RISB1_BRUA2
ID RISB1_BRUA2 Reviewed; 157 AA.
AC Q2YNC6;
DT 19-MAR-2014, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 1.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=6,7-dimethyl-8-ribityllumazine synthase 1 {ECO:0000255|HAMAP-Rule:MF_00178};
DE Short=DMRL synthase 1 {ECO:0000255|HAMAP-Rule:MF_00178};
DE Short=LS 1 {ECO:0000255|HAMAP-Rule:MF_00178};
DE Short=Lumazine synthase 1 {ECO:0000255|HAMAP-Rule:MF_00178};
DE EC=2.5.1.78 {ECO:0000255|HAMAP-Rule:MF_00178, ECO:0000269|PubMed:16923880, ECO:0000269|PubMed:20195542};
DE AltName: Full=Type I lumazine synthase {ECO:0000303|PubMed:16923880};
GN Name=ribH1; OrderedLocusNames=BAB1_0791;
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 PROTEIN SEQUENCE OF 1-12, FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS,
RP GENE NAME, SUBUNIT, AND PATHWAY.
RX PubMed=16923880; DOI=10.1128/jb.00207-06;
RA Zylberman V., Klinke S., Haase I., Bacher A., Fischer M., Goldbaum F.A.;
RT "Evolution of vitamin B2 biosynthesis: 6,7-dimethyl-8-ribityllumazine
RT synthases of Brucella.";
RL J. Bacteriol. 188:6135-6142(2006).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, GENE NAME, DISRUPTION PHENOTYPE, INDUCTION,
RP AND PATHWAY.
RC STRAIN=2308;
RX PubMed=20195542; DOI=10.1371/journal.pone.0009435;
RA Bonomi H.R., Marchesini M.I., Klinke S., Ugalde J.E., Zylberman V.,
RA Ugalde R.A., Comerci D.J., Goldbaum F.A.;
RT "An atypical riboflavin pathway is essential for Brucella abortus
RT virulence.";
RL PLoS ONE 5:E9435-E9435(2010).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.22 ANGSTROMS) OF APOENZYME AND IN COMPLEX WITH
RP SUBSTRATE ANALOG INHIBITOR, AND SUBUNIT.
RX PubMed=17854827; DOI=10.1016/j.jmb.2007.08.021;
RA Klinke S., Zylberman V., Bonomi H.R., Haase I., Guimaraes B.G.,
RA Braden B.C., Bacher A., Fischer M., Goldbaum F.A.;
RT "Structural and kinetic properties of lumazine synthase isoenzymes in the
RT order Rhizobiales.";
RL J. Mol. Biol. 373:664-680(2007).
CC -!- FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-ribityllumazine by
CC condensation of 5-amino-6-(D-ribitylamino)uracil with 3,4-dihydroxy-2-
CC butanone 4-phosphate. This is the penultimate step in the biosynthesis
CC of riboflavin. {ECO:0000255|HAMAP-Rule:MF_00178,
CC ECO:0000269|PubMed:16923880, ECO:0000269|PubMed:20195542}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=(2S)-2-hydroxy-3-oxobutyl phosphate + 5-amino-6-(D-
CC ribitylamino)uracil = 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) + 2
CC H2O + phosphate; Xref=Rhea:RHEA:26152, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:58201, ChEBI:CHEBI:58830; EC=2.5.1.78;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_00178,
CC ECO:0000269|PubMed:16923880, ECO:0000269|PubMed:20195542};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=90 uM for 5-amino-6-(D-ribitylamino)uracil (at 37 degrees Celsius
CC and pH 7.0) {ECO:0000269|PubMed:16923880};
CC KM=125 uM for 3,4-dihydroxy-2-butanone 4-phosphate (at 37 degrees
CC Celsius and pH 7.0) {ECO:0000269|PubMed:16923880};
CC Vmax=18 nmol/min/mg enzyme (at 37 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:16923880};
CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin
CC from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-
CC ribitylamino)uracil: step 1/2. {ECO:0000255|HAMAP-Rule:MF_00178,
CC ECO:0000305|PubMed:16923880, ECO:0000305|PubMed:20195542}.
CC -!- SUBUNIT: Homopentamer. {ECO:0000269|PubMed:16923880,
CC ECO:0000269|PubMed:17854827}.
