RIBF_SYNY3
ID RIBF_SYNY3 Reviewed; 284 AA.
AC P73651;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 111.
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=slr1882;
OS Synechocystis sp. (strain PCC 6803 / Kazusa).
OC Bacteria; Cyanobacteria; Synechococcales; Merismopediaceae; Synechocystis;
OC unclassified Synechocystis.
OX NCBI_TaxID=1111708;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 6803 / Kazusa;
RX PubMed=8905231; DOI=10.1093/dnares/3.3.109;
RA Kaneko T., Sato S., Kotani H., Tanaka A., Asamizu E., Nakamura Y.,
RA Miyajima N., Hirosawa M., Sugiura M., Sasamoto S., Kimura T., Hosouchi T.,
RA Matsuno A., Muraki A., Nakazaki N., Naruo K., Okumura S., Shimpo S.,
RA Takeuchi C., Wada T., Watanabe A., Yamada M., Yasuda M., Tabata S.;
RT "Sequence analysis of the genome of the unicellular cyanobacterium
RT Synechocystis sp. strain PCC6803. II. Sequence determination of the entire
RT genome and assignment of potential protein-coding regions.";
RL DNA Res. 3:109-136(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; BA000022; BAA17696.1; -; Genomic_DNA.
DR PIR; S77138; S77138.
DR AlphaFoldDB; P73651; -.
DR SMR; P73651; -.
DR STRING; 1148.1652777; -.
DR PaxDb; P73651; -.
DR EnsemblBacteria; BAA17696; BAA17696; BAA17696.
DR KEGG; syn:slr1882; -.
DR eggNOG; COG0196; Bacteria.
DR InParanoid; P73651; -.
DR OMA; HRGHQAI; -.
DR PhylomeDB; P73651; -.
DR UniPathway; UPA00276; UER00406.
DR UniPathway; UPA00277; UER00407.
DR Proteomes; UP000001425; 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 3: Inferred from homology;
KW ATP-binding; FAD; Flavoprotein; FMN; Kinase; Multifunctional enzyme;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..284
FT /note="Bifunctional riboflavin kinase/FMN
FT adenylyltransferase"
FT /id="PRO_0000194144"
SQ SEQUENCE 284 AA; 31380 MW; 3049D89D35D6F5C6 CRC64;
MVLRQVMDFA QAVEHLLHPA VVSFNPHPRS FFSGRTQPLL TPLPEKAAQL TAIGIEQLVL
LPFTEKLANL SPKQFVQSIL VEQLQAKFIS VGQDFCFGHQ RRGNVQDLQN LGQEFGITVA
IAQLEQTDTE RISSSRIRRA LKEGKLAMAN HLLGRPYALR GTVVQGQQLG RKLGFPTANL
CLPADKLWPK YGVYAGWVNL NALDVPIPAV INLGDRPTVN GQEPSAEVHL LQWSGDLYGQ
GLEVALTHYL RPETKFAGLD QLKNQIAQDC QQAEKLLNLD GAIP
