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Protein

Bifunctional riboflavin kinase/FMN adenylyltransferase

Gene

ribF

Organism
Corynebacterium ammoniagenes (Brevibacterium ammoniagenes)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Catalyzes the phosphorylation of riboflavin to FMN followed by the adenylation of FMN to FAD.1 Publication

Catalytic activityi

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

Cofactori

a divalent metal cation1 Publication

Enzyme regulationi

Higher divalent cation concentrations lead to decrease in the turnover of riboflavin and the 5'-phosphotransferase activity, while the adenylyltransferase activity increases.1 Publication

Kineticsi

  1. KM=5 µM for Mg-ATP (for riboflavin kinase activity)1 Publication
  2. KM=160 µM for Mg-ATP (for FMN adenylyltransferase activity)1 Publication

    pH dependencei

    With magnesium ions the highest turnover of riboflavin is observed between pH 6 and 7.5, while that of FAD is between 7.0 and 9.0. With zinc ions a steady increase in riboflavin turnover is observed between pH 4.5 and 10, while FAD is the major product at pH 7.0 and decreases rapidly above pH 8.0.1 Publication

    Pathwayi: FAD biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes FAD from FMN.Curated
    Proteins known to be involved in this subpathway in this organism are:
    1. Bifunctional riboflavin kinase/FMN adenylyltransferase (ribF)
    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.

    Pathwayi: FMN biosynthesis

    This protein is involved in step 1 of the subpathway that synthesizes FMN from riboflavin (ATP route).Curated
    Proteins known to be involved in this subpathway in this organism are:
    1. Bifunctional riboflavin kinase/FMN adenylyltransferase (ribF)
    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

    Keywordsi

    Molecular functionKinase, Multifunctional enzyme, Nucleotidyltransferase, Transferase
    LigandATP-binding, FAD, Flavoprotein, FMN, Nucleotide-binding

    Enzyme and pathway databases

    BRENDAi2.7.1.26 959
    2.7.7.2 959
    UniPathwayiUPA00276; UER00406
    UPA00277; UER00407

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Bifunctional riboflavin kinase/FMN adenylyltransferaseCurated
    Alternative name(s):
    Riboflavin biosynthesis protein RibFCurated
    Including the following 2 domains:
    Riboflavin kinaseCurated (EC:2.7.1.261 Publication)
    Alternative name(s):
    FlavokinaseCurated
    FMN adenylyltransferaseCurated (EC:2.7.7.21 Publication)
    Alternative name(s):
    FAD pyrophosphorylaseCurated
    FAD synthaseCurated
    Gene namesi
    Name:ribF
    OrganismiCorynebacterium ammoniagenes (Brevibacterium ammoniagenes)
    Taxonomic identifieri1697 [NCBI]
    Taxonomic lineageiBacteriaActinobacteriaCorynebacterialesCorynebacteriaceaeCorynebacterium

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    ChainiPRO_00001941361 – 338Bifunctional riboflavin kinase/FMN adenylyltransferaseAdd BLAST338

    Structurei

    Secondary structure

    1338
    Legend: HelixTurnBeta strandPDB Structure known for this area
    Show more details
    Feature keyPosition(s)DescriptionActionsGraphical viewLength
    Beta strandi2 – 6Combined sources5
    Helixi7 – 9Combined sources3
    Beta strandi17 – 22Combined sources6
    Helixi29 – 45Combined sources17
    Beta strandi48 – 56Combined sources9
    Helixi58 – 62Combined sources5
    Beta strandi70 – 72Combined sources3
    Helixi74 – 83Combined sources10
    Beta strandi87 – 92Combined sources6
    Turni94 – 96Combined sources3
    Beta strandi97 – 100Combined sources4
    Helixi103 – 109Combined sources7
    Helixi110 – 114Combined sources5
    Beta strandi117 – 123Combined sources7
    Beta strandi127 – 129Combined sources3
    Helixi130 – 132Combined sources3
    Helixi136 – 142Combined sources7
    Turni143 – 146Combined sources4
    Beta strandi147 – 152Combined sources6
    Helixi164 – 172Combined sources9
    Helixi176 – 183Combined sources8
    Beta strandi188 – 192Combined sources5
    Helixi200 – 204Combined sources5
    Beta strandi209 – 212Combined sources4
    Beta strandi222 – 231Combined sources10
    Beta strandi239 – 241Combined sources3
    Beta strandi247 – 255Combined sources9
    Turni258 – 260Combined sources3
    Beta strandi266 – 271Combined sources6
    Beta strandi282 – 292Combined sources11
    Helixi300 – 324Combined sources25
    Turni325 – 327Combined sources3
    Helixi329 – 331Combined sources3

