RIBF_MYCPN
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 03-AUG-2022, entry version 105.
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 Mycoplasma pneumoniae (strain ATCC 29342 / M129) (Mycoplasmoides
OS pneumoniae).
OC Bacteria; Tenericutes; Mollicutes; Mycoplasmataceae; Mycoplasma.
OX NCBI_TaxID=272634;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29342 / M129;
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=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; U00089; AAB96321.1; -; Genomic_DNA.
DR PIR; S73999; S73999.
DR RefSeq; NP_109846.1; NC_000912.1.
DR RefSeq; WP_010874515.1; NC_000912.1.
DR AlphaFoldDB; P75587; -.
DR SMR; P75587; -.
DR IntAct; P75587; 1.
DR STRING; 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; VCETHIF; -.
DR BioCyc; MPNE272634:G1GJ3-265-MON; -.
DR UniPathway; UPA00276; UER00406.
DR UniPathway; UPA00277; UER00407.
DR Proteomes; UP000000808; Chromosome.
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; 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
