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Protein

Putative riboflavin biosynthesis protein RibF

Gene

ribF

Organism
Geobacillus thermodenitrificans (strain NG80-2)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Catalytic activityi

ATP + riboflavin = ADP + FMN.1 Publication
ATP + FMN = diphosphate + FAD.1 Publication

Kineticsi

    1. Vmax=270.3 µmol/min/mg enzyme toward FMN1 Publication
    2. Vmax=170.09 µmol/min/mg enzyme toward riboflavin1 Publication

    Pathway:iFAD biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes FAD from FMN.By similarity
    Proteins known to be involved in this subpathway in this organism are:
    1. Putative riboflavin biosynthesis protein RibF (ribF), Riboflavin biosynthesis protein (GTNG_1121)
    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.

    Pathway:iFMN biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes FMN from riboflavin (ATP route).By similarity
    Proteins known to be involved in this subpathway in this organism are:
    1. Putative riboflavin biosynthesis protein RibF (ribF), Riboflavin biosynthesis protein (GTNG_1121)
    This subpathway is part of the pathway FMN 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 FMN from riboflavin (ATP route), the pathway FMN biosynthesis and in Cofactor biosynthesis.

    GO - Molecular functioni

    GO - Biological processi

    Complete GO annotation...

    Keywords - Molecular functioni

    Kinase, Nucleotidyltransferase, Transferase

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BioCyciGTHE420246:GIXT-3255-MONOMER.
    UniPathwayiUPA00276; UER00406.
    UPA00277; UER00407.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Putative riboflavin biosynthesis protein RibF
    Including the following 2 domains:
    Riboflavin kinase1 Publication (EC:2.7.1.261 Publication)
    Alternative name(s):
    FlavokinaseBy similarity
    FMN adenylyltransferase1 Publication (EC:2.7.7.21 Publication)
    Alternative name(s):
    FAD pyrophosphorylaseBy similarity
    FAD synthaseBy similarity
    Gene namesi
    Name:ribF
    Ordered Locus Names:GTNG_3159
    OrganismiGeobacillus thermodenitrificans (strain NG80-2)
    Taxonomic identifieri420246 [NCBI]
    Taxonomic lineageiBacteriaFirmicutesBacilliBacillalesBacillaceaeGeobacillus
    ProteomesiUP000001578 Componenti: Chromosome

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 179179Putative riboflavin biosynthesis protein RibFPRO_0000421234Add
    BLAST

    Interactioni

    Protein-protein interaction databases

    STRINGi420246.GTNG_3159.

    Structurei

    3D structure databases

    ProteinModelPortaliA4IT50.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the RibF family.Sequence Analysis

    Phylogenomic databases

    eggNOGiCOG0196.
    HOGENOMiHOG000088656.
    OMAiSEIWISP.
    OrthoDBiEOG6QP0ZV.

    Family and domain databases

    Gene3Di3.40.50.620. 1 hit.
    InterProiIPR015864. FAD_synthase.
    IPR023468. Riboflavin_kinase.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view]
    PANTHERiPTHR22749. PTHR22749. 1 hit.
    PfamiPF06574. FAD_syn. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    A4IT50-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MKVHEANQGL TLPGSVVAIG AFDGVHQGHQ AVLRQAVERS RQLGVESVAY
    60 70 80 90 100
    TIDPPPRCRF QGSRMLTTLQ EKLDRFAVLG LNHAVVAHFD ERYAARRVDA
    110 120 130 140 150
    FIRELTALNP REVIVGQDFR FGRNREGDVA LLRRHFPVRI VQTVCCADGQ
    160 170
    RISSTRIREL IERGEWEQST VLLGWPLSS
    Length:179
    Mass (Da):20,167
    Last modified:May 1, 2007 - v1
    Checksum:i78CC00E8A22FCE33
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000557 Genomic DNA. Translation: ABO68504.1.
    RefSeqiWP_011888288.1. NC_009328.1.

    Genome annotation databases

    EnsemblBacteriaiABO68504; ABO68504; GTNG_3159.
    KEGGigtn:GTNG_3159.
    PATRICi21982961. VBIGeoThe136879_3323.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    CP000557 Genomic DNA. Translation: ABO68504.1.
    RefSeqiWP_011888288.1. NC_009328.1.

    3D structure databases

    ProteinModelPortaliA4IT50.
    ModBaseiSearch...
    MobiDBiSearch...

    Protein-protein interaction databases

    STRINGi420246.GTNG_3159.

    Protocols and materials databases

    Structural Biology KnowledgebaseSearch...

    Genome annotation databases

    EnsemblBacteriaiABO68504; ABO68504; GTNG_3159.
    KEGGigtn:GTNG_3159.
    PATRICi21982961. VBIGeoThe136879_3323.

    Phylogenomic databases

    eggNOGiCOG0196.
    HOGENOMiHOG000088656.
    OMAiSEIWISP.
    OrthoDBiEOG6QP0ZV.

    Enzyme and pathway databases

    UniPathwayiUPA00276; UER00406.
    UPA00277; UER00407.
    BioCyciGTHE420246:GIXT-3255-MONOMER.

    Family and domain databases

    Gene3Di3.40.50.620. 1 hit.
    InterProiIPR015864. FAD_synthase.
    IPR023468. Riboflavin_kinase.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view]
    PANTHERiPTHR22749. PTHR22749. 1 hit.
    PfamiPF06574. FAD_syn. 1 hit.
    [Graphical view]
    ProtoNetiSearch...

    Publicationsi

    « Hide 'large scale' publications
    1. "Genome and proteome of long-chain alkane degrading Geobacillus thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir."
      Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X., Han W., Peng X., Liu R., Wang L.
      Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: NG80-2.
    2. "Characterization of the anthranilate degradation pathway in Geobacillus thermodenitrificans NG80-2."
      Liu X., Dong Y., Li X., Ren Y., Li Y., Wang W., Wang L., Feng L.
      Microbiology 156:589-595(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES.
      Strain: NG80-21 Publication.

    Entry informationi

    Entry nameiRIBF_GEOTN
    AccessioniPrimary (citable) accession number: A4IT50
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 6, 2013
    Last sequence update: May 1, 2007
    Last modified: July 22, 2015
    This is version 46 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, Multifunctional enzyme

    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.