RIBF_ECO57
ID RIBF_ECO57 Reviewed; 313 AA.
AC P0AG42; P08391; P75621;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 100.
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=Z0029, ECs0028;
OS Escherichia coli O157:H7.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83334;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / EDL933 / ATCC 700927 / EHEC;
RX PubMed=11206551; DOI=10.1038/35054089;
RA Perna N.T., Plunkett G. III, Burland V., Mau B., Glasner J.D., Rose D.J.,
RA Mayhew G.F., Evans P.S., Gregor J., Kirkpatrick H.A., Posfai G.,
RA Hackett J., Klink S., Boutin A., Shao Y., Miller L., Grotbeck E.J.,
RA Davis N.W., Lim A., Dimalanta E.T., Potamousis K., Apodaca J.,
RA Anantharaman T.S., Lin J., Yen G., Schwartz D.C., Welch R.A.,
RA Blattner F.R.;
RT "Genome sequence of enterohaemorrhagic Escherichia coli O157:H7.";
RL Nature 409:529-533(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=O157:H7 / Sakai / RIMD 0509952 / EHEC;
RX PubMed=11258796; DOI=10.1093/dnares/8.1.11;
RA Hayashi T., Makino K., Ohnishi M., Kurokawa K., Ishii K., Yokoyama K.,
RA Han C.-G., Ohtsubo E., Nakayama K., Murata T., Tanaka M., Tobe T., Iida T.,
RA Takami H., Honda T., Sasakawa C., Ogasawara N., Yasunaga T., Kuhara S.,
RA Shiba T., Hattori M., Shinagawa H.;
RT "Complete genome sequence of enterohemorrhagic Escherichia coli O157:H7 and
RT genomic comparison with a laboratory strain K-12.";
RL DNA Res. 8:11-22(2001).
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; AE005174; AAG54327.1; -; Genomic_DNA.
DR EMBL; BA000007; BAB33451.1; -; Genomic_DNA.
DR PIR; C85483; C85483.
DR PIR; D90632; D90632.
DR RefSeq; NP_308055.1; NC_002695.1.
DR RefSeq; WP_000767329.1; NZ_SWKA01000005.1.
DR AlphaFoldDB; P0AG42; -.
DR SMR; P0AG42; -.
DR STRING; 155864.EDL933_0024; -.
DR EnsemblBacteria; AAG54327; AAG54327; Z0029.
DR EnsemblBacteria; BAB33451; BAB33451; ECs_0028.
DR GeneID; 66671685; -.
DR GeneID; 913423; -.
DR KEGG; ece:Z0029; -.
DR KEGG; ecs:ECs_0028; -.
DR PATRIC; fig|386585.9.peg.123; -.
DR eggNOG; COG0196; Bacteria.
DR HOGENOM; CLU_048437_0_1_6; -.
DR OMA; HRGHQAI; -.
DR UniPathway; UPA00276; UER00406.
DR UniPathway; UPA00277; UER00407.
DR Proteomes; UP000000558; Chromosome.
DR Proteomes; UP000002519; 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..313
FT /note="Bifunctional riboflavin kinase/FMN
FT adenylyltransferase"
FT /id="PRO_0000194138"
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