CC -!- INDUCTION: The two ribH genes may be differentially expressed during
CC the Brucella infection cycle. Brucella would use RibH1 for flavin
CC biosynthesis during the extracellular phase and RibH2 during
CC intracellular growth. {ECO:0000305|PubMed:20195542}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are not auxotrophic for
CC riboflavin and grow at wild-type rates in both rich and minimal media.
CC But simultaneous disruption of ribH1 and ribH2 is lethal.
CC {ECO:0000269|PubMed:20195542}.
CC -!- SIMILARITY: Belongs to the DMRL synthase family. {ECO:0000255|HAMAP-
CC Rule:MF_00178}.
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DR EMBL; AM040264; CAJ10747.1; -; Genomic_DNA.
DR PDB; 2F59; X-ray; 2.30 A; A/B/C/D/E=1-157.
DR PDB; 2I0F; X-ray; 2.22 A; A/B/C/D/E=1-157.
DR PDBsum; 2F59; -.
DR PDBsum; 2I0F; -.
DR AlphaFoldDB; Q2YNC6; -.
DR SMR; Q2YNC6; -.
DR STRING; 359391.BAB1_0791; -.
DR EnsemblBacteria; CAJ10747; CAJ10747; BAB1_0791.
DR KEGG; bmf:BAB1_0791; -.
DR HOGENOM; CLU_089358_1_2_5; -.
DR OMA; CQGVTQG; -.
DR BRENDA; 2.5.1.78; 994.
DR UniPathway; UPA00275; UER00404.
DR Proteomes; UP000002719; Chromosome I.
DR GO; GO:0009349; C:riboflavin synthase complex; IEA:InterPro.
DR GO; GO:0000906; F:6,7-dimethyl-8-ribityllumazine synthase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniRule.
DR CDD; cd09209; Lumazine_synthase-I; 1.
DR Gene3D; 3.40.50.960; -; 1.
DR HAMAP; MF_00178; Lumazine_synth; 1.
DR InterPro; IPR034964; LS.
DR InterPro; IPR002180; LS/RS.
DR InterPro; IPR036467; LS/RS_sf.
DR PANTHER; PTHR21058; PTHR21058; 1.
DR Pfam; PF00885; DMRL_synthase; 1.
DR SUPFAM; SSF52121; SSF52121; 1.
DR TIGRFAMs; TIGR00114; lumazine-synth; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Direct protein sequencing; Reference proteome;
KW Riboflavin biosynthesis; Transferase.
FT CHAIN 1..157
FT /note="6,7-dimethyl-8-ribityllumazine synthase 1"
FT /id="PRO_0000425959"
FT ACT_SITE 90
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT BINDING 22
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000305|PubMed:17854827"
FT BINDING 53..55
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000305|PubMed:17854827"
FT BINDING 82..84
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00178,
FT ECO:0000305|PubMed:17854827"
FT BINDING 87..88
FT /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58830"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT BINDING 115
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000305|PubMed:17854827"
FT BINDING 129
FT /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58830"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT STRAND 14..20
FT /evidence="ECO:0007829|PDB:2I0F"
FT HELIX 24..40
FT /evidence="ECO:0007829|PDB:2I0F"
FT STRAND 44..52
FT /evidence="ECO:0007829|PDB:2I0F"
FT HELIX 53..55
FT /evidence="ECO:0007829|PDB:2I0F"
FT HELIX 56..68
FT /evidence="ECO:0007829|PDB:2I0F"
FT STRAND 75..84
FT /evidence="ECO:0007829|PDB:2I0F"
FT STRAND 87..89
FT /evidence="ECO:0007829|PDB:2I0F"
FT HELIX 92..108
FT /evidence="ECO:0007829|PDB:2I0F"
FT STRAND 113..122
FT /evidence="ECO:0007829|PDB:2I0F"
FT HELIX 123..130
FT /evidence="ECO:0007829|PDB:2I0F"
FT TURN 132..135
FT /evidence="ECO:0007829|PDB:2I0F"
FT HELIX 137..154
FT /evidence="ECO:0007829|PDB:2I0F"
SQ SEQUENCE 157 AA; 16791 MW; 657DE105F885A875 CRC64;
MEFLMSKHEA DAPHLLIVEA RFYDDLADAL LDGAKAALDE AGATYDVVTV PGALEIPATI
SFALDGADNG GTEYDGFVAL GTVIRGETYH FDIVSNESCR ALTDLSVEES IAIGNGILTV
ENEEQAWVHA RREDKDKGGF AARAALTMIG LRKKFGA
