ID   RISA_MYCTO              Reviewed;         201 AA.
AC   P9WK34; L0T6K5; P65327; P71680;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 39.
DE   RecName: Full=Riboflavin synthase;
DE            Short=RS;
DE            EC=2.5.1.9;
GN   Name=ribE; Synonyms=ribC; OrderedLocusNames=MT1456;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
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:0000250}.
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;
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. {ECO:0000250}.
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DR   EMBL; AE000516; AAK45721.1; -; Genomic_DNA.
DR   PIR; A70902; A70902.
DR   RefSeq; WP_003407318.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WK34; -.
DR   SMR; P9WK34; -.
DR   EnsemblBacteria; AAK45721; AAK45721; MT1456.
DR   GeneID; 45425390; -.
DR   KEGG; mtc:MT1456; -.
DR   PATRIC; fig|83331.31.peg.1564; -.
DR   HOGENOM; CLU_034388_2_0_11; -.
DR   UniPathway; UPA00275; UER00405.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0004746; F:riboflavin synthase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway.
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   3: Inferred from homology;
KW   Repeat; Riboflavin biosynthesis; Transferase.
FT   CHAIN           1..201
FT                   /note="Riboflavin synthase"
FT                   /id="PRO_0000427723"
FT   REPEAT          1..97
FT                   /note="Lumazine-binding 1"
FT   REPEAT          98..197
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   BINDING         47..49
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         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:P0AFU8"
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         136
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         145..147
FT                   /ligand="2,4-dihydroxypteridine"
FT                   /ligand_id="ChEBI:CHEBI:16489"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q2YN92"
FT   BINDING         162..167
FT                   /ligand="2,4-dihydroxypteridine"
FT                   /ligand_id="ChEBI:CHEBI:16489"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q2YN92"
SQ   SEQUENCE   201 AA;  21320 MW;  1CE1C3A20A61D2FF CRC64;
     MFTGIVEERG EVTGREALVD AARLTIRGPM VTADAGHGDS IAVNGVCLTV VDVLPDGQFT
     ADVMAETLNR SNLGELRPGS RVNLERAAAL GSRLGGHIVQ GHVDATGEIV ARCPSEHWEV
     VRIEMPASVA RYVVEKGSIT VDGISLTVSG LGAEQRDWFE VSLIPTTREL TTLGSAAVGT
     RVNLEVDVVA KYVERLMRSA G