RISA_ECOLI
ID RISA_ECOLI Reviewed; 213 AA.
AC P0AFU8; P29015;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 127.
DE RecName: Full=Riboflavin synthase;
DE Short=RS;
DE EC=2.5.1.9;
GN Name=ribC; Synonyms=ribE; OrderedLocusNames=b1662, JW1654;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], FUNCTION, CATALYTIC ACTIVITY, AND
RP SUBUNIT.
RC STRAIN=K12 / RR28;
RX PubMed=9022701; DOI=10.1111/j.1432-1033.1996.0712r.x;
RA Eberhardt S.M.R., Richter G., Gimbel W., Werner T., Bacher A.;
RT "Cloning, sequencing, mapping and hyperexpression of the ribC gene coding
RT for riboflavin synthase of Escherichia coli.";
RL Eur. J. Biochem. 242:712-719(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9023191; DOI=10.1128/jb.179.4.1105-1111.1997;
RA Hensel M., Shea J.E., Baeumler A.J., Gleeson C., Blattner F.R.,
RA Holden D.W.;
RT "Analysis of the boundaries of Salmonella pathogenicity island 2 and the
RT corresponding chromosomal region of Escherichia coli K-12.";
RL J. Bacteriol. 179:1105-1111(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=9097039; DOI=10.1093/dnares/3.6.363;
RA Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T.,
RA Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K.,
RA Miki T., Mizobuchi K., Mori H., Mori T., Motomura K., Nakade S.,
RA Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G.,
RA Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y.,
RA Wada C., Yamamoto Y., Horiuchi T.;
RT "A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to
RT the 28.0-40.1 min region on the linkage map.";
RL DNA Res. 3:363-377(1996).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [6]
RP STRUCTURE BY NMR OF 1-97 IN COMPLEX WITH RIBOFLAVIN.
RX PubMed=11399071; DOI=10.1006/jmbi.2001.4683;
RA Truffault V., Coles M., Diercks T., Abelmann K., Eberhardt S., Luttgen H.,
RA Bacher A., Kessler H.;
RT "The solution structure of the N-terminal domain of riboflavin synthase.";
RL J. Mol. Biol. 309:949-960(2001).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=11377200; DOI=10.1016/s0969-2126(01)00600-1;
RA Liao D.I., Wawrzak Z., Calabrese J.C., Viitanen P.V., Jordan D.B.;
RT "Crystal structure of riboflavin synthase.";
RL Structure 9:399-408(2001).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.60 ANGSTROMS) OF 1-97 IN COMPLEX WITH RIBOFLAVIN.
RX PubMed=12927541; DOI=10.1016/s0022-2836(03)00844-1;
RA Meining W., Eberhardt S., Bacher A., Ladenstein R.;
RT "The structure of the N-terminal domain of riboflavin synthase in complex
RT with riboflavin at 2.6A resolution.";
RL J. Mol. Biol. 331:1053-1063(2003).
CC -!- FUNCTION: Catalyzes the dismutation of two molecules of 6,7-dimethyl-8-
CC ribityllumazine, resulting in the formation of riboflavin and 5-amino-
CC 6-(D-ribitylamino)uracil. {ECO:0000269|PubMed:9022701}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) = 5-amino-6-(D-
CC ribitylamino)uracil + riboflavin; Xref=Rhea:RHEA:20772,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:57986,
CC ChEBI:CHEBI:58201; EC=2.5.1.9; Evidence={ECO:0000269|PubMed:9022701};
CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin
CC from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-
CC ribitylamino)uracil: step 2/2.
CC -!- SUBUNIT: Homotrimer. Unlike in B.subtilis, does not interact with 6,7-
CC dimethyl-8-ribityllumazine synthase. {ECO:0000269|PubMed:11399071,
CC ECO:0000269|PubMed:12927541, ECO:0000269|PubMed:9022701}.
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DR EMBL; X69109; CAA48861.1; -; Genomic_DNA.
DR EMBL; U68703; AAB47940.1; -; Genomic_DNA.
