ID   RIBF_PSEFL              Reviewed;         311 AA.
AC   P22990;
DT   01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1991, sequence version 1.
DT   03-AUG-2022, entry version 86.
DE   RecName: Full=Bifunctional riboflavin kinase/FMN adenylyltransferase {ECO:0000250|UniProtKB:Q59263};
DE   AltName: Full=Riboflavin biosynthesis protein RibF {ECO:0000250|UniProtKB:Q59263};
DE   Includes:
DE     RecName: Full=Riboflavin kinase {ECO:0000250|UniProtKB:Q59263};
DE              EC=2.7.1.26 {ECO:0000250|UniProtKB:Q59263};
DE     AltName: Full=Flavokinase {ECO:0000250|UniProtKB:Q59263};
DE   Includes:
DE     RecName: Full=FMN adenylyltransferase {ECO:0000250|UniProtKB:Q59263};
DE              EC=2.7.7.2 {ECO:0000250|UniProtKB:Q59263};
DE     AltName: Full=FAD pyrophosphorylase {ECO:0000250|UniProtKB:Q59263};
DE     AltName: Full=FAD synthase {ECO:0000250|UniProtKB:Q59263};
GN   Name=ribF;
OS   Pseudomonas fluorescens.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=294;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 49323 / NCIMB 10586;
RX   PubMed=2121716; DOI=10.1128/jb.172.11.6512-6517.1990;
RA   Isaki L., Beers R., Wu H.C.;
RT   "Nucleotide sequence of the Pseudomonas fluorescens signal peptidase II
RT   gene (lsp) and flanking genes.";
RL   J. Bacteriol. 172:6512-6517(1990).
CC   -!- FUNCTION: Catalyzes the phosphorylation of riboflavin to FMN followed
CC       by the adenylation of FMN to FAD. {ECO:0000250|UniProtKB:Q59263}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + riboflavin = ADP + FMN + H(+); Xref=Rhea:RHEA:14357,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:57986,
CC         ChEBI:CHEBI:58210, ChEBI:CHEBI:456216; EC=2.7.1.26;
CC         Evidence={ECO:0000250|UniProtKB:Q59263};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + FMN + H(+) = diphosphate + FAD; Xref=Rhea:RHEA:17237,
CC         ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC         ChEBI:CHEBI:57692, ChEBI:CHEBI:58210; EC=2.7.7.2;
CC         Evidence={ECO:0000250|UniProtKB:Q59263};
CC   -!- PATHWAY: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step
CC       1/1. {ECO:0000250|UniProtKB:Q59263}.
CC   -!- PATHWAY: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin
CC       (ATP route): step 1/1. {ECO:0000250|UniProtKB:Q59263}.
CC   -!- SIMILARITY: Belongs to the RibF family. {ECO:0000305}.
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DR   EMBL; M35367; AAA26021.1; -; Genomic_DNA.
DR   PIR; E37152; E37152.
DR   AlphaFoldDB; P22990; -.
DR   SMR; P22990; -.
DR   STRING; 690597.JH730966_gene5351; -.
DR   eggNOG; COG0196; Bacteria.
DR   UniPathway; UPA00276; UER00406.
DR   UniPathway; UPA00277; UER00407.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0003919; F:FMN adenylyltransferase activity; IEA:UniProtKB-EC.
DR   GO; GO:0008531; F:riboflavin kinase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006747; P:FAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0009398; P:FMN biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IEA:InterPro.
DR   CDD; cd02064; FAD_synthetase_N; 1.
DR   Gene3D; 2.40.30.30; -; 1.
DR   Gene3D; 3.40.50.620; -; 1.
DR   InterPro; IPR015864; FAD_synthase.
DR   InterPro; IPR023468; Riboflavin_kinase.
DR   InterPro; IPR002606; Riboflavin_kinase_bac.
DR   InterPro; IPR015865; Riboflavin_kinase_bac/euk.
DR   InterPro; IPR023465; Riboflavin_kinase_dom_sf.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR22749; PTHR22749; 1.
DR   Pfam; PF06574; FAD_syn; 1.
DR   Pfam; PF01687; Flavokinase; 1.
DR   PIRSF; PIRSF004491; FAD_Synth; 1.
DR   SMART; SM00904; Flavokinase; 1.
DR   SUPFAM; SSF82114; SSF82114; 1.
DR   TIGRFAMs; TIGR00083; ribF; 1.
PE   3: Inferred from homology;
KW   ATP-binding; FAD; Flavoprotein; FMN; Kinase; Multifunctional enzyme;
KW   Nucleotide-binding; Nucleotidyltransferase; Transferase.
FT   CHAIN           1..311
FT                   /note="Bifunctional riboflavin kinase/FMN
FT                   adenylyltransferase"
FT                   /id="PRO_0000194141"
SQ   SEQUENCE   311 AA;  33898 MW;  E4ED0EF97C064D60 CRC64;
     MQLVRGLHNL RPEHRGCVAT IGNFDGVHRG HQAILARLRE RAVELGVPSC VVIFEPQPRE
     FFTPETAPAR LALARQAATA GGEGVDRVLC LAFNQRLRSL SAAEFVDRIL VDGLGVQHLE
     VGDDFHFGCD RVGDFDFLQH AGVNQGFTVE AAQTVELDGL RVSSTQVRNA LAAADFDLAE
     RLLGRPFRIA GRVLHGQKLA RQLGTPTANV QLKRRRVPLT GVYLVSVDID GQSWPGVANI
     GVRPTVAGDG KAHLEVHLLD FAGDLYDRRL TVVFHQKLRE EQRFASLEAL KTAINADVAA
     ARALAAPSAH R