ID   B4RLW2_NEIG2            Unreviewed;       259 AA.
AC   B4RLW2;
DT   23-SEP-2008, integrated into UniProtKB/TrEMBL.
DT   23-SEP-2008, sequence version 1.
DT   02-SEP-2026, entry version 82.
DE   RecName: Full=Riboflavin synthase {ECO:0000256|ARBA:ARBA00013950, ECO:0000256|NCBIfam:TIGR00187};
DE            EC=2.5.1.9 {ECO:0000256|ARBA:ARBA00012827, ECO:0000256|NCBIfam:TIGR00187};
GN   OrderedLocusNames=NGK_1122 {ECO:0000313|EMBL:ACF29799.1};
OS   Neisseria gonorrhoeae (strain NCCP11945).
OC   Bacteria; Pseudomonadati; Pseudomonadota; Betaproteobacteria; Neisseriales;
OC   Neisseriaceae; Neisseria.
OX   NCBI_TaxID=521006 {ECO:0000313|EMBL:ACF29799.1, ECO:0000313|Proteomes:UP000002564};
RN   [1] {ECO:0000313|EMBL:ACF29799.1, ECO:0000313|Proteomes:UP000002564}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCCP11945 {ECO:0000313|EMBL:ACF29799.1,
RC   ECO:0000313|Proteomes:UP000002564};
RX   PubMed=18586945; DOI=10.1128/JB.00566-08;
RA   Chung G.T., Yoo J.S., Oh H.B., Lee Y.S., Cha S.H., Kim S.J., Yoo C.K.;
RT   "Complete genome sequence of Neisseria gonorrhoeae NCCP11945.";
RL   J. Bacteriol. 190:6035-6036(2008).
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:0000256|ARBA:ARBA00002803}.
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         Evidence={ECO:0000256|ARBA:ARBA00000968};
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. {ECO:0000256|ARBA:ARBA00004887}.
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DR   EMBL; CP001050; ACF29799.1; -; Genomic_DNA.
DR   AlphaFoldDB; B4RLW2; -.
DR   KEGG; ngk:NGK_1122; -.
DR   HOGENOM; CLU_034388_0_1_4; -.
DR   Proteomes; UP000002564; Chromosome.
DR   GO; GO:0005829; C:cytosol; IEA:TreeGrafter.
DR   GO; GO:0004746; F:riboflavin synthase activity; IEA:UniProtKB-UniRule.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IEA:TreeGrafter.
DR   CDD; cd00402; Riboflavin_synthase_like; 1.
DR   FunFam; 2.40.30.20:FF:000003; Riboflavin synthase, alpha subunit; 1.
DR   FunFam; 2.40.30.20:FF:000005; Riboflavin synthase, alpha subunit; 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   NCBIfam; NF006767; PRK09289.1; 1.
DR   NCBIfam; NF009566; PRK13020.1; 1.
DR   NCBIfam; TIGR00187; ribE; 1.
DR   PANTHER; PTHR21098:SF0; RIBOFLAVIN SYNTHASE; 1.
DR   PANTHER; PTHR21098; RIBOFLAVIN SYNTHASE ALPHA CHAIN; 1.
DR   Pfam; PF00677; Lum_binding; 2.
DR   SUPFAM; SSF63380; Riboflavin synthase domain-like; 2.
DR   PROSITE; PS51177; LUMAZINE_BIND; 2.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000002564};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT   DOMAIN          55..152
FT                   /note="Lumazine-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51177"
FT   REPEAT          55..152
FT                   /note="Lumazine-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00524"
FT   DOMAIN          153..249
FT                   /note="Lumazine-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS51177"
FT   REPEAT          153..249
FT                   /note="Lumazine-binding"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00524"
SQ   SEQUENCE   259 AA;  28535 MW;  10F53619B5025BFE CRC64;
     MQDRRPARKG KVKAYRAVFA RTGGTMPSEG VSDGIFRGEM LQFAPFLPTQ GNRIMFTGIV
     QGLGKLTAIH RPSEAFQTYV VELPQEAAEN LQHGASVANN GCCLTITEIE GNRVSFDLMA
     ETLAKTNLGL LKEGDCVNIE RAARFGDEIG GHVMSGHIMA TVPIVEIERD GFNRTVWFAL
     PHELKPYILT KGFVGLDGCS LTIGKVEDSR FNVHLIPETL ERTLFGSRKA GDRINIEIDP
     NTQAIVDTVE RLMAQRYAK
//