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Database: UniProt
Entry: A0A1M3KF51_9CHLR
LinkDB: A0A1M3KF51_9CHLR
Original site: A0A1M3KF51_9CHLR 
ID   A0A1M3KF51_9CHLR        Unreviewed;       323 AA.
AC   A0A1M3KF51;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 22.
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=BGO78_04255 {ECO:0000313|EMBL:OJX46105.1};
OS   Chloroflexi bacterium 44-23.
OC   Bacteria; Chloroflexota.
OX   NCBI_TaxID=1895927 {ECO:0000313|EMBL:OJX46105.1, ECO:0000313|Proteomes:UP000184201};
RN   [1] {ECO:0000313|EMBL:OJX46105.1, ECO:0000313|Proteomes:UP000184201}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=44-23 {ECO:0000313|EMBL:OJX46105.1};
RA   Kantor R.S., Huddy R.J., Iyer R., Thomas B.C., Brown C.T., Anantharaman K.,
RA   Tringe S., Hettich R.L., Harrison S.T., Banfield J.F.;
RT   "Genome-resolved meta-omics ties microbial dynamics to process performance
RT   in biotechnology for thiocyanate degradation.";
RL   Submitted (SEP-2016) 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:OJX46105.1}.
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DR   EMBL; MKUW01000007; OJX46105.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A1M3KF51; -.
DR   STRING; 1895927.BGO78_04255; -.
DR   UniPathway; UPA00276; UER00406.
DR   UniPathway; UPA00277; UER00407.
DR   Proteomes; UP000184201; 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   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR004491}.
FT   DOMAIN          180..306
FT                   /note="Riboflavin kinase"
FT                   /evidence="ECO:0000259|SMART:SM00904"
SQ   SEQUENCE   323 AA;  35921 MW;  AE7FF84E24295498 CRC64;
     MKHLRELTSL PTTGLYAAIG TFDGVHTGHQ QLIQAMVNQA QKTSTECAVI TFFPIPAIVI
     RNIQTPITLT SPEEKAALFE KLGLNYTITL QFTKEMAQLT PTEFIDLLVS NLPIKQIWVG
     EDFTFGHQRR GNTTVLSQLG MQYGFETIIV KHFLQNSEKI SSSQIRNWLT SGDLESANKA
     LGRPYSITGV VKHGDQRGSK IGFPTANLAV WEGKLLPASG VYATFAQVEG KIYTSVTNIG
     FRPTFVDNEP NAQVECYIHN FDRNIYDLPV QLFLVSRIRA EKRFESISAL IQQIKNDAAK
     SEEILKHAEF QTGLLTGSTK TAP
//
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