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   27-MAR-2024, entry version 77.
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; Bacillota; 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   KEGG; gtn:GTNG_3159; -.
DR   eggNOG; COG0196; Bacteria.
DR   HOGENOM; CLU_048437_4_2_9; -.
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; HUPs; 1.
DR   InterPro; IPR015864; FAD_synthase.
DR   InterPro; IPR023468; Riboflavin_kinase.
DR   InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR   PANTHER; PTHR22749:SF6; RIBOFLAVIN KINASE; 1.
DR   PANTHER; PTHR22749; RIBOFLAVIN KINASE/FMN ADENYLYLTRANSFERASE; 1.
DR   Pfam; PF06574; FAD_syn; 1.
DR   SUPFAM; SSF52374; Nucleotidylyl transferase; 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
//