RIBCF_LISMO
ID RIBCF_LISMO Reviewed; 314 AA.
AC Q8Y7F2;
DT 26-FEB-2020, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2002, sequence version 1.
DT 03-AUG-2022, entry version 104.
DE RecName: Full=Bifunctional riboflavin kinase/FMN adenylyltransferase {ECO:0000305};
DE AltName: Full=Bifunctional flavokinase/FAD synthetase {ECO:0000303|PubMed:27672192};
DE AltName: Full=Riboflavin biosynthesis protein RibCF {ECO:0000305};
DE Includes:
DE RecName: Full=Riboflavin kinase {ECO:0000305};
DE EC=2.7.1.26 {ECO:0000269|PubMed:27672192};
DE AltName: Full=Flavokinase {ECO:0000305};
DE Includes:
DE RecName: Full=FMN adenylyltransferase {ECO:0000305};
DE EC=2.7.7.2 {ECO:0000269|PubMed:27672192};
DE AltName: Full=FAD pyrophosphorylase {ECO:0000305};
DE AltName: Full=FAD synthase {ECO:0000305};
GN Name=ribCF {ECO:0000303|PubMed:27672192};
GN Synonyms=ribC {ECO:0000312|EMBL:CAC99407.1}; OrderedLocusNames=lmo1329;
OS Listeria monocytogenes serovar 1/2a (strain ATCC BAA-679 / EGD-e).
OC Bacteria; Firmicutes; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=169963;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-679 / EGD-e;
RX PubMed=11679669; DOI=10.1126/science.1063447;
RA Glaser P., Frangeul L., Buchrieser C., Rusniok C., Amend A., Baquero F.,
RA Berche P., Bloecker H., Brandt P., Chakraborty T., Charbit A.,
RA Chetouani F., Couve E., de Daruvar A., Dehoux P., Domann E.,
RA Dominguez-Bernal G., Duchaud E., Durant L., Dussurget O., Entian K.-D.,
RA Fsihi H., Garcia-del Portillo F., Garrido P., Gautier L., Goebel W.,
RA Gomez-Lopez N., Hain T., Hauf J., Jackson D., Jones L.-M., Kaerst U.,
RA Kreft J., Kuhn M., Kunst F., Kurapkat G., Madueno E., Maitournam A.,
RA Mata Vicente J., Ng E., Nedjari H., Nordsiek G., Novella S., de Pablos B.,
RA Perez-Diaz J.-C., Purcell R., Remmel B., Rose M., Schlueter T., Simoes N.,
RA Tierrez A., Vazquez-Boland J.-A., Voss H., Wehland J., Cossart P.;
RT "Comparative genomics of Listeria species.";
RL Science 294:849-852(2001).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RX PubMed=27672192; DOI=10.1128/jb.00388-16;
RA Matern A., Pedrolli D., Grosshennig S., Johansson J., Mack M.;
RT "Uptake and metabolism of antibiotics roseoflavin and 8-demethyl-8-
RT aminoriboflavin in riboflavin-auxotrophic Listeria monocytogenes.";
RL J. Bacteriol. 198:3233-3243(2016).
CC -!- FUNCTION: Catalyzes the phosphorylation of riboflavin to FMN followed
CC by the adenylation of FMN to FAD (PubMed:27672192). Can also catalyze
CC the phosphorylation of the toxic riboflavin analogs 8-demethyl-8-
CC aminoriboflavin (AF) to 8-demethyl-8-aminoriboflavin mononucleotide
CC (AFMN) and roseoflavin (RoF) to roseoflavin mononucleotide (RoFMN), and
CC the adenylation of AFMN to 8-demethyl-8-aminoriboflavin adenine
CC dinucleotide (AFAD) (PubMed:27672192). {ECO:0000269|PubMed:27672192}.
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:27672192};
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:27672192};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=6.9 uM for riboflavin {ECO:0000269|PubMed:27672192};
CC KM=29.2 uM for FMN {ECO:0000269|PubMed:27672192};
CC Vmax=668 nmol/min/mg enzyme with riboflavin as substrate
CC {ECO:0000269|PubMed:27672192};
CC Vmax=3706 nmol/min/mg enzyme with FMN as substrate
CC {ECO:0000269|PubMed:27672192};
CC Note=kcat is 0.40 sec(-1) with riboflavin as substrate. kcat is 4.39
CC sec(-1) with FMN as substrate. {ECO:0000269|PubMed:27672192};
CC -!- PATHWAY: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step
CC 1/1. {ECO:0000269|PubMed:27672192}.
CC -!- PATHWAY: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin
CC (ATP route): step 1/1. {ECO:0000269|PubMed:27672192}.
CC -!- SIMILARITY: Belongs to the RibF family. {ECO:0000305}.
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DR EMBL; AL591978; CAC99407.1; -; Genomic_DNA.
DR PIR; AI1240; AI1240.
DR RefSeq; NP_464854.1; NC_003210.1.
DR RefSeq; WP_009925599.1; NZ_CP023861.1.
DR AlphaFoldDB; Q8Y7F2; -.
DR SMR; Q8Y7F2; -.
DR STRING; 169963.lmo1329; -.
DR PaxDb; Q8Y7F2; -.
DR DNASU; 987710; -.
DR EnsemblBacteria; CAC99407; CAC99407; CAC99407.
DR GeneID; 987710; -.
DR KEGG; lmo:lmo1329; -.
DR PATRIC; fig|169963.11.peg.1366; -.
DR eggNOG; COG0196; Bacteria.
DR HOGENOM; CLU_048437_0_2_9; -.
DR OMA; HRGHQAI; -.
DR PhylomeDB; Q8Y7F2; -.
DR BioCyc; LMON169963:LMO1329-MON; -.
DR UniPathway; UPA00276; UER00406.
DR UniPathway; UPA00277; UER00407.
DR Proteomes; UP000000817; 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 1: Evidence at protein level;
KW ATP-binding; FAD; Flavoprotein; FMN; Kinase; Multifunctional enzyme;
KW Nucleotide-binding; Nucleotidyltransferase; Reference proteome;
KW Transferase.
FT CHAIN 1..314
FT /note="Bifunctional riboflavin kinase/FMN
FT adenylyltransferase"
FT /id="PRO_0000448897"
SQ SEQUENCE 314 AA; 35526 MW; 45D2267223C667DD CRC64;
MKTIYLHHPI TTDEWTDINK VMALGFFDGV HLGHQAVIKQ AKQIAGQKGL QTAVLTFDPH
PSVVLSNIRK QVKYLTPLED KAEKMAKLGV DIMYVVRFTT QFSELSPQAF VDNYLVALHV
EHVVAGFDYS YGKKGEGKMT DLAKYADGRF EVTIVDKQTA ASDKISSTNI RRAITEGELE
EANQLLGYPY TTKGTVIHGD KRGRTIGFPT ANIRVNEDYL IPKLGVYAVK FRVNGETHLG
MASIGYNITF KDDQALSIEV YILDFHREIY GEEAEIKWYQ FFRPELKFNG VEGLIAQLEK
DEQDTRAFFA KLED
