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Protein

FAD synthase

Gene

ribL

Organism
Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Catalyzes the transfer of the AMP portion of ATP to flavin mononucleotide (FMN) to produce flavin adenine dinucleotide (FAD) coenzyme. To a lesser extent, is also able to utilize other nucleotides such as CTP and GTP as substrates, producing the modified coenzymes, flavin cytosine dinucleotide (FCD) and flavin guanine dinucleotide (FGD), respectively. Does not catalyze the reverse reaction to produce FMN and ATP from FAD and PPi. Does not function as a glycerol-3-phosphate cytidylyltransferase, as previously annotated in the complete genome.1 Publication

Catalytic activityi

ATP + FMN = diphosphate + FAD.1 Publication

Cofactori

Co2+1 PublicationNote: Divalent metal cations. The best activity is observed with Co2+, where the activity is 4 and 2.5 times greater than that with Mg2+ and Mn2+, respectively.1 Publication

Enzyme regulationi

Is inhibited by the product PPi.1 Publication

Kineticsi

  1. KM=25 µM for ATP1 Publication
  2. KM=63 µM for FMN1 Publication
  3. KM=480 µM for CTP1 Publication
  1. Vmax=14 nmol/min/mg enzyme with ATP and FMN as substrates1 Publication
  2. Vmax=10 nmol/min/mg enzyme with CTP and FMN as substrates1 Publication

Pathwayi: FAD biosynthesis

This protein is involved in step 1 of the subpathway that synthesizes FAD from FMN.1 Publication
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)DescriptionActionsGraphical viewLength
Binding sitei95ATPUniRule annotation1
Binding sitei123ATP; via amide nitrogenUniRule annotation1

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi10 – 11ATPUniRule annotation2
Nucleotide bindingi15 – 18ATPUniRule annotation4

GO - Molecular functioni

  • ATP binding Source: UniProtKB
  • CTP binding Source: UniProtKB
  • FMN adenylyltransferase activity Source: UniProtKB
  • FMN binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • FAD biosynthetic process Source: UniProtKB
  • FMN metabolic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Ligandi

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

Enzyme and pathway databases

BioCyciMetaCyc:MONOMER-16487.
BRENDAi2.7.7.2. 3260.
UniPathwayiUPA00277; UER00407.

Names & Taxonomyi

Protein namesi
Recommended name:
FAD synthaseUniRule annotation (EC:2.7.7.21 Publication)
Alternative name(s):
FMN adenylyltransferaseUniRule annotation
Flavin adenine dinucleotide synthaseUniRule annotation
Gene namesi
Name:ribL
Ordered Locus Names:MJ1179
OrganismiMethanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440) (Methanococcus jannaschii)
Taxonomic identifieri243232 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaMethanococciMethanococcalesMethanocaldococcaceaeMethanocaldococcus
Proteomesi
  • UP000000805 Componenti: Chromosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi126C → S: 2-fold increase in activity with Mg(2+) but loss of activity with Co(2+) as cofactor. 1 Publication1
Mutagenesisi143C → S: Nearly no change in activity with Mg(2+) but loss of activity with Co(2+) as cofactor. 1 Publication1

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001072021 – 149FAD synthaseAdd BLAST149

Interactioni

Subunit structurei

Homodimer.1 Publication

GO - Molecular functioni

  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

STRINGi243232.MJ_1179.

Structurei

3D structure databases

ProteinModelPortaliQ58579.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the archaeal FAD synthase family.Curated

Phylogenomic databases

eggNOGiarCOG01222. Archaea.
COG0615. LUCA.
InParanoidiQ58579.
KOiK14656.
OMAiFAKKHAD.
PhylomeDBiQ58579.

Family and domain databases

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

Sequencei

Sequence statusi: Complete.

Q58579-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKKRVVTAGT FDILHPGHYE ILKFAKSLGD ELIVIVARDE TVKKLKGRKP
60 70 80 90 100
IIPEEQRREM VEALKPVDKA ILGSLKNKLE PILELKPDII VLGPDQTTFD
110 120 130 140
EETLKKELAK YNLYPEIVRF RGYKKCPFHS SFDIVKEIIR RFCNKEIKI
Length:149
Mass (Da):17,288
Last modified:November 1, 1996 - v1
Checksum:i55FD11671ED94594
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB99182.1.
PIRiB64447.
RefSeqiWP_010870692.1. NC_000909.1.

Genome annotation databases

EnsemblBacteriaiAAB99182; AAB99182; MJ_1179.
GeneIDi1452077.
KEGGimja:MJ_1179.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L77117 Genomic DNA. Translation: AAB99182.1.
PIRiB64447.
RefSeqiWP_010870692.1. NC_000909.1.

3D structure databases

ProteinModelPortaliQ58579.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi243232.MJ_1179.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAB99182; AAB99182; MJ_1179.
GeneIDi1452077.
KEGGimja:MJ_1179.

Phylogenomic databases

eggNOGiarCOG01222. Archaea.
COG0615. LUCA.
InParanoidiQ58579.
KOiK14656.
OMAiFAKKHAD.
PhylomeDBiQ58579.

Enzyme and pathway databases

UniPathwayiUPA00277; UER00407.
BioCyciMetaCyc:MONOMER-16487.
BRENDAi2.7.7.2. 3260.

Family and domain databases

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

Entry informationi

Entry nameiRIBL_METJA
AccessioniPrimary (citable) accession number: Q58579
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 16, 2004
Last sequence update: November 1, 1996
Last modified: October 5, 2016
This is version 89 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Alkylation of both Cys-126 and Cys-143 results in complete loss of enzymatic activity.1 Publication

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Methanococcus jannaschii
    Methanococcus jannaschii: entries and gene names
  2. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  3. SIMILARITY comments
    Index of protein domains and families

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 one 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.