ID A0A1F9VQN2_9BACT Unreviewed; 317 AA.
AC A0A1F9VQN2;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 17.
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 ORFNames=A3G41_02235 {ECO:0000313|EMBL:OGS05169.1};
OS Elusimicrobia bacterium RIFCSPLOWO2_12_FULL_59_9.
OC Bacteria; Elusimicrobiota.
OX NCBI_TaxID=1797952 {ECO:0000313|EMBL:OGS05169.1, ECO:0000313|Proteomes:UP000176685};
RN [1] {ECO:0000313|EMBL:OGS05169.1, ECO:0000313|Proteomes:UP000176685}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=27774985; DOI=10.1038/ncomms13219;
RA Anantharaman K., Brown C.T., Hug L.A., Sharon I., Castelle C.J.,
RA Probst A.J., Thomas B.C., Singh A., Wilkins M.J., Karaoz U., Brodie E.L.,
RA Williams K.H., Hubbard S.S., Banfield J.F.;
RT "Thousands of microbial genomes shed light on interconnected biogeochemical
RT processes in an aquifer system.";
RL Nat. Commun. 7:13219-13219(2016).
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}.
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:OGS05169.1}.
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DR EMBL; MGUX01000039; OGS05169.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1F9VQN2; -.
DR STRING; 1797952.A3G41_02235; -.
DR UniPathway; UPA00276; UER00406.
DR UniPathway; UPA00277; UER00407.
DR Proteomes; UP000176685; 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: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 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};
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 169..297
FT /note="Riboflavin kinase"
FT /evidence="ECO:0000259|SMART:SM00904"
FT NON_TER 317
FT /evidence="ECO:0000313|EMBL:OGS05169.1"
SQ SEQUENCE 317 AA; 35226 MW; AB73B535DAE3A12A CRC64;
MKNLVTIGTF DGIHLGHQAL IRKAVRRARR DGMRSLVVVF NRPPRLFFNP RLHIPLITTA
AERAALLGEL GVDKVITLDF DARLAAMSAE RFFTDFLLKK NKMGCLLVGS DFALGKDRAG
TPEALQELCR RHSVAFEACP ILNRRRAKVS SRRIRGLLSE GKIRQAERLL GYRYFLCGKV
VRGRRLGRTI GFPTANLAVP DGKILPPGVF HASVRAGGRR YPAALNVGHR PTAAPPGRAL
KSTSPQAEAH LIGFKGRLVG KTLRVELIRL LRAEKKFDSV SALARQIRAD VARIRRADII
RSRRPARPAT GPGFRRY
//
