RISA_MYCBO
ID RISA_MYCBO Reviewed; 201 AA.
AC P65328; A0A1R3XYA8; P71680; X2BI92;
DT 11-OCT-2004, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2004, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=Riboflavin synthase;
DE Short=RS;
DE EC=2.5.1.9;
GN Name=ribE; Synonyms=ribC; OrderedLocusNames=BQ2027_MB1447;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
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; LT708304; SIU00050.1; -; Genomic_DNA.
DR RefSeq; NP_855099.1; NC_002945.3.
DR RefSeq; WP_003407318.1; NC_002945.4.
DR AlphaFoldDB; P65328; -.
DR SMR; P65328; -.
DR EnsemblBacteria; SIU00050; SIU00050; BQ2027_MB1447.
DR GeneID; 45425390; -.
DR PATRIC; fig|233413.5.peg.1582; -.
DR OMA; HFVTGHV; -.
DR UniPathway; UPA00275; UER00405.
DR Proteomes; UP000001419; 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_0000068169"
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