DR EMBL; U00096; AAC74734.1; -; Genomic_DNA.
DR EMBL; AP009048; BAA15429.1; -; Genomic_DNA.
DR PIR; S28526; S28526.
DR RefSeq; NP_416179.1; NC_000913.3.
DR RefSeq; WP_000493947.1; NZ_SSZK01000001.1.
DR PDB; 1HZE; NMR; -; A/B=1-97.
DR PDB; 1I18; NMR; -; A/B=1-97.
DR PDB; 1I8D; X-ray; 2.00 A; A/B/C=1-213.
DR PDB; 1PKV; X-ray; 2.60 A; A/B=1-97.
DR PDBsum; 1HZE; -.
DR PDBsum; 1I18; -.
DR PDBsum; 1I8D; -.
DR PDBsum; 1PKV; -.
DR AlphaFoldDB; P0AFU8; -.
DR BMRB; P0AFU8; -.
DR SMR; P0AFU8; -.
DR BioGRID; 4261654; 49.
DR DIP; DIP-47865N; -.
DR IntAct; P0AFU8; 3.
DR STRING; 511145.b1662; -.
DR DrugBank; DB00140; Riboflavin.
DR SWISS-2DPAGE; P0AFU8; -.
DR jPOST; P0AFU8; -.
DR PaxDb; P0AFU8; -.
DR PRIDE; P0AFU8; -.
DR EnsemblBacteria; AAC74734; AAC74734; b1662.
DR EnsemblBacteria; BAA15429; BAA15429; BAA15429.
DR GeneID; 66674445; -.
DR GeneID; 945848; -.
DR KEGG; ecj:JW1654; -.
DR KEGG; eco:b1662; -.
DR PATRIC; fig|1411691.4.peg.595; -.
DR EchoBASE; EB1378; -.
DR eggNOG; COG0307; Bacteria.
DR HOGENOM; CLU_034388_0_1_6; -.
DR InParanoid; P0AFU8; -.
DR OMA; HILSGHV; -.
DR PhylomeDB; P0AFU8; -.
DR BioCyc; EcoCyc:RIBOFLAVIN-SYN-MON; -.
DR BioCyc; MetaCyc:RIBOFLAVIN-SYN-MON; -.
DR BRENDA; 2.5.1.9; 2026.
DR SABIO-RK; P0AFU8; -.
DR UniPathway; UPA00275; UER00405.
DR EvolutionaryTrace; P0AFU8; -.
DR PRO; PR:P0AFU8; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0005829; C:cytosol; IDA:EcoCyc.
DR GO; GO:0004746; F:riboflavin synthase activity; IDA:EcoCyc.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IDA:EcoCyc.
DR CDD; cd00402; Riboflavin_synthase_like; 1.
DR Gene3D; 2.40.30.20; -; 2.
DR InterPro; IPR023366; ATP_synth_asu-like_sf.
DR InterPro; IPR001783; Lumazine-bd.
DR InterPro; IPR026017; Lumazine-bd_dom.
DR InterPro; IPR017938; Riboflavin_synthase-like_b-brl.
DR PANTHER; PTHR21098; PTHR21098; 1.
DR Pfam; PF00677; Lum_binding; 2.
DR PIRSF; PIRSF000498; Riboflavin_syn_A; 1.
DR SUPFAM; SSF63380; SSF63380; 2.
DR TIGRFAMs; TIGR00187; ribE; 1.
DR PROSITE; PS51177; LUMAZINE_BIND; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Reference proteome; Repeat; Riboflavin biosynthesis;
KW Transferase.
