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P0AG40

- RIBF_ECOLI

UniProt

P0AG40 - RIBF_ECOLI

Protein

Riboflavin biosynthesis protein RibF

Gene

ribF

Organism
Escherichia coli (strain K12)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 77 (01 Oct 2014)
      Sequence version 1 (20 Dec 2005)
      Previous versions | rss
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    Functioni

    Catalytic activityi

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

    Pathwayi

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. FMN adenylyltransferase activity Source: EcoCyc
    3. riboflavin kinase activity Source: EcoCyc

    GO - Biological processi

    1. FAD biosynthetic process Source: UniProtKB-UniPathway
    2. FMN biosynthetic process Source: UniProtKB-UniPathway
    3. riboflavin biosynthetic process Source: InterPro

    Keywords - Molecular functioni

    Kinase, Nucleotidyltransferase, Transferase

    Keywords - Ligandi

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

    Enzyme and pathway databases

    BioCyciEcoCyc:RIBF-MONOMER.
    ECOL316407:JW0023-MONOMER.
    MetaCyc:RIBF-MONOMER.
    UniPathwayiUPA00276; UER00406.
    UPA00277; UER00407.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Riboflavin biosynthesis protein RibF
    Including the following 2 domains:
    Riboflavin kinase (EC:2.7.1.26)
    Alternative name(s):
    Flavokinase
    FMN adenylyltransferase (EC:2.7.7.2)
    Alternative name(s):
    FAD pyrophosphorylase
    FAD synthase
    Gene namesi
    Name:ribF
    Synonyms:yaaC
    Ordered Locus Names:b0025, JW0023
    OrganismiEscherichia coli (strain K12)
    Taxonomic identifieri83333 [NCBI]
    Taxonomic lineageiBacteriaProteobacteriaGammaproteobacteriaEnterobacterialesEnterobacteriaceaeEscherichia
    ProteomesiUP000000318: Chromosome, UP000000625: Chromosome

    Organism-specific databases

    EcoGeneiEG11079. ribF.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 313313Riboflavin biosynthesis protein RibFPRO_0000194137Add
    BLAST

    Proteomic databases

    PaxDbiP0AG40.
    PRIDEiP0AG40.

    Expressioni

    Gene expression databases

    GenevestigatoriP0AG40.

    Interactioni

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    aceEP0AFG81EBI-542969,EBI-542683

    Protein-protein interaction databases

    DIPiDIP-35789N.
    IntActiP0AG40. 10 interactions.
    MINTiMINT-1256514.
    STRINGi511145.b0025.

    Structurei

    3D structure databases

    ProteinModelPortaliP0AG40.
    SMRiP0AG40. Positions 19-306.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the RibF family.Curated

    Phylogenomic databases

    eggNOGiCOG0196.
    HOGENOMiHOG000006845.
    KOiK11753.
    OMAiGVASFGC.
    OrthoDBiEOG6QP0ZV.
    PhylomeDBiP0AG40.

    Family and domain databases

    Gene3Di2.40.30.30. 1 hit.
    3.40.50.620. 1 hit.
    InterProiIPR015864. FAD_synthase.
    IPR023468. Riboflavin_kinase.
    IPR002606. Riboflavin_kinase_bac.
    IPR015865. Riboflavin_kinase_bac/euk.
    IPR023465. Riboflavin_kinase_domain.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view]
    PANTHERiPTHR22749. PTHR22749. 1 hit.
    PfamiPF06574. FAD_syn. 1 hit.
    PF01687. Flavokinase. 1 hit.
    [Graphical view]
    PIRSFiPIRSF004491. FAD_Synth. 1 hit.
    SMARTiSM00904. Flavokinase. 1 hit.
    [Graphical view]
    SUPFAMiSSF82114. SSF82114. 1 hit.
    TIGRFAMsiTIGR00083. ribF. 1 hit.

    Sequencei

    Sequence statusi: Complete.

    P0AG40-1 [UniParc]FASTAAdd to Basket

    « Hide

    MKLIRGIHNL SQAPQEGCVL TIGNFDGVHR GHRALLQGLQ EEGRKRNLPV    50
    MVMLFEPQPL ELFATDKAPA RLTRLREKLR YLAECGVDYV LCVRFDRRFA 100
    ALTAQNFISD LLVKHLRVKF LAVGDDFRFG AGREGDFLLL QKAGMEYGFD 150
    ITSTQTFCEG GVRISSTAVR QALADDNLAL AESLLGHPFA ISGRVVHGDE 200
    LGRTIGFPTA NVPLRRQVSP VKGVYAVEVL GLGEKPLPGV ANIGTRPTVA 250
    GIRQQLEVHL LDVAMDLYGR HIQVVLRKKI RNEQRFASLD ELKAQIARDE 300
    LTAREFFGLT KPA 313
    Length:313
    Mass (Da):34,734
    Last modified:December 20, 2005 - v1
    Checksum:iC0B2EF5499CD30FE
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti108 – 1081I → V in AAA24605. (PubMed:2985604)Curated
    Sequence conflicti108 – 1081I → V no nucleotide entry (PubMed:1630901)Curated
    Sequence conflicti128 – 16942RFGAG…SSTAV → PLALVVKAISCYYRKLAWNT ASISPVRKLFAEVACASAAR L in AAA24605. (PubMed:2985604)CuratedAdd
    BLAST
    Sequence conflicti128 – 16942RFGAG…SSTAV → PLALVVKAISCYYRKLAWNT ASISPVRKLFAEVACASAAR L no nucleotide entry (PubMed:1630901)CuratedAdd
    BLAST
    Sequence conflicti214 – 2141L → P in AAA24605. (PubMed:2985604)Curated
    Sequence conflicti214 – 2141L → P no nucleotide entry (PubMed:1630901)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M10428 Genomic DNA. Translation: AAA24605.1.
    U00096 Genomic DNA. Translation: AAC73136.1.
    AP009048 Genomic DNA. Translation: BAB96594.2.
    PIRiA64723. QQECIL.
    RefSeqiNP_414566.1. NC_000913.3.
    YP_488331.1. NC_007779.1.

