RIBF_GEOTN
ID RIBF_GEOTN Reviewed; 179 AA.
AC A4IT50;
DT 06-FEB-2013, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2007, sequence version 1.
DT 03-AUG-2022, entry version 71.
DE RecName: Full=Putative bifunctional riboflavin kinase/FMN adenylyltransferase {ECO:0000303|PubMed:19942660};
DE AltName: Full=Putative riboflavin biosynthesis protein RibF {ECO:0000305};
DE Includes:
DE RecName: Full=Riboflavin kinase {ECO:0000303|PubMed:19942660};
DE EC=2.7.1.26 {ECO:0000269|PubMed:19942660};
DE AltName: Full=Flavokinase {ECO:0000250|UniProtKB:Q59263};
DE Includes:
DE RecName: Full=FMN adenylyltransferase {ECO:0000303|PubMed:19942660};
DE EC=2.7.7.2 {ECO:0000269|PubMed:19942660};
DE AltName: Full=FAD pyrophosphorylase {ECO:0000250|UniProtKB:Q59263};
DE AltName: Full=FAD synthase {ECO:0000250|UniProtKB:Q59263};
GN Name=ribF; OrderedLocusNames=GTNG_3159;
OS Geobacillus thermodenitrificans (strain NG80-2).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Geobacillus.
OX NCBI_TaxID=420246;
RN [1] {ECO:0000312|EMBL:ABO68504.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NG80-2;
RX PubMed=17372208; DOI=10.1073/pnas.0609650104;
RA Feng L., Wang W., Cheng J., Ren Y., Zhao G., Gao C., Tang Y., Liu X.,
RA Han W., Peng X., Liu R., Wang L.;
RT "Genome and proteome of long-chain alkane degrading Geobacillus
RT thermodenitrificans NG80-2 isolated from a deep-subsurface oil reservoir.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:5602-5607(2007).
RN [2] {ECO:0000305}
RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RC STRAIN=NG80-2 {ECO:0000269|PubMed:19942660};
RX PubMed=19942660; DOI=10.1099/mic.0.031880-0;
RA Liu X., Dong Y., Li X., Ren Y., Li Y., Wang W., Wang L., Feng L.;
RT "Characterization of the anthranilate degradation pathway in Geobacillus
RT thermodenitrificans NG80-2.";
RL Microbiology 156:589-595(2010).
CC -!- FUNCTION: Catalyzes the phosphorylation of riboflavin to FMN followed
CC by the adenylation of FMN to FAD. {ECO:0000269|PubMed:19942660}.
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:19942660};
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:19942660};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Vmax=270.3 umol/min/mg enzyme toward FMN
CC {ECO:0000269|PubMed:19942660};
CC Vmax=170.09 umol/min/mg enzyme toward riboflavin
CC {ECO:0000269|PubMed:19942660};
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:0000255}.
CC -!- CAUTION: This sequence is divergent compared to other bacterial RibF.
CC {ECO:0000305}.
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DR EMBL; CP000557; ABO68504.1; -; Genomic_DNA.
DR RefSeq; WP_011888288.1; NC_009328.1.
DR AlphaFoldDB; A4IT50; -.
DR SMR; A4IT50; -.
DR STRING; 420246.GTNG_3159; -.
DR PRIDE; A4IT50; -.
DR EnsemblBacteria; ABO68504; ABO68504; GTNG_3159.
DR KEGG; gtn:GTNG_3159; -.
DR eggNOG; COG0196; Bacteria.
DR HOGENOM; CLU_048437_4_2_9; -.
DR OMA; KSASCFI; -.
DR OrthoDB; 1504821at2; -.
DR UniPathway; UPA00276; UER00406.
DR UniPathway; UPA00277; UER00407.
DR Proteomes; UP000001578; 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; 3.40.50.620; -; 1.
DR InterPro; IPR015864; FAD_synthase.
DR InterPro; IPR023468; Riboflavin_kinase.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR PANTHER; PTHR22749; PTHR22749; 1.
DR Pfam; PF06574; FAD_syn; 1.
PE 1: Evidence at protein level;
KW ATP-binding; FAD; Flavoprotein; FMN; Kinase; Multifunctional enzyme;
KW Nucleotide-binding; Nucleotidyltransferase; Transferase.
FT CHAIN 1..179
FT /note="Putative bifunctional riboflavin kinase/FMN
FT adenylyltransferase"
FT /id="PRO_0000421234"
SQ SEQUENCE 179 AA; 20167 MW; 78CC00E8A22FCE33 CRC64;
MKVHEANQGL TLPGSVVAIG AFDGVHQGHQ AVLRQAVERS RQLGVESVAY TIDPPPRCRF
QGSRMLTTLQ EKLDRFAVLG LNHAVVAHFD ERYAARRVDA FIRELTALNP REVIVGQDFR
FGRNREGDVA LLRRHFPVRI VQTVCCADGQ RISSTRIREL IERGEWEQST VLLGWPLSS
