ID C0LWZ9_LISMN Unreviewed; 211 AA.
AC C0LWZ9;
DT 05-MAY-2009, integrated into UniProtKB/TrEMBL.
DT 05-MAY-2009, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Bifunctional riboflavin kinase/FMN adenylyltransferase {ECO:0000256|ARBA:ARBA00018483};
DE EC=2.7.1.26 {ECO:0000256|ARBA:ARBA00012105};
DE EC=2.7.7.2 {ECO:0000256|ARBA:ARBA00012393};
DE Flags: Fragment;
GN Name=ribC {ECO:0000313|EMBL:ACN76312.1};
OS Listeria monocytogenes.
OC Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX NCBI_TaxID=1639 {ECO:0000313|EMBL:ACN76312.1};
RN [1] {ECO:0000313|EMBL:ACN76312.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=N1 {ECO:0000313|EMBL:ACN76312.1}, N11
RC {ECO:0000313|EMBL:ACN76319.1}, N13 {ECO:0000313|EMBL:ACN76321.1}, N14
RC {ECO:0000313|EMBL:ACN76322.1}, N15 {ECO:0000313|EMBL:ACN76323.1}, N16
RC {ECO:0000313|EMBL:ACN76324.1}, N20 {ECO:0000313|EMBL:ACN76325.1}, N22
RC {ECO:0000313|EMBL:ACN76326.1}, N23 {ECO:0000313|EMBL:ACN76327.1}, N25
RC {ECO:0000313|EMBL:ACN76328.1}, N27 {ECO:0000313|EMBL:ACN76330.1}, N29
RC {ECO:0000313|EMBL:ACN76332.1}, and N4 {ECO:0000313|EMBL:ACN76313.1};
RX PubMed=19735205; DOI=10.1089/fpd.2009.0353;
RA Chen J., Chen Q., Jiang J., Hu H., Ye J., Fang W.;
RT "Serovar 4b complex predominates among Listeria monocytogenes isolates from
RT imported aquatic products in China.";
RL Foodborne Pathog. Dis. 7:31-41(2010).
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:0000256|ARBA:ARBA00001332};
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:0000256|ARBA:ARBA00000372};
CC -!- PATHWAY: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step
CC 1/1. {ECO:0000256|ARBA:ARBA00004726}.
CC -!- PATHWAY: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin
CC (ATP route): step 1/1. {ECO:0000256|ARBA:ARBA00005201}.
CC -!- SIMILARITY: Belongs to the RibF family.
CC {ECO:0000256|ARBA:ARBA00010214}.
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DR EMBL; FJ774458; ACN76312.1; -; Genomic_DNA.
DR EMBL; FJ774459; ACN76313.1; -; Genomic_DNA.
DR EMBL; FJ774465; ACN76319.1; -; Genomic_DNA.
DR EMBL; FJ774467; ACN76321.1; -; Genomic_DNA.
DR EMBL; FJ774468; ACN76322.1; -; Genomic_DNA.
DR EMBL; FJ774469; ACN76323.1; -; Genomic_DNA.
DR EMBL; FJ774470; ACN76324.1; -; Genomic_DNA.
DR EMBL; FJ774471; ACN76325.1; -; Genomic_DNA.
DR EMBL; FJ774472; ACN76326.1; -; Genomic_DNA.
DR EMBL; FJ774473; ACN76327.1; -; Genomic_DNA.
DR EMBL; FJ774474; ACN76328.1; -; Genomic_DNA.
DR EMBL; FJ774476; ACN76330.1; -; Genomic_DNA.
DR EMBL; FJ774478; ACN76332.1; -; Genomic_DNA.
DR AlphaFoldDB; C0LWZ9; -.
DR UniPathway; UPA00276; UER00406.
DR UniPathway; UPA00277; UER00407.
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:0009231; P:riboflavin biosynthetic process; IEA:InterPro.
DR CDD; cd02064; FAD_synthetase_N; 1.
DR Gene3D; 3.40.50.620; HUPs; 1.
DR Gene3D; 2.40.30.30; Riboflavin kinase-like; 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 NCBIfam; TIGR00083; ribF; 1.
DR PANTHER; PTHR22749:SF6; RIBOFLAVIN KINASE; 1.
DR PANTHER; PTHR22749; RIBOFLAVIN KINASE/FMN ADENYLYLTRANSFERASE; 1.
DR Pfam; PF06574; FAD_syn; 1.
DR Pfam; PF01687; Flavokinase; 1.
DR SMART; SM00904; Flavokinase; 1.
DR SUPFAM; SSF52374; Nucleotidylyl transferase; 1.
DR SUPFAM; SSF82114; Riboflavin kinase-like; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW FAD {ECO:0000256|ARBA:ARBA00022827};
KW Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 149..211
FT /note="Riboflavin kinase"
FT /evidence="ECO:0000259|SMART:SM00904"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACN76312.1"
FT NON_TER 211
FT /evidence="ECO:0000313|EMBL:ACN76312.1"
SQ SEQUENCE 211 AA; 23460 MW; 839FDABD1F87CA9C CRC64;
VIKKAKQIAE KKGLQTAVLT FDPHPSVVLS NIRKQVKYLT PLEDKAEKMA ELGVDIMYVV
RFTTQFSELS PQAFVDNYLV ALHVQHVVAG FDYSYGKKGE GKMTDLAKYA DGRFEVTIVD
KQTAASDKIS STNIRRAIIE GELEEANQLL GYPYTTKGTV IHGDKRGRTI GFPTANIRVN
EDYLIPKLGV YAVKFRVNGE THLGMASIGY N
//