    Genome annotation databases

    EnsemblBacteriaiAAC73136; AAC73136; b0025.
    BAB96594; BAB96594; BAB96594.
    GeneIDi12932854.
    949129.
    KEGGiecj:Y75_p0025.
    eco:b0025.
    PATRICi32115141. VBIEscCol129921_0022.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M10428 Genomic DNA. Translation: AAA24605.1 .
    U00096 Genomic DNA. Translation: AAC73136.1 .
    AP009048 Genomic DNA. Translation: BAB96594.2 .
    PIRi A64723. QQECIL.
    RefSeqi NP_414566.1. NC_000913.3.
    YP_488331.1. NC_007779.1.

    3D structure databases

    ProteinModelPortali P0AG40.
    SMRi P0AG40. Positions 19-306.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    DIPi DIP-35789N.
    IntActi P0AG40. 10 interactions.
    MINTi MINT-1256514.
    STRINGi 511145.b0025.

    Proteomic databases

    PaxDbi P0AG40.
    PRIDEi P0AG40.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    EnsemblBacteriai AAC73136 ; AAC73136 ; b0025 .
    BAB96594 ; BAB96594 ; BAB96594 .
    GeneIDi 12932854.
    949129.
    KEGGi ecj:Y75_p0025.
    eco:b0025.
    PATRICi 32115141. VBIEscCol129921_0022.

    Organism-specific databases

    EchoBASEi EB1071.
    EcoGenei EG11079. ribF.

    Phylogenomic databases

    eggNOGi COG0196.
    HOGENOMi HOG000006845.
    KOi K11753.
    OMAi GVASFGC.
    OrthoDBi EOG6QP0ZV.
    PhylomeDBi P0AG40.

    Enzyme and pathway databases

    UniPathwayi UPA00276 ; UER00406 .
    UPA00277 ; UER00407 .
    BioCyci EcoCyc:RIBF-MONOMER.
    ECOL316407:JW0023-MONOMER.
    MetaCyc:RIBF-MONOMER.

    Miscellaneous databases

    PROi P0AG40.

    Gene expression databases

    Genevestigatori P0AG40.

    Family and domain databases

    Gene3Di 2.40.30.30. 1 hit.
    3.40.50.620. 1 hit.
    InterProi IPR015864. FAD_synthase.
    IPR023468. Riboflavin_kinase.
    IPR002606. Riboflavin_kinase_bac.
    IPR015865. Riboflavin_kinase_bac/euk.
    IPR023465. Riboflavin_kinase_domain.
    IPR014729. Rossmann-like_a/b/a_fold.
    [Graphical view ]
    PANTHERi PTHR22749. PTHR22749. 1 hit.
    Pfami PF06574. FAD_syn. 1 hit.
    PF01687. Flavokinase. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF004491. FAD_Synth. 1 hit.
    SMARTi SM00904. Flavokinase. 1 hit.
    [Graphical view ]
    SUPFAMi SSF82114. SSF82114. 1 hit.
    TIGRFAMsi TIGR00083. ribF. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Characterization of the ileS-lsp operon in Escherichia coli. Identification of an open reading frame upstream of the ileS gene and potential promoter(s) for the ileS-lsp operon."
      Kamio Y., Lin C.-K., Regue M., Wu H.C.
      J. Biol. Chem. 260:5616-5620(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    2. "Systematic sequencing of the Escherichia coli genome: analysis of the 0-2.4 min region."
      Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K., Mizobuchi K., Nakata A.
      Nucleic Acids Res. 20:3305-3308(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: K12 / MG1655 / ATCC 47076.
    4. "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110."
      Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.
      Mol. Syst. Biol. 2:E1-E5(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], SEQUENCE REVISION TO 108; 128-169 AND 214.
      Strain: K12 / W3110 / ATCC 27325 / DSM 5911.

    Entry informationi

    Entry nameiRIBF_ECOLI
    AccessioniPrimary (citable) accession number: P0AG40
    Secondary accession number(s): P08391, P75621
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 1, 1988
    Last sequence update: December 20, 2005
    Last modified: October 1, 2014
    This is version 77 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, Reference proteome

    Documents

    1. Escherichia coli
      Escherichia coli (strain K12): entries and cross-references to EcoGene
    2. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    3. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3