ID J2HEC1_9CAUL Unreviewed; 317 AA.
AC J2HEC1;
DT 03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT 03-OCT-2012, sequence version 1.
DT 27-MAR-2024, entry version 51.
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=PMI01_01878 {ECO:0000313|EMBL:EJL33923.1};
OS Caulobacter sp. AP07.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Caulobacterales;
OC Caulobacteraceae; Caulobacter.
OX NCBI_TaxID=1144304 {ECO:0000313|EMBL:EJL33923.1, ECO:0000313|Proteomes:UP000007300};
RN [1] {ECO:0000313|EMBL:EJL33923.1, ECO:0000313|Proteomes:UP000007300}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AP07 {ECO:0000313|EMBL:EJL33923.1,
RC ECO:0000313|Proteomes:UP000007300};
RX PubMed=23045501; DOI=10.1128/JB.01243-12;
RA Brown S.D., Utturkar S.M., Klingeman D.M., Johnson C.M., Martin S.L.,
RA Land M.L., Lu T.Y., Schadt C.W., Doktycz M.J., Pelletier D.A.;
RT "Twenty-one genome sequences from Pseudomonas species and 19 genome
RT sequences from diverse bacteria isolated from the rhizosphere and
RT endosphere of Populus deltoides.";
RL J. Bacteriol. 194:5991-5993(2012).
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:EJL33923.1}.
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DR EMBL; AKKF01000131; EJL33923.1; -; Genomic_DNA.
DR RefSeq; WP_007667007.1; NZ_AKKF01000131.1.
DR AlphaFoldDB; J2HEC1; -.
DR PATRIC; fig|1144304.3.peg.1760; -.
DR UniPathway; UPA00276; UER00406.
DR UniPathway; UPA00277; UER00407.
DR Proteomes; UP000007300; 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:EJL33923.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|PIRNR:PIRNR004491};
KW Nucleotidyltransferase {ECO:0000256|PIRNR:PIRNR004491,
KW ECO:0000313|EMBL:EJL33923.1};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR004491}.
FT DOMAIN 190..314
FT /note="Riboflavin kinase"
FT /evidence="ECO:0000259|SMART:SM00904"
SQ SEQUENCE 317 AA; 34741 MW; 82CF6B032D8860AD CRC64;
MRLKIVHGWK DLPEEQRGAA VALGNFDGVH RGHQQVIAQA AKAALTAKVP LGVVTFDPHP
RRLFRPSEPA FKLMTHDQQA RALEALGVDI LYLLPFDFEM ASFGDREFVE RVLVGGPGEG
LGVKHVAVGF DISFGRGRTG SADLMKTYGQ QDGFSVSVAE PVASRDGEKF SSTAVRCALR
DGHPEQAARI LGRPFAIEGV VRRGQQLGRQ LGFPTANVEV EDYVVPKLGV YATRTRLPDG
RLVPGVANLG NNPTTGVVET RLETWLFDFD EDLYGQIIET QLITFLRPEL KFDSIELLVE
QVLRDEVAAR AIVAPGF
//
