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Protein

FAD synthase

Gene

ribL

Organism
Methanothermobacter marburgensis (strain DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Protein inferred from homologyi

Functioni

Catalyzes the transfer of the AMP portion of ATP to flavin mononucleotide (FMN) to produce flavin adenine dinucleotide (FAD) coenzyme.UniRule annotation

Catalytic activityi

ATP + FMN = diphosphate + FAD.UniRule annotation

Cofactori

a divalent metal cationUniRule annotation

Pathway: FAD biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes FAD from FMN.UniRule annotation
Proteins known to be involved in this subpathway in this organism are:
  1. FAD synthase (ribL)
This subpathway is part of the pathway FAD biosynthesis, which is itself part of Cofactor biosynthesis.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes FAD from FMN, the pathway FAD biosynthesis and in Cofactor biosynthesis.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei133 – 1331ATP; via amide nitrogenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi19 – 202ATPUniRule annotation
Nucleotide bindingi24 – 274ATPUniRule annotation
Nucleotide bindingi104 – 1074ATPUniRule annotation

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Ligandi

ATP-binding, FAD, Flavoprotein, FMN, Nucleotide-binding

Enzyme and pathway databases

BioCyciMMAR79929:GH5J-1244-MONOMER.
UniPathwayiUPA00277; UER00407.

Names & Taxonomyi

Protein namesi
Recommended name:
FAD synthaseUniRule annotation (EC:2.7.7.2UniRule annotation)
Alternative name(s):
FMN adenylyltransferaseUniRule annotation
Flavin adenine dinucleotide synthaseUniRule annotation
Gene namesi
Name:ribLUniRule annotation
Ordered Locus Names:MTBMA_c12410
OrganismiMethanothermobacter marburgensis (strain DSM 2133 / 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium thermoautotrophicum)
Taxonomic identifieri79929 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanobacteriaMethanobacterialesMethanobacteriaceaeMethanothermobacter
ProteomesiUP000000345 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 161161FAD synthasePRO_0000406274Add
BLAST

Interactioni

Subunit structurei

Homodimer.UniRule annotation

Protein-protein interaction databases

STRINGi79929.MTBMA_c12410.

Family & Domainsi

Sequence similaritiesi

Belongs to the archaeal FAD synthase family.UniRule annotation

Phylogenomic databases

HOGENOMiHOG000284153.
KOiK14656.
OMAiVAHDETV.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_02115. FAD_synth_arch.
InterProiIPR004821. Cyt_trans-like.
IPR024902. FAD_synth_RibL.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF01467. CTP_transf_2. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00125. cyt_tran_rel. 1 hit.

Sequencei

Sequence statusi: Complete.

D9PX81-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKRFSDKRTQ IKTVMATGTF DIIHPGHGFF LEEAKKLGGE NARLVVVLAR
60 70 80 90 100
DSTVRARKRT PIIGEKQRLE VVMMLKPVDE AYLGSETDMF EIVHRLKPDI
110 120 130 140 150
IAIGPDQKFD IDELRDELRR RGLECEVKRV GKYRRSELDS TCKIIKKIRK
160
MEFDEDALKN C
Length:161
Mass (Da):18,664
Last modified:October 5, 2010 - v1
Checksum:i60C2822CE8D830C1
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001710 Genomic DNA. Translation: ADL58829.1.
RefSeqiWP_013296051.1. NC_014408.1.
YP_003850142.1. NC_014408.1.

Genome annotation databases

EnsemblBacteriaiADL58829; ADL58829; MTBMA_c12410.
GeneIDi9704949.
KEGGimmg:MTBMA_c12410.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
CP001710 Genomic DNA. Translation: ADL58829.1.
RefSeqiWP_013296051.1. NC_014408.1.
YP_003850142.1. NC_014408.1.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi79929.MTBMA_c12410.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiADL58829; ADL58829; MTBMA_c12410.
GeneIDi9704949.
KEGGimmg:MTBMA_c12410.

Phylogenomic databases

HOGENOMiHOG000284153.
KOiK14656.
OMAiVAHDETV.

Enzyme and pathway databases

UniPathwayiUPA00277; UER00407.
BioCyciMMAR79929:GH5J-1244-MONOMER.

Family and domain databases

Gene3Di3.40.50.620. 1 hit.
HAMAPiMF_02115. FAD_synth_arch.
InterProiIPR004821. Cyt_trans-like.
IPR024902. FAD_synth_RibL.
IPR014729. Rossmann-like_a/b/a_fold.
[Graphical view]
PfamiPF01467. CTP_transf_2. 1 hit.
[Graphical view]
TIGRFAMsiTIGR00125. cyt_tran_rel. 1 hit.
ProtoNetiSearch...

Publicationsi

  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.

Entry informationi

Entry nameiRIBL_METTM
AccessioniPrimary (citable) accession number: D9PX81
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 5, 2011
Last sequence update: October 5, 2010
Last modified: June 24, 2015
This is version 31 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.