ID J9YTV9_9PROT Unreviewed; 305 AA.
AC J9YTV9;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 28-NOV-2012, sequence version 1.
DT 27-MAR-2024, entry version 43.
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 ORFNames=HIMB5_00000950 {ECO:0000313|EMBL:AFS46868.1};
OS alpha proteobacterium HIMB5.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Candidatus Pelagibacterales;
OC Candidatus Pelagibacteraceae.
OX NCBI_TaxID=859653 {ECO:0000313|EMBL:AFS46868.1, ECO:0000313|Proteomes:UP000006098};
RN [1] {ECO:0000313|EMBL:AFS46868.1, ECO:0000313|Proteomes:UP000006098}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HIMB5 {ECO:0000313|EMBL:AFS46868.1,
RC ECO:0000313|Proteomes:UP000006098};
RA Grote J., Thrash C., Huggett M.J., Landry Z., Carini P., Giovannoni S.J.,
RA Rappe M.S., Brinkac L., Kim M., Beeson K., Ferriera S., Sutton G.,
RA Friedman R., Venter J.C.;
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the phosphorylation of riboflavin to FMN followed
CC by the adenylation of FMN to FAD. {ECO:0000256|ARBA:ARBA00002121}.
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; CP003809; AFS46868.1; -; Genomic_DNA.
DR AlphaFoldDB; J9YTV9; -.
DR STRING; 859653.HIMB5_00000950; -.
DR KEGG; apm:HIMB5_00000950; -.
DR PATRIC; fig|859653.3.peg.95; -.
DR eggNOG; COG0196; Bacteria.
DR HOGENOM; CLU_048437_0_2_5; -.
DR OrthoDB; 9803667at2; -.
DR UniPathway; UPA00276; UER00406.
DR UniPathway; UPA00277; UER00407.
DR Proteomes; UP000006098; Chromosome.
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; 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 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:AFS46868.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR004491};
KW Nucleotidyltransferase {ECO:0000256|PIRNR:PIRNR004491,
KW ECO:0000313|EMBL:AFS46868.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR004491}.
FT DOMAIN 182..305
FT /note="Riboflavin kinase"
FT /evidence="ECO:0000259|SMART:SM00904"
SQ SEQUENCE 305 AA; 35788 MW; 9D765A33363DE3C5 CRC64;
MKIFNNFDIP KNIKGSILLI GNFDGVHLGH KKLFKEAQKY KKKYKLKIGV LTFEPMPKMF
FNKKLKNFRI SSLKQKNELM KNLKIDFLIN KKFDKNFSST NSINFIKNII SKKLKTKFIF
VSDNFRFGKN REGDVKQLKS FESDLNYKLV KPKPVKLNNK IVSSTLIRKS LENGKLDFAN
KLLDRKWFVD GKVEKGRQLG RKIGFPTCNI GIKDFLIPML GVYAVNVFMK GKIYKGIANI
GYRPTFNQKK LLLEVHLFNF SGNLYNKYLR VNFLKFIRKE KKFTNIEKLK QQIKIDLAKA
KKKYV
//
