RISA_BRUA2
ID RISA_BRUA2 Reviewed; 202 AA.
AC Q2YN92;
DT 17-FEB-2016, integrated into UniProtKB/Swiss-Prot.
DT 07-FEB-2006, sequence version 1.
DT 03-AUG-2022, entry version 85.
DE RecName: Full=Riboflavin synthase {ECO:0000303|PubMed:24816110};
DE Short=RS {ECO:0000303|PubMed:24816110};
DE EC=2.5.1.9 {ECO:0000269|PubMed:24816110};
GN Name=ribE {ECO:0000303|PubMed:24816110};
GN OrderedLocusNames=BAB1_0790 {ECO:0000312|EMBL:CAJ10746.1};
OS Brucella abortus (strain 2308).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Brucellaceae; Brucella/Ochrobactrum group; Brucella.
OX NCBI_TaxID=359391;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2308;
RX PubMed=16299333; DOI=10.1128/iai.73.12.8353-8361.2005;
RA Chain P.S., Comerci D.J., Tolmasky M.E., Larimer F.W., Malfatti S.A.,
RA Vergez L.M., Aguero F., Land M.L., Ugalde R.A., Garcia E.;
RT "Whole-genome analyses of speciation events in pathogenic Brucellae.";
RL Infect. Immun. 73:8353-8361(2005).
RN [2]
RP X-RAY CRYSTALLOGRAPHY (1.78 ANGSTROMS) OF APOENZYME AND IN COMPLEXES WITH
RP RIBOFLAVIN AND WITH TWO DIFFERENT PRODUCT ANALOGS, SUBUNIT, FUNCTION,
RP CATALYTIC ACTIVITY, ACTIVITY REGULATION, AND DOMAIN.
RC STRAIN=2308;
RX PubMed=24816110; DOI=10.1107/s1399004714005161;
RA Serer M.I., Bonomi H.R., Guimaraes B.G., Rossi R.C., Goldbaum F.A.,
RA Klinke S.;
RT "Crystallographic and kinetic study of riboflavin synthase from Brucella
RT abortus, a chemotherapeutic target with an enhanced intrinsic
RT flexibility.";
RL Acta Crystallogr. D 70:1419-1434(2014).
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:24816110}.
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:0000269|PubMed:24816110};
CC -!- ACTIVITY REGULATION: Is inhibited by riboflavin. Product inhibition may
CC be the major mechanism by which RS regulates its enzymatic activity in
CC vivo. {ECO:0000269|PubMed:24816110}.
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:0000305|PubMed:24816110}.
CC -!- SUBUNIT: Homotrimer. {ECO:0000269|PubMed:24816110}.
CC -!- DOMAIN: Each monomer can bind two substrate molecules, yet there is
CC only one active site for the whole trimeric enzyme, which is located at
CC the interface between two neighboring chains and formed by the N-
CC terminal barrel from chain A and the C-terminal barrel from chain B.
CC {ECO:0000269|PubMed:24816110}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AM040264; CAJ10746.1; -; Genomic_DNA.
DR RefSeq; WP_002969422.1; NZ_KN046823.1.
DR PDB; 4E0F; X-ray; 2.85 A; A/B/C=1-202.
DR PDB; 4FXU; X-ray; 1.90 A; A/B/C=1-202.
DR PDB; 4G6I; X-ray; 1.78 A; A/B/C=1-202.
DR PDB; 4GQN; X-ray; 1.85 A; A/B/C=1-202.
DR PDBsum; 4E0F; -.
DR PDBsum; 4FXU; -.
DR PDBsum; 4G6I; -.
DR PDBsum; 4GQN; -.
DR AlphaFoldDB; Q2YN92; -.
DR SMR; Q2YN92; -.
DR STRING; 359391.BAB1_0790; -.
DR EnsemblBacteria; CAJ10746; CAJ10746; BAB1_0790.
DR GeneID; 3787490; -.
DR KEGG; bmf:BAB1_0790; -.
DR PATRIC; fig|359391.11.peg.3101; -.
DR HOGENOM; CLU_034388_2_2_5; -.
DR OMA; HFVTGHV; -.
DR PhylomeDB; Q2YN92; -.
DR BRENDA; 2.5.1.9; 994.
DR UniPathway; UPA00275; UER00405.
DR Proteomes; UP000002719; Chromosome I.
DR GO; GO:1902444; F:riboflavin binding; IDA:UniProtKB.
DR GO; GO:0004746; F:riboflavin synthase activity; IDA:UniProtKB.
DR GO; GO:0070207; P:protein homotrimerization; IDA:UniProtKB.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IDA:UniProtKB.
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..202
FT /note="Riboflavin synthase"
FT /id="PRO_0000435442"
FT REPEAT 1..101
FT /note="Lumazine-binding 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00524"
FT REPEAT 102..198
FT /note="Lumazine-binding 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00524"
FT BINDING 4..6
FT /ligand="2,4-dihydroxypteridine"
FT /ligand_id="ChEBI:CHEBI:16489"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:24816110"
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:0000305|PubMed:24816110"
FT BINDING 66..68
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:0000305|PubMed:24816110"
FT BINDING 105..107
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:0000305|PubMed:24816110"
FT BINDING 140
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:0000305|PubMed:24816110"
FT BINDING 149..151
FT /ligand="2,4-dihydroxypteridine"
FT /ligand_id="ChEBI:CHEBI:16489"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:24816110"
FT BINDING 163..168
FT /ligand="2,4-dihydroxypteridine"
FT /ligand_id="ChEBI:CHEBI:16489"
FT /ligand_label="1"
FT /evidence="ECO:0000305|PubMed:24816110"
SQ SEQUENCE 202 AA; 22223 MW; 6265FA459B3C0195 CRC64;
MFTGIITDIG KVDRVKPLNE GVLLRIETAY DPETIELGAS IACSGVCLTV VALPEKGSNA
RWFEVEAWEE ALRLTTISSW QSGRKINLER SLKLGDEMGG HLVFGHVDGQ AEIVERKDEG
DAVRFTLRAP EELAPFIAQK GSVALDGTSL TVNGVNANEF DVLLIRHSLE VTTWGERKAG
DKVNIEIDQL ARYAARLAQY QK