    3D structure databases

    Select the link destinations:
    PDBei
    RCSB PDBi
    PDBji
    Links Updated
    PDB entryMethodResolution (Å)ChainPositionsPDBsum
    2X0KX-ray1.95A/B1-338[»]
    3ZUGX-ray2.05A/B1-338[»]
    4UZEX-ray2.34A/B1-338[»]
    4UZFX-ray2.52A/B1-338[»]
    5A88X-ray2.08A/B/C/D183-338[»]
    5A89X-ray1.65A/B183-338[»]
    5A8AX-ray1.80A/B183-338[»]
    5FNZX-ray2.52A/B1-338[»]
    5FO0X-ray2.51A/B1-338[»]
    5FO1X-ray2.45A/B1-338[»]
    ProteinModelPortaliQ59263
    SMRiQ59263
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ59263

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the RibF family.Curated

    Family and domain databases

    Gene3Di2.40.30.30, 1 hit
    3.40.50.620, 1 hit
    InterProiView protein in InterPro
    IPR015864 FAD_synthase
    IPR023468 Riboflavin_kinase
    IPR002606 Riboflavin_kinase_bac
    IPR015865 Riboflavin_kinase_bac/euk
    IPR023465 Riboflavin_kinase_dom_sf
    IPR014729 Rossmann-like_a/b/a_fold
    PANTHERiPTHR22749 PTHR22749, 1 hit
    PfamiView protein in Pfam
    PF06574 FAD_syn, 1 hit
    PF01687 Flavokinase, 1 hit
    PIRSFiPIRSF004491 FAD_Synth, 1 hit
    SMARTiView protein in SMART
    SM00904 Flavokinase, 1 hit
    SUPFAMiSSF82114 SSF82114, 1 hit
    TIGRFAMsiTIGR00083 ribF, 1 hit

    Sequencei

    Sequence statusi: Complete.

    Q59263-1 [UniParc]FASTAAdd to basket

    « Hide

            10         20         30         40         50
    MDIWYGTAAV PKDLDNSAVT IGVFDGVHRG HQKLINATVE KAREVGAKAI
    60 70 80 90 100
    MVTFDPHPVS VFLPRRAPLG ITTLAERFAL AESFGIDGVL VIDFTRELSG
    110 120 130 140 150
    TSPEKYVEFL LEDTLHASHV VVGANFTFGE NAAGTADSLR QICQSRLTVD
    160 170 180 190 200
    VIDLLDDEGV RISSTTVREF LSEGDVARAN WALGRHFYVT GPVVRGAGRG
    210 220 230 240 250
    GKELGFPTAN QYFHDTVALP ADGVYAGWLT ILPTEAPVSG NMEPEVAYAA
    260 270 280 290 300
    AISVGTNPTF GDEQRSVESF VLDRDADLYG HDVKVEFVDH VRAMEKFDSV
    310 320 330
    EQLLEVMAKD VQKTRTLLAQ DVQAHKMAPE TYFLQAES
    Length:338
    Mass (Da):36,844
    Last modified:November 1, 1996 - v1
    Checksum:iB714FD885412CC68
    GO

    Sequence databases

    Select the link destinations:
    EMBLi
    GenBanki
    DDBJi
    Links Updated
    D37967 Genomic DNA Translation: BAA07182.1
    PIRiJC4008

    Similar proteinsi

    Entry informationi

    Entry nameiRIBF_CORAM
    AccessioniPrimary (citable) accession number: Q59263
    Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: November 1, 1996
    Last modified: April 25, 2018
    This is version 82 of the entry and version 1 of the sequence. See complete history.
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programProkaryotic Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Direct protein sequencing

    Documents

    1. PATHWAY comments
      Index of metabolic and biosynthesis pathways
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. SIMILARITY comments
      Index of protein domains and families
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    Main funding by: National Institutes of Health