RIBF_CORAM
ID RIBF_CORAM Reviewed; 338 AA.
AC Q59263;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 93.
DE RecName: Full=Bifunctional riboflavin kinase/FMN adenylyltransferase {ECO:0000305};
DE AltName: Full=Riboflavin biosynthesis protein RibF {ECO:0000305};
DE Includes:
DE RecName: Full=Riboflavin kinase {ECO:0000305};
DE EC=2.7.1.26 {ECO:0000269|PubMed:3023344};
DE AltName: Full=Flavokinase {ECO:0000305};
DE Includes:
DE RecName: Full=FMN adenylyltransferase {ECO:0000305};
DE EC=2.7.7.2 {ECO:0000269|PubMed:3023344};
DE AltName: Full=FAD pyrophosphorylase {ECO:0000305};
DE AltName: Full=FAD synthase {ECO:0000305};
GN Name=ribF;
OS Corynebacterium ammoniagenes (Brevibacterium ammoniagenes).
OC Bacteria; Actinobacteria; Corynebacteriales; Corynebacteriaceae;
OC Corynebacterium.
OX NCBI_TaxID=1697;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 6872 / DSM 20305 / IAM 1645 / KCTC 1019 / NCTC 2399;
RX PubMed=7772835; DOI=10.1271/bbb.59.694;
RA Nakagawa S., Igarashi A., Ohta T., Hagihara T., Fujio T., Aisaka K.;
RT "Nucleotide sequence of the FAD synthetase gene from Corynebacterium
RT ammoniagenes and its expression in Escherichia coli.";
RL Biosci. Biotechnol. Biochem. 59:694-702(1995).
RN [2]
RP PROTEIN SEQUENCE OF 1-18, FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ACTIVITY
RP REGULATION, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=ATCC 6872 / DSM 20305 / IAM 1645 / KCTC 1019 / NCTC 2399;
RX PubMed=3023344; DOI=10.1016/s0021-9258(18)66693-1;
RA Manstein D.J., Pai E.F.;
RT "Purification and characterization of FAD synthetase from Brevibacterium
RT ammoniagenes.";
RL J. Biol. Chem. 261:16169-16173(1986).
CC -!- FUNCTION: Catalyzes the phosphorylation of riboflavin to FMN followed
CC by the adenylation of FMN to FAD. {ECO:0000269|PubMed:3023344}.
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:0000269|PubMed:3023344};
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:0000269|PubMed:3023344};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000269|PubMed:3023344};
CC -!- ACTIVITY REGULATION: Higher divalent cation concentrations lead to
CC decrease in the turnover of riboflavin and the 5'-phosphotransferase
CC activity, while the adenylyltransferase activity increases.
CC {ECO:0000269|PubMed:3023344}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=5 uM for Mg-ATP (for riboflavin kinase activity)
CC {ECO:0000269|PubMed:3023344};
CC KM=160 uM for Mg-ATP (for FMN adenylyltransferase activity)
CC {ECO:0000269|PubMed:3023344};
CC pH dependence:
CC With magnesium ions the highest turnover of riboflavin is observed
CC between pH 6 and 7.5, while that of FAD is between 7.0 and 9.0. With
CC zinc ions a steady increase in riboflavin turnover is observed
CC between pH 4.5 and 10, while FAD is the major product at pH 7.0 and
CC decreases rapidly above pH 8.0. {ECO:0000269|PubMed:3023344};
CC -!- PATHWAY: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step
CC 1/1. {ECO:0000305}.
CC -!- PATHWAY: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin
CC (ATP route): step 1/1. {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the RibF family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; D37967; BAA07182.1; -; Genomic_DNA.
DR PIR; JC4008; JC4008.
DR PDB; 2X0K; X-ray; 1.95 A; A/B=1-338.
DR PDB; 3ZUG; X-ray; 2.05 A; A/B=1-338.
DR PDB; 4UZE; X-ray; 2.34 A; A/B=1-338.
DR PDB; 4UZF; X-ray; 2.52 A; A/B=1-338.
DR PDB; 5A88; X-ray; 2.08 A; A/B/C/D=183-338.
DR PDB; 5A89; X-ray; 1.65 A; A/B=183-338.
DR PDB; 5A8A; X-ray; 1.80 A; A/B=183-338.
DR PDB; 5FNZ; X-ray; 2.52 A; A/B=1-338.
DR PDB; 5FO0; X-ray; 2.51 A; A/B=1-338.
DR PDB; 5FO1; X-ray; 2.45 A; A/B=1-338.
DR PDBsum; 2X0K; -.
DR PDBsum; 3ZUG; -.
DR PDBsum; 4UZE; -.
DR PDBsum; 4UZF; -.
DR PDBsum; 5A88; -.
