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Database: UniProt
Entry: Q4JH00_LISWE
LinkDB: Q4JH00_LISWE
Original site: Q4JH00_LISWE 
ID   Q4JH00_LISWE            Unreviewed;       314 AA.
AC   Q4JH00;
DT   02-AUG-2005, integrated into UniProtKB/TrEMBL.
DT   02-AUG-2005, sequence version 1.
DT   27-MAR-2024, entry version 65.
DE   RecName: Full=Riboflavin biosynthesis protein {ECO:0000256|PIRNR:PIRNR004491};
DE   Includes:
DE     RecName: Full=Riboflavin kinase {ECO:0000256|PIRNR:PIRNR004491};
DE              EC=2.7.1.26 {ECO:0000256|PIRNR:PIRNR004491};
DE     AltName: Full=Flavokinase {ECO:0000256|PIRNR:PIRNR004491};
DE   Includes:
DE     RecName: Full=FMN adenylyltransferase {ECO:0000256|PIRNR:PIRNR004491};
DE              EC=2.7.7.2 {ECO:0000256|PIRNR:PIRNR004491};
DE     AltName: Full=FAD pyrophosphorylase {ECO:0000256|PIRNR:PIRNR004491};
DE     AltName: Full=FAD synthase {ECO:0000256|PIRNR:PIRNR004491};
GN   Name=ribC {ECO:0000313|EMBL:AAY87951.1};
OS   Listeria welshimeri.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Listeriaceae; Listeria.
OX   NCBI_TaxID=1643 {ECO:0000313|EMBL:AAY87951.1};
RN   [1] {ECO:0000313|EMBL:AAY87951.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=91672 {ECO:0000313|EMBL:AAY87951.1};
RA   Volokhov D.V., George J., Chizhikov V.E.;
RT   "Characterization of atypical non-hemolytic Listeria seeligeri isolates.";
RL   Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AAY87951.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=91672 {ECO:0000313|EMBL:AAY87951.1};
RX   PubMed=16597942; DOI=10.1128/AEM.72.4.2439-2448.2006;
RA   Volokhov D., George J., Anderson C., Duvall R.E., Hitchins A.D.;
RT   "Discovery of natural atypical nonhemolytic Listeria seeligeri isolates.";
RL   Appl. Environ. Microbiol. 72:2439-2448(2006).
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         ECO:0000256|PIRNR:PIRNR004491};
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         ECO:0000256|PIRNR:PIRNR004491};
CC   -!- PATHWAY: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step
CC       1/1. {ECO:0000256|ARBA:ARBA00004726, ECO:0000256|PIRNR:PIRNR004491}.
CC   -!- PATHWAY: Cofactor biosynthesis; FMN biosynthesis; FMN from riboflavin
CC       (ATP route): step 1/1. {ECO:0000256|ARBA:ARBA00005201,
CC       ECO:0000256|PIRNR:PIRNR004491}.
CC   -!- SIMILARITY: Belongs to the ribF family.
CC       {ECO:0000256|PIRNR:PIRNR004491}.
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DR   EMBL; DQ091840; AAY87951.1; -; Genomic_DNA.
DR   AlphaFoldDB; Q4JH00; -.
DR   UniPathway; UPA00276; UER00406.
DR   UniPathway; UPA00277; UER00407.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0003919; F:FMN adenylyltransferase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0008531; F:riboflavin kinase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0006747; P:FAD biosynthetic process; IEA:UniProtKB-UniRule.
DR   GO; GO:0009398; P:FMN biosynthetic process; IEA:UniProtKB-UniRule.
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   Gene3D; 2.40.30.30; Riboflavin kinase-like; 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   NCBIfam; TIGR00125; cyt_tran_rel; 1.
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   PIRSF; PIRSF004491; FAD_Synth; 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, ECO:0000256|PIRNR:PIRNR004491};
KW   FAD {ECO:0000256|ARBA:ARBA00022827, ECO:0000256|PIRNR:PIRNR004491};
KW   Flavoprotein {ECO:0000256|ARBA:ARBA00022630,
KW   ECO:0000256|PIRNR:PIRNR004491};
KW   FMN {ECO:0000256|ARBA:ARBA00022643, ECO:0000256|PIRNR:PIRNR004491};
KW   Kinase {ECO:0000256|PIRNR:PIRNR004491, ECO:0000313|EMBL:AAY87951.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR004491};
KW   Nucleotidyltransferase {ECO:0000256|PIRNR:PIRNR004491};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR004491}.
FT   DOMAIN          185..310
FT                   /note="Riboflavin kinase"
FT                   /evidence="ECO:0000259|SMART:SM00904"
SQ   SEQUENCE   314 AA;  35615 MW;  DD751353C168EEF1 CRC64;
     MKTIYLHHPI KVDEWTDVKK VMALGFFDGV HLGHQAVIKK AKQIAEQKGL QTAVLTFDPH
     PSVVLSNIRK QVRYLTPLED KAEKMAELGV DIMYVVRFTT QFSELSPQAF VDKYLVSLNV
     SHVVAGFDYS YGKKGEGKMA DLERYANGRF DVTIVDKQTA ASDKISSTNI RRAISEGELE
     EANQLLGYPY TTKGTVIHGD KRGRTIGFPT ANILVNEDYL IPKLGVYAVK FRVNGETYLG
     MASIGYNITF KDDQALSIEV YILDFHREIY GEEAEIEWYQ FFRPELKFNG VEGLIAQLEK
     DEQDTRAFFA DLED
//
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