ID   RIBF_MYCPN              Reviewed;         269 AA.
AC   P75587;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1997, sequence version 1.
DT   04-NOV-2026, entry version 118.
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; OrderedLocusNames=MPN_158; ORFNames=MP673;
OS   Mycoplasmoides pneumoniae (strain ATCC 29342 / M129 / Subtype 1)
OS   (Mycoplasma pneumoniae).
OC   Bacteria; Bacillati; Mycoplasmatota; Mycoplasmoidales; Mycoplasmoidaceae;
OC   Mycoplasmoides.
OX   NCBI_TaxID=272634;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29342 / M129 / Subtype 1;
RX   PubMed=8948633; DOI=10.1093/nar/24.22.4420;
RA   Himmelreich R., Hilbert H., Plagens H., Pirkl E., Li B.-C., Herrmann R.;
RT   "Complete sequence analysis of the genome of the bacterium Mycoplasma
RT   pneumoniae.";
RL   Nucleic Acids Res. 24:4420-4449(1996).
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=riboflavin + ATP = FMN + ADP + 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=FMN + ATP + H(+) = FAD + diphosphate; 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; U00089; AAB96321.1; -; Genomic_DNA.
DR   PIR; S73999; S73999.
DR   RefSeq; WP_010874515.1; NC_000912.1.
DR   AlphaFoldDB; P75587; -.
DR   SMR; P75587; -.
DR   IntAct; P75587; 1.
DR   STRING; 272634.MPN_158; -.
DR   PaxDb; 272634-MPN_158; -.
DR   EnsemblBacteria; AAB96321; AAB96321; MPN_158.
DR   GeneID; 66609194; -.
DR   KEGG; mpn:MPN_158; -.
DR   PATRIC; fig|272634.6.peg.176; -.
DR   HOGENOM; CLU_048437_0_2_14; -.
DR   OMA; AACCVMT; -.
DR   OrthoDB; 9803667at2; -.
DR   BioCyc; MPNE272634:G1GJ3-265-MONOMER; -.
DR   UniPathway; UPA00276; UER00406.
DR   UniPathway; UPA00277; UER00407.
DR   Proteomes; UP000000808; Chromosome.
DR   GO; GO:0003919; F:FMN adenylyltransferase activity; ISS:UniProtKB.
DR   GO; GO:0008531; F:riboflavin kinase activity; ISS:UniProtKB.
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:0009231; P:riboflavin biosynthetic process; IEA:InterPro.
DR   CDD; cd02064; FAD_synthetase_N; 1.
DR   Gene3D; 3.40.50.620; HUPs; 1.
DR   Gene3D; 2.40.30.30; Riboflavin kinase-like; 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   NCBIfam; TIGR00083; ribF; 1.
DR   PANTHER; PTHR22749:SF6; RIBOFLAVIN KINASE; 1.
DR   PANTHER; PTHR22749; RIBOFLAVIN KINASE/FMN ADENYLYLTRANSFERASE; 1.
DR   Pfam; PF01687; Flavokinase; 1.
DR   PIRSF; PIRSF004491; FAD_Synth; 1.
DR   SMART; SM00904; Flavokinase; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR   SUPFAM; SSF82114; Riboflavin kinase-like; 1.
PE   3: Inferred from homology;
KW   ATP-binding; FAD; Flavoprotein; FMN; Kinase; Multifunctional enzyme;
KW   Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW   Transferase.
FT   CHAIN           1..269
FT                   /note="Bifunctional riboflavin kinase/FMN
FT                   adenylyltransferase"
FT                   /id="PRO_0000194146"
SQ   SEQUENCE   269 AA;  30435 MW;  2E63D7BC7A8FA12D CRC64;
     MQQTLIIGAF DGLHKGHQLL AQAASGPVVA LLIANIPSLQ SDWLYEPKQR QVQLQQHFQS
     VVHSYDVIEH NISAQAFFDQ IISPLRCQQL VVGADFCFGK DNQNADFLRR LFPNTTIIPK
     DSQTLSSSTI RQWLKQGQIE QANAVLLEPY FREGVVIRGN QQARFLGWPT ANITLKPYMV
     PLRCGSYVIT VTYHQTNYPG VGFISYKNDQ LVCETHLIGF SGDLYGKQLR FTFNQFIRPQ
     QKFSGVQALQ KAISGDLKQA QKWFAQSTN
//