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Database: UniProt
Entry: A0A0L0GKE0_9ENTR
LinkDB: A0A0L0GKE0_9ENTR
Original site: A0A0L0GKE0_9ENTR 
ID   A0A0L0GKE0_9ENTR        Unreviewed;       312 AA.
AC   A0A0L0GKE0;
DT   11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT   11-NOV-2015, sequence version 1.
DT   27-MAR-2024, entry version 38.
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=GM31_11615 {ECO:0000313|EMBL:KNC88122.1};
OS   Trabulsiella odontotermitis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Trabulsiella.
OX   NCBI_TaxID=379893 {ECO:0000313|EMBL:KNC88122.1, ECO:0000313|Proteomes:UP000037393};
RN   [1] {ECO:0000313|EMBL:KNC88122.1, ECO:0000313|Proteomes:UP000037393}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12 {ECO:0000313|EMBL:KNC88122.1,
RC   ECO:0000313|Proteomes:UP000037393};
RX   PubMed=26162887;
RA   Sapountzis P., Gruntjes T., Otani S., Estevez J., da Costa R.R.,
RA   Plunkett G.3rd., Perna N.T., Poulsen M.;
RT   "The Enterobacterium Trabulsiella odontotermitis Presents Novel Adaptations
RT   Related to Its Association with Fungus-Growing Termites.";
RL   Appl. Environ. Microbiol. 81:6577-6588(2015).
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:KNC88122.1}.
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DR   EMBL; JNGI01000185; KNC88122.1; -; Genomic_DNA.
DR   RefSeq; WP_049849782.1; NZ_JNGI01000185.1.
DR   AlphaFoldDB; A0A0L0GKE0; -.
DR   STRING; 379893.GCA_001297775_01983; -.
DR   PATRIC; fig|379893.3.peg.1916; -.
DR   OrthoDB; 9803667at2; -.
DR   UniPathway; UPA00276; UER00406.
DR   UniPathway; UPA00277; UER00407.
DR   Proteomes; UP000037393; 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; IPR004821; Cyt_trans-like.
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; TIGR00125; cyt_tran_rel; 1.
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|ARBA:ARBA00022695,
KW   ECO:0000256|PIRNR:PIRNR004491};
KW   Reference proteome {ECO:0000313|Proteomes:UP000037393};
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   312 AA;  34447 MW;  3D5D7E5587F476A1 CRC64;
     MKLIRGIHNL SQAPHGCVLT IGNFDGVHRG HQALLQRLRE EGRERGVPVV VMIFEPQPLE
     LFSAEKAPAR LTRLREKLRY LAESGVDYVL CVRFDRRFAA LTAQTFISDL LVKRLGVQYL
     AVGDDFRFGA GRQGDFLLLQ KAGAEFGFSV TSTQTFCEGG VRISSTAVRQ ALADDDLLQA
     EKLLGHPFII SGRVVHGDEL GRTIGFPTAN LPLRRQVSPV KGVYAVEVAG LGNTLLPGVA
     NIGTRPTVSG VRQQLEVHLL DVAMDLYGRH IDVILRKKIR NEQRFASLDE LKAQIARDEL
     TARDFFGLSN PA
//
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