(data stored in SCRATCH zone)

SWISSPROT: C8U198_ECO10

ID   C8U198_ECO10            Unreviewed;       313 AA.
AC   C8U198;
DT   03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT   03-NOV-2009, sequence version 1.
DT   08-MAY-2019, entry version 55.
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:BAI28906.1};
GN   OrderedLocusNames=ECO103_0026 {ECO:0000313|EMBL:BAI28906.1};
OS   Escherichia coli O103:H2 (strain 12009 / EHEC).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC   Enterobacteriaceae; Escherichia.
OX   NCBI_TaxID=585395 {ECO:0000313|EMBL:BAI28906.1, ECO:0000313|Proteomes:UP000000959};
RN   [1] {ECO:0000313|EMBL:BAI28906.1, ECO:0000313|Proteomes:UP000000959}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=12009 / EHEC {ECO:0000313|Proteomes:UP000000959};
RX   PubMed=19815525; DOI=10.1073/pnas.0903585106;
RA   Ogura Y., Ooka T., Iguchi A., Toh H., Asadulghani M., Oshima K.,
RA   Kodama T., Abe H., Nakayama K., Kurokawa K., Tobe T., Hattori M.,
RA   Hayashi T.;
RT   "Comparative genomics reveal the mechanism of the parallel evolution
RT   of O157 and non-O157 enterohemorrhagic Escherichia coli.";
RL   Proc. Natl. Acad. Sci. U.S.A. 106:17939-17944(2009).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + FMN + H(+) = diphosphate + FAD;
CC         Xref=Rhea:RHEA:17237, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:33019, ChEBI:CHEBI:57692, ChEBI:CHEBI:58210;
CC         EC=2.7.7.2; Evidence={ECO:0000256|PIRNR:PIRNR004491};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + riboflavin = ADP + FMN + H(+);
CC         Xref=Rhea:RHEA:14357, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:57986, ChEBI:CHEBI:58210, ChEBI:CHEBI:456216;
CC         EC=2.7.1.26; Evidence={ECO:0000256|PIRNR:PIRNR004491};
CC   -!- PATHWAY: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN:
CC       step 1/1. {ECO:0000256|PIRNR:PIRNR004491}.
CC   -!- PATHWAY: Cofactor biosynthesis; FMN biosynthesis; FMN from
CC       riboflavin (ATP route): step 1/1. {ECO:0000256|PIRNR:PIRNR004491}.
CC   -!- SIMILARITY: Belongs to the ribF family.
CC       {ECO:0000256|PIRNR:PIRNR004491}.
CC   -----------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   -----------------------------------------------------------------------
DR   EMBL; AP010958; BAI28906.1; -; Genomic_DNA.
DR   RefSeq; WP_000767329.1; NC_013353.1.
DR   SMR; C8U198; -.
DR   EnsemblBacteria; BAI28906; BAI28906; ECO103_0026.
DR   KEGG; eoh:ECO103_0026; -.
DR   HOGENOM; HOG000006845; -.
DR   KO; K11753; -.
DR   OMA; HRGHQAI; -.
DR   BioCyc; ECOL585395:ECO103_RS00130-MONOMER; -.
DR   UniPathway; UPA00276; UER00406.
DR   UniPathway; UPA00277; UER00407.
DR   Proteomes; UP000000959; 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:0009231; P:riboflavin biosynthetic process; IEA:InterPro.
DR   CDD; cd02064; FAD_synthetase_N; 1.
DR   Gene3D; 2.40.30.30; -; 1.
DR   Gene3D; 3.40.50.620; -; 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   PANTHER; PTHR22749; PTHR22749; 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; SSF82114; SSF82114; 1.
DR   TIGRFAMs; TIGR00083; ribF; 1.
PE   3: Inferred from homology;
DR   PRODOM; C8U198.
DR   SWISS-2DPAGE; C8U198.
KW   ATP-binding {ECO:0000256|PIRNR:PIRNR004491};
KW   Complete proteome {ECO:0000313|Proteomes:UP000000959};
KW   FAD {ECO:0000256|PIRNR:PIRNR004491};
KW   Flavoprotein {ECO:0000256|PIRNR:PIRNR004491};
KW   FMN {ECO:0000256|PIRNR:PIRNR004491};
KW   Kinase {ECO:0000256|PIRNR:PIRNR004491, ECO:0000313|EMBL:BAI28906.1};
KW   Nucleotide-binding {ECO:0000256|PIRNR:PIRNR004491};
KW   Nucleotidyltransferase {ECO:0000256|PIRNR:PIRNR004491};
KW   Transferase {ECO:0000256|PIRNR:PIRNR004491}.
FT   DOMAIN      184    308       Flavokinase. {ECO:0000259|SMART:SM00904}.
SQ   SEQUENCE   313 AA;  34734 MW;  C0B2EF5499CD30FE CRC64;
     MKLIRGIHNL SQAPQEGCVL TIGNFDGVHR GHRALLQGLQ EEGRKRNLPV MVMLFEPQPL
     ELFATDKAPA RLTRLREKLR YLAECGVDYV LCVRFDRRFA ALTAQNFISD LLVKHLRVKF
     LAVGDDFRFG AGREGDFLLL QKAGMEYGFD ITSTQTFCEG GVRISSTAVR QALADDNLAL
     AESLLGHPFA ISGRVVHGDE LGRTIGFPTA NVPLRRQVSP VKGVYAVEVL GLGEKPLPGV
     ANIGTRPTVA GIRQQLEVHL LDVAMDLYGR HIQVVLRKKI RNEQRFASLD ELKAQIARDE
     LTAREFFGLT KPA
//

If you have problems or comments...

PBIL Back to PBIL home page