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Q58579

- RIBL_METJA

UniProt

Q58579 - RIBL_METJA

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: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 78 (01 Oct 2014)
      Sequence version 1 (01 Nov 1996)
      Previous versions | rss
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    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

    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

    Vmax=14 nmol/min/mg enzyme with ATP and FMN as substrates1 Publication

    Vmax=10 nmol/min/mg enzyme with CTP and FMN as substrates1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei123 – 1231ATP; via amide nitrogenBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Nucleotide bindingi10 – 112ATPBy similarity
    Nucleotide bindingi15 – 184ATPBy similarity
    Nucleotide bindingi93 – 964ATPBy similarity

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB
    2. CTP binding Source: UniProtKB
    3. FMN adenylyltransferase activity Source: UniProtKB
    4. FMN binding Source: UniProtKB
    5. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. FAD biosynthetic process Source: UniProtKB
    2. FMN metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Nucleotidyltransferase, Transferase

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BioCyciMetaCyc:MONOMER-16487.
    UniPathwayiUPA00277; UER00407.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    FAD synthase (EC:2.7.7.2)
    Alternative name(s):
    FMN adenylyltransferase
    Flavin adenine dinucleotide synthase
    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
    ProteomesiUP000000805: Chromosome

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi126 – 1261C → S: 2-fold increase in activity with Mg(2+) but loss of activity with Co(2+) as cofactor. 1 Publication
    Mutagenesisi143 – 1431C → S: Nearly no change in activity with Mg(2+) but loss of activity with Co(2+) as cofactor. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 149149FAD synthasePRO_0000107202Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    STRINGi243232.MJ1179.

    Structurei

    3D structure databases

    ProteinModelPortaliQ58579.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the archaeal FAD synthase family.Curated

    Phylogenomic databases

    eggNOGiCOG0615.
    KOiK14656.
    OMAiFAKKHAD.
    PhylomeDBiQ58579.

    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.

    Q58579-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKKRVVTAGT FDILHPGHYE ILKFAKSLGD ELIVIVARDE TVKKLKGRKP    50
    IIPEEQRREM VEALKPVDKA ILGSLKNKLE PILELKPDII VLGPDQTTFD 100
    EETLKKELAK YNLYPEIVRF RGYKKCPFHS SFDIVKEIIR RFCNKEIKI 149
    Length:149
    Mass (Da):17,288
    Last modified:November 1, 1996 - v1
    Checksum:i55FD11671ED94594
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L77117 Genomic DNA. Translation: AAB99182.1.
    PIRiB64447.
    RefSeqiNP_248173.1. NC_000909.1.

    Genome annotation databases

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

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    L77117 Genomic DNA. Translation: AAB99182.1 .
    PIRi B64447.
    RefSeqi NP_248173.1. NC_000909.1.

    3D structure databases

    ProteinModelPortali Q58579.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    STRINGi 243232.MJ1179.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAB99182 ; AAB99182 ; MJ_1179 .
    GeneIDi 1452077.
    KEGGi mja:MJ_1179.

    Phylogenomic databases

    eggNOGi COG0615.
    KOi K14656.
    OMAi FAKKHAD.
    PhylomeDBi Q58579.

    Enzyme and pathway databases

    UniPathwayi UPA00277 ; UER00407 .
    BioCyci MetaCyc:MONOMER-16487.

    Family and domain databases

    Gene3Di 3.40.50.620. 1 hit.
    HAMAPi MF_02115. FAD_synth_arch.
    InterProi IPR004821. Cyt_trans-like.
    IPR024902. FAD_synth_RibL.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view ]
    Pfami PF01467. CTP_transf_2. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR00125. cyt_tran_rel. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.
    2. "Archaeal RibL: a new FAD synthetase that is air sensitive."
      Mashhadi Z., Xu H., Grochowski L.L., White R.H.
      Biochemistry 49:8748-8755(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, KINETIC PARAMETERS, ENZYME REGULATION, GENE NAME, PATHWAY, SUBUNIT, MUTAGENESIS OF CYS-126 AND CYS-143.
      Strain: ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440.

    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 1, 2014
    This is version 78 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.

    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

    External Data

    Dasty 3