RIBF_ECOLI
ID RIBF_ECOLI Reviewed; 313 AA.
AC P0AG40; P08391; P75621;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 119.
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; Synonyms=yaaC; OrderedLocusNames=b0025, JW0023;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2985604; DOI=10.1016/s0021-9258(18)89067-6;
RA Kamio Y., Lin C.-K., Regue M., Wu H.C.;
RT "Characterization of the ileS-lsp operon in Escherichia coli.
RT Identification of an open reading frame upstream of the ileS gene and
RT potential promoter(s) for the ileS-lsp operon.";
RL J. Biol. Chem. 260:5616-5620(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12;
RX PubMed=1630901; DOI=10.1093/nar/20.13.3305;
RA Yura T., Mori H., Nagai H., Nagata T., Ishihama A., Fujita N., Isono K.,
RA Mizobuchi K., Nakata A.;
RT "Systematic sequencing of the Escherichia coli genome: analysis of the 0-
RT 2.4 min region.";
RL Nucleic Acids Res. 20:3305-3308(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND SEQUENCE REVISION TO
RP 108; 128-169 AND 214.
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
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 -!- INTERACTION:
CC P0AG40; P0AFG8: aceE; NbExp=2; IntAct=EBI-542969, EBI-542683;
CC -!- SIMILARITY: Belongs to the RibF family. {ECO:0000305}.
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DR EMBL; M10428; AAA24605.1; -; Genomic_DNA.
DR EMBL; U00096; AAC73136.1; -; Genomic_DNA.
DR EMBL; AP009048; BAB96594.2; -; Genomic_DNA.
DR PIR; A64723; QQECIL.
DR RefSeq; NP_414566.1; NC_000913.3.
DR RefSeq; WP_000767329.1; NZ_STEB01000010.1.
DR AlphaFoldDB; P0AG40; -.
DR SMR; P0AG40; -.
DR BioGRID; 4261848; 7.
DR DIP; DIP-35789N; -.
DR IntAct; P0AG40; 10.
DR STRING; 511145.b0025; -.
DR jPOST; P0AG40; -.
DR PaxDb; P0AG40; -.
DR PRIDE; P0AG40; -.
DR EnsemblBacteria; AAC73136; AAC73136; b0025.
DR EnsemblBacteria; BAB96594; BAB96594; BAB96594.
DR GeneID; 66671685; -.
DR GeneID; 949129; -.
DR KEGG; ecj:JW0023; -.
DR KEGG; eco:b0025; -.
DR PATRIC; fig|1411691.4.peg.2260; -.
DR EchoBASE; EB1071; -.
DR eggNOG; COG0196; Bacteria.
DR HOGENOM; CLU_048437_0_1_6; -.
DR InParanoid; P0AG40; -.
DR OMA; HRGHQAI; -.
DR PhylomeDB; P0AG40; -.
DR BioCyc; EcoCyc:RIBF-MON; -.
DR BioCyc; MetaCyc:RIBF-MON; -.
DR BRENDA; 2.7.7.2; 2026.
DR UniPathway; UPA00276; UER00406.
DR UniPathway; UPA00277; UER00407.
DR PRO; PR:P0AG40; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; 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; IBA:GO_Central.
DR GO; GO:0006747; P:FAD biosynthetic process; IEA:UniProtKB-UniPathway.
DR GO; GO:0009398; P:FMN biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:InterPro.
DR GO; GO:0006771; P:riboflavin metabolic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW ATP-binding; FAD; Flavoprotein; FMN; Kinase; Multifunctional enzyme;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..313
FT /note="Bifunctional riboflavin kinase/FMN
FT adenylyltransferase"
FT /id="PRO_0000194137"
FT CONFLICT 108
FT /note="I -> V (in Ref. 1; AAA24605 and 2; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 128..169
FT /note="RFGAGREGDFLLLQKAGMEYGFDITSTQTFCEGGVRISSTAV -> PLALVV
FT KAISCYYRKLAWNTASISPVRKLFAEVACASAARL (in Ref. 1; AAA24605
FT and 2; no nucleotide entry)"
FT /evidence="ECO:0000305"
FT CONFLICT 214
FT /note="L -> P (in Ref. 1; AAA24605 and 2; no nucleotide
FT entry)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 313 AA; 34734 MW; C0B2EF5499CD30FE CRC64;
MKLIRGIHNL SQAPQEGCVL TIGNFDGVHR GHRALLQGLQ EEGRKRNLPV MVMLFEPQPL
ELFATDKAPA RLTRLREKLR YLAECGVDYV LCVRFDRRFA ALTAQNFISD LLVKHLRVKF
LAVGDDFRFG AGREGDFLLL QKAGMEYGFD ITSTQTFCEG GVRISSTAVR QALADDNLAL
AESLLGHPFA ISGRVVHGDE LGRTIGFPTA NVPLRRQVSP VKGVYAVEVL GLGEKPLPGV
ANIGTRPTVA GIRQQLEVHL LDVAMDLYGR HIQVVLRKKI RNEQRFASLD ELKAQIARDE
LTAREFFGLT KPA
