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Database: UniProt
Entry: A0A089PVK9_PLUGE
LinkDB: A0A089PVK9_PLUGE
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ID   A0A089PVK9_PLUGE        Unreviewed;       312 AA.
AC   A0A089PVK9;
DT   26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT   26-NOV-2014, sequence version 1.
DT   27-MAR-2024, entry version 57.
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   Name=ribF {ECO:0000313|EMBL:SUB73326.1};
GN   ORFNames=ABW06_15265 {ECO:0000313|EMBL:KMK12619.1}, NCTC11434_04832
GN   {ECO:0000313|EMBL:SUB73326.1};
OS   Pluralibacter gergoviae (Enterobacter gergoviae).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Pluralibacter.
OX   NCBI_TaxID=61647 {ECO:0000313|EMBL:KMK12619.1, ECO:0000313|Proteomes:UP000036196};
RN   [1] {ECO:0000313|EMBL:KMK12619.1, ECO:0000313|Proteomes:UP000036196}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JS81F13 {ECO:0000313|EMBL:KMK12619.1,
RC   ECO:0000313|Proteomes:UP000036196};
RA   Greninger A.L., Miller S.;
RT   "Genome sequences of Pluralibacter gergoviae.";
RL   Submitted (MAY-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:SUB73326.1, ECO:0000313|Proteomes:UP000254381}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC11434 {ECO:0000313|EMBL:SUB73326.1,
RC   ECO:0000313|Proteomes:UP000254381};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; LDZF01000016; KMK12619.1; -; Genomic_DNA.
DR   EMBL; UGTG01000002; SUB73326.1; -; Genomic_DNA.
DR   RefSeq; WP_043086068.1; NZ_VWRP01000040.1.
DR   STRING; 61647.LG71_24895; -.
DR   GeneID; 61383403; -.
DR   KEGG; pge:LG71_24895; -.
DR   PATRIC; fig|61647.13.peg.4020; -.
DR   eggNOG; COG0196; Bacteria.
DR   OrthoDB; 9803667at2; -.
DR   UniPathway; UPA00276; UER00406.
DR   UniPathway; UPA00277; UER00407.
DR   Proteomes; UP000036196; Unassembled WGS sequence.
DR   Proteomes; UP000254381; 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|ARBA:ARBA00022695,
KW   ECO:0000256|PIRNR:PIRNR004491};
KW   Reference proteome {ECO:0000313|Proteomes:UP000036196};
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;  34232 MW;  9271F9390D446061 CRC64;
     MKLIRGIHNL GQAPRGCVLT IGNFDGVHRG HQALLQRLQM EGRERGLPVV VMIFEPQPLE
     MFAMDKAPAR LTRLREKVAY LAASGVDYVL CVRFDRRFAA LTAQQFIRDL LVKQLGVQFL
     AVGDDFRFGA GREGDFLLLQ KAGAEFGFDV TSTHTFCEGG LRISSTAVRQ ALASDDLALA
     ETLLGHPFVI SGRVVHGDAL GRTIGFPTAN LPLRRQVSPV KGVYAVEVAG LGETLLPGVA
     NVGTRPTVSG VRQQLEVHLL DVAMDLYGRH IDVILRKKIR NEQRFASLDE LKAQIARDEL
     TAREYLGLSN PA
//
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