ID A0A086YYT5_9BIFI Unreviewed; 417 AA.
AC A0A086YYT5;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Riboflavin kinase/FMN adenylyltransferase {ECO:0000313|EMBL:KFI39435.1};
DE EC=2.7.1.26 {ECO:0000313|EMBL:KFI39435.1};
DE EC=2.7.7.2 {ECO:0000313|EMBL:KFI39435.1};
GN ORFNames=BACT_0267 {ECO:0000313|EMBL:KFI39435.1};
OS Bifidobacterium actinocoloniiforme DSM 22766.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Bifidobacterium.
OX NCBI_TaxID=1437605 {ECO:0000313|EMBL:KFI39435.1, ECO:0000313|Proteomes:UP000029015};
RN [1] {ECO:0000313|EMBL:KFI39435.1, ECO:0000313|Proteomes:UP000029015}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 22766 {ECO:0000313|EMBL:KFI39435.1,
RC ECO:0000313|Proteomes:UP000029015};
RA Ventura M., Milani C., Lugli G.A.;
RT "Genomics of Bifidobacteria.";
RL Submitted (MAR-2014) to the EMBL/GenBank/DDBJ databases.
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 -!- SIMILARITY: Belongs to the RibF family.
CC {ECO:0000256|ARBA:ARBA00010214}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFI39435.1}.
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DR EMBL; JGYK01000002; KFI39435.1; -; Genomic_DNA.
DR RefSeq; WP_033504363.1; NZ_JGYK01000002.1.
DR AlphaFoldDB; A0A086YYT5; -.
DR STRING; 1437605.AB656_07170; -.
DR KEGG; bact:AB656_07170; -.
DR PATRIC; fig|1437605.7.peg.1468; -.
DR eggNOG; COG0196; Bacteria.
DR OrthoDB; 9803667at2; -.
DR UniPathway; UPA00277; UER00407.
DR Proteomes; UP000029015; Unassembled WGS sequence.
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: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; IPR015865; Riboflavin_kinase_bac/euk.
DR InterPro; IPR023465; Riboflavin_kinase_dom_sf.
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 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 Flavoprotein {ECO:0000256|ARBA:ARBA00022630};
KW FMN {ECO:0000256|ARBA:ARBA00022643}; Kinase {ECO:0000313|EMBL:KFI39435.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleotidyltransferase {ECO:0000313|EMBL:KFI39435.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000029015};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000313|EMBL:KFI39435.1}.
FT DOMAIN 246..411
FT /note="Riboflavin kinase"
FT /evidence="ECO:0000259|SMART:SM00904"
SQ SEQUENCE 417 AA; 45089 MW; FD6A8FA56C3F58DC CRC64;
MNVSRLEPDT SGIVDWPTLS TRKQSVVSVG VFDGMHRGHR AVIERLVELA HEQGDYAVVI
MFDPSPKRVH SYAATHGGAE LPDGEPSADP DELMAAGERI RLMRGLGVDW VLSVGYSLAF
AAKSYRYFLG SLAGTIGMRT LVLGQDASMG SGRVGDIRAI QELAEATGVF RLEVVDDAGP
GLTWTPTCHI PVPQGPGEPA DPLEGMNKAE RRAWTKAHAC KHVRAWSSSN VRSLLDQGRI
GAADAVLGRP HVVEGEVVHG EQRGRALGYP TANISPDYSG YMPAEGVYAG WLVDLGPAEE
AERDAKAASG DQDQERVAVS SLEARLAPGS PWRWPADISI GSKETFAEDG RTYERVLEVN
AIAGDDWLEL YGHRVRVEFL AYLRPQEKFA DGDALADQLQ RDAADSLRLA QEAAARS
//