DR PDBsum; 5A89; -.
DR PDBsum; 5A8A; -.
DR PDBsum; 5FNZ; -.
DR PDBsum; 5FO0; -.
DR PDBsum; 5FO1; -.
DR AlphaFoldDB; Q59263; -.
DR SMR; Q59263; -.
DR BRENDA; 2.7.1.26; 959.
DR BRENDA; 2.7.7.2; 959.
DR UniPathway; UPA00276; UER00406.
DR UniPathway; UPA00277; UER00407.
DR EvolutionaryTrace; Q59263; -.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Direct protein sequencing; FAD; Flavoprotein;
KW FMN; Kinase; Multifunctional enzyme; Nucleotide-binding;
KW Nucleotidyltransferase; Transferase.
FT CHAIN 1..338
FT /note="Bifunctional riboflavin kinase/FMN
FT adenylyltransferase"
FT /id="PRO_0000194136"
FT STRAND 2..6
FT /evidence="ECO:0007829|PDB:2X0K"
FT HELIX 7..9
FT /evidence="ECO:0007829|PDB:2X0K"
FT STRAND 17..22
FT /evidence="ECO:0007829|PDB:2X0K"
FT HELIX 29..45
FT /evidence="ECO:0007829|PDB:2X0K"
FT STRAND 48..56
FT /evidence="ECO:0007829|PDB:2X0K"
FT HELIX 58..62
FT /evidence="ECO:0007829|PDB:2X0K"
FT STRAND 70..72
FT /evidence="ECO:0007829|PDB:2X0K"
FT HELIX 74..83
FT /evidence="ECO:0007829|PDB:2X0K"
FT STRAND 87..92
FT /evidence="ECO:0007829|PDB:2X0K"
FT TURN 94..96
FT /evidence="ECO:0007829|PDB:2X0K"
FT STRAND 97..100
FT /evidence="ECO:0007829|PDB:2X0K"
FT HELIX 103..109
FT /evidence="ECO:0007829|PDB:2X0K"
FT HELIX 110..114
FT /evidence="ECO:0007829|PDB:2X0K"
FT STRAND 117..123
FT /evidence="ECO:0007829|PDB:2X0K"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:2X0K"
FT HELIX 130..132
FT /evidence="ECO:0007829|PDB:2X0K"
FT HELIX 136..142
FT /evidence="ECO:0007829|PDB:2X0K"
FT TURN 143..146
FT /evidence="ECO:0007829|PDB:2X0K"
FT STRAND 147..152
FT /evidence="ECO:0007829|PDB:2X0K"
FT HELIX 164..172
FT /evidence="ECO:0007829|PDB:2X0K"
FT HELIX 176..183
FT /evidence="ECO:0007829|PDB:2X0K"
FT STRAND 188..192
FT /evidence="ECO:0007829|PDB:5A89"
FT HELIX 200..204
FT /evidence="ECO:0007829|PDB:5A89"
FT STRAND 209..212
FT /evidence="ECO:0007829|PDB:5A89"
FT STRAND 222..231
FT /evidence="ECO:0007829|PDB:5A89"
FT STRAND 239..241
FT /evidence="ECO:0007829|PDB:5A8A"
FT STRAND 247..255
FT /evidence="ECO:0007829|PDB:5A89"
FT TURN 258..260
FT /evidence="ECO:0007829|PDB:5A89"
FT STRAND 266..271
FT /evidence="ECO:0007829|PDB:5A89"
FT STRAND 282..292
FT /evidence="ECO:0007829|PDB:5A89"
FT HELIX 300..324
FT /evidence="ECO:0007829|PDB:5A89"
FT TURN 325..327
FT /evidence="ECO:0007829|PDB:2X0K"
FT HELIX 329..331
FT /evidence="ECO:0007829|PDB:5A89"
SQ SEQUENCE 338 AA; 36844 MW; B714FD885412CC68 CRC64;
MDIWYGTAAV PKDLDNSAVT IGVFDGVHRG HQKLINATVE KAREVGAKAI MVTFDPHPVS
VFLPRRAPLG ITTLAERFAL AESFGIDGVL VIDFTRELSG TSPEKYVEFL LEDTLHASHV
VVGANFTFGE NAAGTADSLR QICQSRLTVD VIDLLDDEGV RISSTTVREF LSEGDVARAN
WALGRHFYVT GPVVRGAGRG GKELGFPTAN QYFHDTVALP ADGVYAGWLT ILPTEAPVSG
NMEPEVAYAA AISVGTNPTF GDEQRSVESF VLDRDADLYG HDVKVEFVDH VRAMEKFDSV
EQLLEVMAKD VQKTRTLLAQ DVQAHKMAPE TYFLQAES
