ID   RIBF_RHOOP              Reviewed;         248 AA.
AC   O84990;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 66.
DE   RecName: Full=Putative bifunctional riboflavin kinase/FMN adenylyltransferase {ECO:0000250|UniProtKB:A4IT50};
DE   AltName: Full=Putative riboflavin biosynthesis protein RibF {ECO:0000250|UniProtKB:A4IT50};
DE   Includes:
DE     RecName: Full=Riboflavin kinase {ECO:0000250|UniProtKB:A4IT50};
DE              EC=2.7.1.26 {ECO:0000250|UniProtKB:A4IT50};
DE     AltName: Full=Flavokinase {ECO:0000250|UniProtKB:Q59263};
DE   Includes:
DE     RecName: Full=FMN adenylyltransferase {ECO:0000250|UniProtKB:A4IT50};
DE              EC=2.7.7.2 {ECO:0000250|UniProtKB:A4IT50};
DE     AltName: Full=FAD pyrophosphorylase {ECO:0000250|UniProtKB:Q59263};
DE     AltName: Full=FAD synthase {ECO:0000250|UniProtKB:Q59263};
GN   Name=ribF;
OS   Rhodococcus opacus (Nocardia opaca).
OC   Bacteria; Actinobacteria; Corynebacteriales; Nocardiaceae; Rhodococcus.
OX   NCBI_TaxID=37919;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=1CP;
RX   PubMed=9657989; DOI=10.1128/jb.180.14.3503-3508.1998;
RA   Seibert V., Kourbatova E.M., Golovleva L.A., Schloemann M.;
RT   "Characterization of the maleylacetate reductase MacA of Rhodococcus opacus
RT   1CP and evidence for the presence of an isofunctional enzyme.";
RL   J. Bacteriol. 180:3503-3508(1998).
CC   -!- FUNCTION: Catalyzes the phosphorylation of riboflavin to FMN followed
CC       by the adenylation of FMN to FAD. {ECO:0000250|UniProtKB:A4IT50}.
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:A4IT50};
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:A4IT50};
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}.
CC   -!- CAUTION: This sequence is divergent compared to other bacterial RibF.
CC       {ECO:0000305}.
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DR   EMBL; AF030176; AAC38800.1; -; Genomic_DNA.
DR   AlphaFoldDB; O84990; -.
DR   SMR; O84990; -.
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; 3.40.50.620; -; 1.
DR   InterPro; IPR015864; FAD_synthase.
DR   InterPro; IPR023468; Riboflavin_kinase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR22749; PTHR22749; 1.
DR   Pfam; PF06574; FAD_syn; 1.
PE   3: Inferred from homology;
KW   ATP-binding; FAD; Flavoprotein; FMN; Kinase; Multifunctional enzyme;
KW   Nucleotide-binding; Nucleotidyltransferase; Transferase.
FT   CHAIN           1..248
FT                   /note="Putative bifunctional riboflavin kinase/FMN
FT                   adenylyltransferase"
FT                   /id="PRO_0000194142"
SQ   SEQUENCE   248 AA;  26703 MW;  7869F5B3D244B56A CRC64;
     MPVAEATTAT GLASHNGRQS GVAIGAFDGV HLGHRQVLVG CDTVLTFDPH PMHVLAPRPA
     LRLLSDRRTK LRKLEALGIR RVAFIPFDEG WSRVTADDFV ERVVIDRLHA SRVSVGANFR
     FGAHGVGTPE TFNNYQSLQT RVVQLVQRGP GAEPISSTRI RKLVAAGNIE DAIDLLGGPF
     SLPAVAVSES RLVIADEFAL PAPGLYSAQV DGNAVSLRTF IEGVVELTHP ASLQRDTTVE
     VSFLNRMA