ID   RISA_CHLTR              Reviewed;         199 AA.
AC   O84410;
DT   01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1998, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Riboflavin synthase;
DE            Short=RS;
DE            EC=2.5.1.9;
GN   Name=ribE; Synonyms=ribC; OrderedLocusNames=CT_405;
OS   Chlamydia trachomatis (strain D/UW-3/Cx).
OC   Bacteria; Chlamydiae; Chlamydiales; Chlamydiaceae;
OC   Chlamydia/Chlamydophila group; Chlamydia.
OX   NCBI_TaxID=272561;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=D/UW-3/Cx;
RX   PubMed=9784136; DOI=10.1126/science.282.5389.754;
RA   Stephens R.S., Kalman S., Lammel C.J., Fan J., Marathe R., Aravind L.,
RA   Mitchell W.P., Olinger L., Tatusov R.L., Zhao Q., Koonin E.V., Davis R.W.;
RT   "Genome sequence of an obligate intracellular pathogen of humans: Chlamydia
RT   trachomatis.";
RL   Science 282:754-759(1998).
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; AE001273; AAC68002.1; -; Genomic_DNA.
DR   PIR; H71519; H71519.
DR   RefSeq; NP_219915.1; NC_000117.1.
DR   RefSeq; WP_010725187.1; NC_000117.1.
DR   AlphaFoldDB; O84410; -.
DR   SMR; O84410; -.
DR   STRING; 813.O172_02200; -.
DR   EnsemblBacteria; AAC68002; AAC68002; CT_405.
DR   GeneID; 884709; -.
DR   KEGG; ctr:CT_405; -.
DR   PATRIC; fig|272561.5.peg.436; -.
DR   HOGENOM; CLU_034388_0_1_0; -.
DR   InParanoid; O84410; -.
DR   OMA; HFVTGHV; -.
DR   UniPathway; UPA00275; UER00405.
DR   Proteomes; UP000000431; Chromosome.
DR   GO; GO:0004746; F:riboflavin synthase activity; IBA:GO_Central.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IBA:GO_Central.
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   Reference proteome; Repeat; Riboflavin biosynthesis; Transferase.
FT   CHAIN           1..199
FT                   /note="Riboflavin synthase"
FT                   /id="PRO_0000068165"
FT   REPEAT          1..95
FT                   /note="Lumazine-binding 1"
FT   REPEAT          96..188
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         46..48
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         60..65
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         99..101
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         130
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         139..141
FT                   /ligand="2,4-dihydroxypteridine"
FT                   /ligand_id="ChEBI:CHEBI:16489"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q2YN92"
FT   BINDING         153..158
FT                   /ligand="2,4-dihydroxypteridine"
FT                   /ligand_id="ChEBI:CHEBI:16489"
FT                   /ligand_label="1"
FT                   /evidence="ECO:0000250|UniProtKB:Q2YN92"
SQ   SEQUENCE   199 AA;  22222 MW;  C815DE0AC8534E16 CRC64;
     MFSGIIQEVA RVDLIHHLRD SMEIGVFARK LIDVVPGSSF SVDGICLTLV KRQYELLFFD
     VTEETMAWTT IKDYTVGTMV NLERSVRLGD EIGGHFVSGH VCGIGTIIAI EKSYMFFKAP
     ANLVPYILEK GFIAIDGISL TIARVKGDIF SVSLIPETRA RTSLGYKQVG AHVNMEPDMM
     TKMQVDTIMR FHAEKEISK