UniProt: Q87BL4

Database: UniProt
Entry: Q87BL4_XYLFT

LinkDB:  Q87BL4_XYLFT 
Original site:  Q87BL4_XYLFT

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Ontology (7)   
   GO (7)   
Chemical reaction (2)   
   KEGG ENZYME (2)   
Gene (2)   
   KEGG GENES (1)   
   NCBI-Gene (1)   
Protein sequence (1)   
   RefSeq(pep) (1)   
DNA sequence (1)   
   EMBL (1)   
Protein domain (9)   
   InterPro (6)   
   Pfam (2)   
   SMART (1)   
Literature (1)   
   PubMed (1)   
All databases (23)   

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ID   Q87BL4_XYLFT            Unreviewed;       315 AA.
AC   Q87BL4;
DT   01-JUN-2003, integrated into UniProtKB/TrEMBL.
DT   01-JUN-2003, sequence version 1.
DT   27-MAR-2024, entry version 104.
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:AAO29282.1};
GN   OrderedLocusNames=PD_1438 {ECO:0000313|EMBL:AAO29282.1};
OS   Xylella fastidiosa (strain Temecula1 / ATCC 700964).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Xanthomonadales;
OC   Xanthomonadaceae; Xylella.
OX   NCBI_TaxID=183190 {ECO:0000313|EMBL:AAO29282.1, ECO:0000313|Proteomes:UP000002516};
RN   [1] {ECO:0000313|EMBL:AAO29282.1, ECO:0000313|Proteomes:UP000002516}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Temecula1 / ATCC 700964 {ECO:0000313|Proteomes:UP000002516};
RX   PubMed=12533478; DOI=10.1128/JB.185.3.1018-1026.2003;
RA   Van Sluys M.A., de Oliveira M.C., Monteiro-Vitorello C.B., Miyaki C.Y.,
RA   Furlan L.R., Camargo L.E., da Silva A.C., Moon D.H., Takita M.A.,
RA   Lemos E.G., Machado M.A., Ferro M.I., da Silva F.R., Goldman M.H.,
RA   Goldman G.H., Lemos M.V., El-Dorry H., Tsai S.M., Carrer H., Carraro D.M.,
RA   de Oliveira R.C., Nunes L.R., Siqueira W.J., Coutinho L.L., Kimura E.T.,
RA   Ferro E.S., Harakava R., Kuramae E.E., Marino C.L., Giglioti E.,
RA   Abreu I.L., Alves L.M., do Amaral A.M., Baia G.S., Blanco S.R., Brito M.S.,
RA   Cannavan F.S., Celestino A.V., da Cunha A.F., Fenille R.C., Ferro J.A.,
RA   Formighieri E.F., Kishi L.T., Leoni S.G., Oliveira A.R., Rosa V.E.Jr.,
RA   Sassaki F.T., Sena J.A., de Souza A.A., Truffi D., Tsukumo F., Yanai G.M.,
RA   Zaros L.G., Civerolo E.L., Simpson A.J., Almeida N.F.Jr., Setubal J.C.,
RA   Kitajima J.P.;
RT   "Comparative analyses of the complete genome sequences of Pierce's disease
RT   and citrus variegated chlorosis strains of Xylella fastidiosa.";
RL   J. Bacteriol. 185:1018-1026(2003).
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; AE009442; AAO29282.1; -; Genomic_DNA.
DR   RefSeq; WP_011098115.1; NC_004556.1.
DR   AlphaFoldDB; Q87BL4; -.
DR   DNASU; 1144160; -.
DR   GeneID; 58016962; -.
DR   KEGG; xft:PD_1438; -.
DR   HOGENOM; CLU_048437_0_2_6; -.
DR   UniPathway; UPA00276; UER00406.
DR   UniPathway; UPA00277; UER00407.
DR   Proteomes; UP000002516; Chromosome.
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:AAO29282.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW   ECO:0000256|PIRNR:PIRNR004491};
KW   Nucleotidyltransferase {ECO:0000256|PIRNR:PIRNR004491};
KW   Reference proteome {ECO:0000313|Proteomes:UP000002516};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR004491}.
FT   DOMAIN          184..307
FT                   /note="Riboflavin kinase"
FT                   /evidence="ECO:0000259|SMART:SM00904"
SQ   SEQUENCE   315 AA;  34966 MW;  A62D82C216ED355A CRC64;
     MGSVFRHIEG GMLFPQGSVT CIGAFDGLHL GHRALVRHAL QRATALHLPT VALSFEPLPR
     EYFASTTPPP RLTLTRAKIQ GLHRFGADSV GLLRFDSRLA SMSPQTFVER VLLGRLGVRE
     VLIGPQFRFG HQRSGDIALL QRLGLEHGFT ATEIPPLHLN NERISATKIR ALLAAGDFAH
     AAELLGRPYM IGGRVVRGQQ LGSTLGYPTA NLRFPHPIAL SGIYATWVHG IFEQPWPSVS
     SFGTRPTVAG VEPLLEVHLF DFHSDLYGRR IDVEFIAKLR DEETFPDLHT MTTQIHRDAQ
     QARHILSEHR LRATA
//

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