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Database: UniProt
Entry: A0A1M5XXM9_9FIRM
LinkDB: A0A1M5XXM9_9FIRM
Original site: A0A1M5XXM9_9FIRM 
ID   A0A1M5XXM9_9FIRM        Unreviewed;       302 AA.
AC   A0A1M5XXM9;
DT   15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT   15-MAR-2017, sequence version 1.
DT   27-MAR-2024, entry version 24.
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=SAMN02745823_02123 {ECO:0000313|EMBL:SHI04540.1};
OS   Sporobacter termitidis DSM 10068.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Oscillospiraceae;
OC   Sporobacter.
OX   NCBI_TaxID=1123282 {ECO:0000313|EMBL:SHI04540.1, ECO:0000313|Proteomes:UP000183995};
RN   [1] {ECO:0000313|EMBL:SHI04540.1, ECO:0000313|Proteomes:UP000183995}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 10068 {ECO:0000313|EMBL:SHI04540.1,
RC   ECO:0000313|Proteomes:UP000183995};
RA   Jaros S., Januszkiewicz K., Wedrychowicz H.;
RL   Submitted (NOV-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}.
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DR   EMBL; FQXV01000006; SHI04540.1; -; Genomic_DNA.
DR   RefSeq; WP_073078610.1; NZ_FQXV01000006.1.
DR   AlphaFoldDB; A0A1M5XXM9; -.
DR   STRING; 1123282.SAMN02745823_02123; -.
DR   OrthoDB; 9803667at2; -.
DR   UniPathway; UPA00276; UER00406.
DR   UniPathway; UPA00277; UER00407.
DR   Proteomes; UP000183995; 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:SHI04540.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR004491};
KW   Nucleotidyltransferase {ECO:0000256|PIRNR:PIRNR004491,
KW   ECO:0000313|EMBL:SHI04540.1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000183995};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR004491}.
FT   DOMAIN          171..297
FT                   /note="Riboflavin kinase"
FT                   /evidence="ECO:0000259|SMART:SM00904"
SQ   SEQUENCE   302 AA;  33762 MW;  64A0F4585808979F CRC64;
     MTEKKRVIAL GFFDGLHIGH SALMERVLKI AKEKDLLPSV ITFDNHPASM VAGQPIPLIN
     SCEDRAGLIH RIFGINNVII LHFDKDLMRM PWTEFVERLS NEFNAAYLVA GHDFTFGHKG
     EGTAEKLAQK SRELGIGCDI IPAVTYKGVV SSSTYIRKLI AEGDIEQANE FLGHPHVLTD
     IVHYGYRLGR TLGTPTINMC FQAGVIIPAY GVYATRVYLE DGSEHIGVTN VGIRPTVNHT
     ETVTAETYIL DYSGNLYGKM VRVEFYKRLR PEIKFSGIDA LKAQIHADAE SARNYFTRLY
     SK
//
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