ID Q2G2Q2_STAA8 Unreviewed; 323 AA.
AC Q2G2Q2;
DT 21-MAR-2006, integrated into UniProtKB/TrEMBL.
DT 21-MAR-2006, sequence version 1.
DT 27-MAR-2024, entry version 103.
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 OrderedLocusNames=SAOUHSC_01249 {ECO:0000313|EMBL:ABD30350.1};
OS Staphylococcus aureus (strain NCTC 8325 / PS 47).
OC Bacteria; Bacillota; Bacilli; Bacillales; Staphylococcaceae;
OC Staphylococcus.
OX NCBI_TaxID=93061 {ECO:0000313|EMBL:ABD30350.1, ECO:0000313|Proteomes:UP000008816};
RN [1] {ECO:0000313|Proteomes:UP000008816}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC 8325 / PS 47 {ECO:0000313|Proteomes:UP000008816};
RA Gillaspy A.F., Worrell V., Orvis J., Roe B.A., Dyer D.W., Iandolo J.J.;
RT "The Staphylococcus aureus NCTC 8325 genome.";
RL (In) Fischetti V., Novick R., Ferretti J., Portnoy D., Rood J. (eds.);
RL Gram positive pathogens, 2nd edition, pp.381-412, ASM Press, Washington D.C
RL (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; CP000253; ABD30350.1; -; Genomic_DNA.
DR RefSeq; WP_000864185.1; NZ_LS483365.1.
DR RefSeq; YP_499782.1; NC_007795.1.
DR AlphaFoldDB; Q2G2Q2; -.
DR SMR; Q2G2Q2; -.
DR STRING; 93061.SAOUHSC_01249; -.
DR PaxDb; 1280-SAXN108_1276; -.
DR GeneID; 3919980; -.
DR KEGG; sao:SAOUHSC_01249; -.
DR PATRIC; fig|93061.5.peg.1143; -.
DR eggNOG; COG0196; Bacteria.
DR HOGENOM; CLU_048437_0_2_9; -.
DR OrthoDB; 9803667at2; -.
DR UniPathway; UPA00276; UER00406.
DR UniPathway; UPA00277; UER00407.
DR Proteomes; UP000008816; 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; IBA:GO_Central.
DR GO; GO:0006747; P:FAD biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0009398; P:FMN biosynthetic process; IBA:GO_Central.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:InterPro.
DR GO; GO:0006771; P:riboflavin metabolic process; IBA:GO_Central.
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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR004491};
KW Nucleotidyltransferase {ECO:0000256|PIRNR:PIRNR004491};
KW Reference proteome {ECO:0000313|Proteomes:UP000008816};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR004491}.
FT DOMAIN 183..312
FT /note="Riboflavin kinase"
FT /evidence="ECO:0000259|SMART:SM00904"
SQ SEQUENCE 323 AA; 36692 MW; DC65B31BAF8AAB80 CRC64;
MKVIEVTHPI QSKQYITEDV AMAFGFFDGM HKGHDKVFDI LNEIAEARSL KKAVMTFDPH
PSVVLNPKRK RTTYLTPLSD KIEKISQHDI DYCIVVNFSS RFANVSVEDF VENYIIKNNV
KEVIAGFDFT FGKFGKGNMT VLQEYDAFNT TIVSKQEIEN EKISTTSIRQ DLINGELQKA
NDALGYIYSI KGTVVQGEKR GRTIGFPTAN IQPSDDYLLP RKGVYAVSIE IGTENKLYRG
VANIGVKPTF HDPNKAEVVI EVNIFDFEDN IYGERVTVNW HHFLRPEIKF DGIDPLVKQM
NDDKSRAKYL LAVDFGDEVA YNI
//
