ID J3GK56_9PSED Unreviewed; 316 AA.
AC J3GK56;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 45.
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=PMI30_02243 {ECO:0000313|EMBL:EJM67207.1};
OS Pseudomonas sp. GM50.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1144332 {ECO:0000313|EMBL:EJM67207.1, ECO:0000313|Proteomes:UP000007513};
RN [1] {ECO:0000313|EMBL:EJM67207.1, ECO:0000313|Proteomes:UP000007513}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GM50 {ECO:0000313|EMBL:EJM67207.1,
RC ECO:0000313|Proteomes:UP000007513};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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}.
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:EJM67207.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AKJK01000047; EJM67207.1; -; Genomic_DNA.
DR RefSeq; WP_007901886.1; NZ_AKJK01000047.1.
DR AlphaFoldDB; J3GK56; -.
DR PATRIC; fig|1144332.3.peg.2164; -.
DR UniPathway; UPA00276; UER00406.
DR UniPathway; UPA00277; UER00407.
DR Proteomes; UP000007513; Unassembled WGS sequence.
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:EJM67207.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR004491};
KW Nucleotidyltransferase {ECO:0000256|PIRNR:PIRNR004491,
KW ECO:0000313|EMBL:EJM67207.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR004491}.
FT DOMAIN 183..307
FT /note="Riboflavin kinase"
FT /evidence="ECO:0000259|SMART:SM00904"
SQ SEQUENCE 316 AA; 34794 MW; D7B5FBEA566315E9 CRC64;
MQLVRGLHNL RPQHRGCVAT IGNFDGVHRG HQAILARLRE RALELGVPSC VVIFEPQPRE
FFAPDTAPAR LARLRDKLQL LALEGVDRVL CLAFNQRLSK LSASEFVDTI LVDGLGVQHL
EVGDDFRFGC DRLGDFDFLQ QAGVLQGFTV EAAQTVELDG IRVSSTQVRN ALAAADFALA
ERLLGRPYRI AGRVLHGQKL ARQLGTPTAN IQLKRRRVPL SGVYLVNVDI DGKTWPGVAN
IGVRPTVQGD GKAHLEVHLL DFAGDLYDRR LTVVFHHKLR EEQRFASLEA LKTAINADVA
AARALSHLAP IANEEP
//
