enzyme and pathway databases

BioCycMHUN323259:GH0L-2436-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_METHJ
AccessionPrimary (citable) accession number: Q2FT79
Entry history
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: March 21, 2006
Last modified: February 19, 2014
This is version 48 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