ID K9CL93_9FIRM Unreviewed; 319 AA.
AC K9CL93;
DT 06-FEB-2013, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2013, 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=HMPREF9161_00331 {ECO:0000313|EMBL:EKU71646.1};
OS Selenomonas sp. F0473.
OC Bacteria; Bacillota; Negativicutes; Selenomonadales; Selenomonadaceae;
OC Selenomonas.
OX NCBI_TaxID=999423 {ECO:0000313|EMBL:EKU71646.1, ECO:0000313|Proteomes:UP000009883};
RN [1] {ECO:0000313|EMBL:EKU71646.1, ECO:0000313|Proteomes:UP000009883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=F0473 {ECO:0000313|EMBL:EKU71646.1,
RC ECO:0000313|Proteomes:UP000009883};
RG The Broad Institute Genome Sequencing Platform;
RA Earl A., Ward D., Feldgarden M., Gevers D., Blanton J.M., Baranova O.V.,
RA Mathney J., Dewhirst F.E., Izard J., Tanner A.C., Walker B., Young S.K.,
RA Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA Arachchi H.M., Berlin A., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
RA Hansen M., Howarth C., Imamovic A., Larimer J., McCowen C., Montmayeur A.,
RA Murphy C., Neiman D., Pearson M., Priest M., Roberts A., Saif S., Shea T.,
RA Sisk P., Sykes S., Wortman J., Nusbaum C., Birren B.;
RT "The Genome Sequence of Selenomonas sp. Oral taxon 133 strain F0473.";
RL Submitted (SEP-2012) 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 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:EKU71646.1}.
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; AGZT01000003; EKU71646.1; -; Genomic_DNA.
DR RefSeq; WP_009727940.1; NZ_JH992902.1.
DR AlphaFoldDB; K9CL93; -.
DR STRING; 999423.HMPREF9161_00331; -.
DR PATRIC; fig|999423.3.peg.345; -.
DR eggNOG; COG0196; Bacteria.
DR HOGENOM; CLU_048437_0_2_9; -.
DR OrthoDB; 9803667at2; -.
DR UniPathway; UPA00276; UER00406.
DR UniPathway; UPA00277; UER00407.
DR Proteomes; UP000009883; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR004491};
KW Nucleotidyltransferase {ECO:0000256|PIRNR:PIRNR004491};
KW Reference proteome {ECO:0000313|Proteomes:UP000009883};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR004491}.
FT DOMAIN 182..306
FT /note="Riboflavin kinase"
FT /evidence="ECO:0000259|SMART:SM00904"
SQ SEQUENCE 319 AA; 36042 MW; CAE7492CF5FAB4E1 CRC64;
MESYKKLVEF YALYPRIVIA LGMFDGIHLG HQRIIKTAVK KAHEIGGTAL VFSFLNHPRS
VVDPEGSPRR IDSDILRQKI LKNLGVDVLV EIPFTPHFAK TDALDFVEFL HRNFAPKYIV
IGENYTFGRY GRGTPVLLRQ EAGRYGFQTI ICPPVICDGE TISSTCVRKL IQQGNIAKVN
EYLGYPFSIM GIVVHGKARG RQLGFPTANI ELHQENEILS NGVYAVTVQQ GTVRYGGVAN
IGNNPTFEDC KRRLEVHIFD FFKDIYGENL TVSFYARIRK ERRFSSIDSL IAQIECDKKA
AISLIAENFH LQENISMII
//
