RIBF_HAEIN
ID RIBF_HAEIN Reviewed; 308 AA.
AC P44957;
DT 01-NOV-1995, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1995, sequence version 1.
DT 03-AUG-2022, entry version 121.
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=HI_0963;
OS Haemophilus influenzae (strain ATCC 51907 / DSM 11121 / KW20 / Rd).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pasteurellales;
OC Pasteurellaceae; Haemophilus.
OX NCBI_TaxID=71421;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 51907 / DSM 11121 / KW20 / Rd;
RX PubMed=7542800; DOI=10.1126/science.7542800;
RA Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F.,
RA Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M.,
RA McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D.,
RA Scott J.D., Shirley R., Liu L.-I., Glodek A., Kelley J.M., Weidman J.F.,
RA Phillips C.A., Spriggs T., Hedblom E., Cotton M.D., Utterback T.R.,
RA Hanna M.C., Nguyen D.T., Saudek D.M., Brandon R.C., Fine L.D.,
RA Fritchman J.L., Fuhrmann J.L., Geoghagen N.S.M., Gnehm C.L., McDonald L.A.,
RA Small K.V., Fraser C.M., Smith H.O., Venter J.C.;
RT "Whole-genome random sequencing and assembly of Haemophilus influenzae
RT Rd.";
RL Science 269:496-512(1995).
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}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAC22622.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; L42023; AAC22622.1; ALT_INIT; Genomic_DNA.
DR PIR; H64162; H64162.
DR RefSeq; NP_439124.1; NC_000907.1.
DR RefSeq; WP_032828335.1; NC_000907.1.
DR AlphaFoldDB; P44957; -.
DR SMR; P44957; -.
DR STRING; 71421.HI_0963; -.
DR EnsemblBacteria; AAC22622; AAC22622; HI_0963.
DR KEGG; hin:HI_0963; -.
DR PATRIC; fig|71421.8.peg.1005; -.
DR eggNOG; COG0196; Bacteria.
DR HOGENOM; CLU_048437_0_1_6; -.
DR PhylomeDB; P44957; -.
DR UniPathway; UPA00276; UER00406.
DR UniPathway; UPA00277; UER00407.
DR Proteomes; UP000000579; 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; IPR004821; Cyt_trans-like.
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; TIGR00125; cyt_tran_rel; 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..308
FT /note="Bifunctional riboflavin kinase/FMN
FT adenylyltransferase"
FT /id="PRO_0000194140"
SQ SEQUENCE 308 AA; 35121 MW; 5DA4EA0F5492923E CRC64;
MQLIRGLHNA NRVLQGCALT IGNFDGVHLG HQTVLRHLRQ KADELNLPMA VLLFESQPRE
YFMGKNAPAR LMRLRDKIYY LEKAKVDVVI VAKFDRTFAE QLADVFIEQT LVNHLHVKFL
SIGDDFKFGS KRQGNFAMLQ AASKRFGFIV EDNRSFCLDA QRISSTAIRE ALANDDLQLA
ENLLGKPYRI FGRVIHGNKL GRTIGFPTAN IRLHRQVNPI KGVYAVKVRL KSGEIFNGVA
NMGKRPTING LMQLLEVHLF DFSQNIYGQM VEVEFCHKIR NEIKFPSFDD LKVQIEKDVE
TAKAFFNS