FT CHAIN 1..213
FT /note="Riboflavin synthase"
FT /id="PRO_0000068166"
FT REPEAT 1..97
FT /note="Lumazine-binding 1"
FT REPEAT 98..195
FT /note="Lumazine-binding 2"
FT BINDING 4..6
FT /ligand="2,4-dihydroxypteridine"
FT /ligand_id="ChEBI:CHEBI:16489"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q2YN92,
FT ECO:0000305|PubMed:12927541"
FT BINDING 48..50
FT /ligand="2,4-dihydroxypteridine"
FT /ligand_id="ChEBI:CHEBI:16489"
FT /ligand_label="2"
FT /ligand_note="ligand shared between two trimeric partners"
FT /evidence="ECO:0000250|UniProtKB:Q2YN92,
FT ECO:0000305|PubMed:12927541"
FT BINDING 62..67
FT /ligand="2,4-dihydroxypteridine"
FT /ligand_id="ChEBI:CHEBI:16489"
FT /ligand_label="2"
FT /ligand_note="ligand shared between two trimeric partners"
FT /evidence="ECO:0000250|UniProtKB:Q2YN92,
FT ECO:0000305|PubMed:12927541"
FT BINDING 101..103
FT /ligand="2,4-dihydroxypteridine"
FT /ligand_id="ChEBI:CHEBI:16489"
FT /ligand_label="2"
FT /ligand_note="ligand shared between two trimeric partners"
FT /evidence="ECO:0000250|UniProtKB:Q2YN92"
FT BINDING 137
FT /ligand="2,4-dihydroxypteridine"
FT /ligand_id="ChEBI:CHEBI:16489"
FT /ligand_label="2"
FT /ligand_note="ligand shared between two trimeric partners"
FT /note="in other chain"
FT /evidence="ECO:0000250|UniProtKB:Q2YN92"
FT BINDING 146..148
FT /ligand="2,4-dihydroxypteridine"
FT /ligand_id="ChEBI:CHEBI:16489"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q2YN92"
FT BINDING 160..165
FT /ligand="2,4-dihydroxypteridine"
FT /ligand_id="ChEBI:CHEBI:16489"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:Q2YN92"
FT STRAND 8..17
FT /evidence="ECO:0007829|PDB:1I8D"
FT STRAND 19..27
FT /evidence="ECO:0007829|PDB:1I8D"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:1I8D"
FT STRAND 41..44
FT /evidence="ECO:0007829|PDB:1I8D"
FT STRAND 47..55
FT /evidence="ECO:0007829|PDB:1I8D"
FT STRAND 58..64
FT /evidence="ECO:0007829|PDB:1I8D"
FT HELIX 65..70
FT /evidence="ECO:0007829|PDB:1I8D"
FT HELIX 72..75
FT /evidence="ECO:0007829|PDB:1I8D"
FT STRAND 81..86
FT /evidence="ECO:0007829|PDB:1I8D"
FT STRAND 105..115
FT /evidence="ECO:0007829|PDB:1I8D"
FT STRAND 118..126
FT /evidence="ECO:0007829|PDB:1I8D"
FT HELIX 128..133
FT /evidence="ECO:0007829|PDB:1I8D"
FT STRAND 139..142
FT /evidence="ECO:0007829|PDB:1I8D"
FT STRAND 145..148
FT /evidence="ECO:0007829|PDB:1I8D"
FT STRAND 154..161
FT /evidence="ECO:0007829|PDB:1I8D"
FT HELIX 163..168
FT /evidence="ECO:0007829|PDB:1I8D"
FT HELIX 171..173
FT /evidence="ECO:0007829|PDB:1I8D"
FT STRAND 179..184
FT /evidence="ECO:0007829|PDB:1I8D"
FT HELIX 186..204
FT /evidence="ECO:0007829|PDB:1I8D"
SQ SEQUENCE 213 AA; 23445 MW; CD1C7E40E4AC88B6 CRC64;
MFTGIVQGTA KLVSIDEKPN FRTHVVELPD HMLDGLETGA SVAHNGCCLT VTEINGNHVS
FDLMKETLRI TNLGDLKVGD WVNVERAAKF SDEIGGHLMS GHIMTTAEVA KILTSENNRQ
IWFKVQDSQL MKYILYKGFI GIDGISLTVG EVTPTRFCVH LIPETLERTT LGKKKLGARV
NIEIDPQTQA VVDTVERVLA ARENAMNQPG TEA
