RISB_BACAN
ID RISB_BACAN Reviewed; 153 AA.
AC Q81MB5; Q6HTR7; Q6KN05;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 128.
DE RecName: Full=6,7-dimethyl-8-ribityllumazine synthase {ECO:0000255|HAMAP-Rule:MF_00178};
DE Short=DMRL synthase {ECO:0000255|HAMAP-Rule:MF_00178};
DE Short=LS {ECO:0000255|HAMAP-Rule:MF_00178};
DE Short=Lumazine synthase {ECO:0000255|HAMAP-Rule:MF_00178};
DE EC=2.5.1.78 {ECO:0000255|HAMAP-Rule:MF_00178};
GN Name=ribH {ECO:0000255|HAMAP-Rule:MF_00178};
GN OrderedLocusNames=BA_4334, GBAA_4334, BAS4021;
OS Bacillus anthracis.
OC Bacteria; Firmicutes; Bacilli; Bacillales; Bacillaceae; Bacillus;
OC Bacillus cereus group.
OX NCBI_TaxID=1392;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames / isolate Porton;
RX PubMed=12721629; DOI=10.1038/nature01586;
RA Read T.D., Peterson S.N., Tourasse N.J., Baillie L.W., Paulsen I.T.,
RA Nelson K.E., Tettelin H., Fouts D.E., Eisen J.A., Gill S.R.,
RA Holtzapple E.K., Okstad O.A., Helgason E., Rilstone J., Wu M.,
RA Kolonay J.F., Beanan M.J., Dodson R.J., Brinkac L.M., Gwinn M.L.,
RA DeBoy R.T., Madpu R., Daugherty S.C., Durkin A.S., Haft D.H., Nelson W.C.,
RA Peterson J.D., Pop M., Khouri H.M., Radune D., Benton J.L., Mahamoud Y.,
RA Jiang L., Hance I.R., Weidman J.F., Berry K.J., Plaut R.D., Wolf A.M.,
RA Watkins K.L., Nierman W.C., Hazen A., Cline R.T., Redmond C., Thwaite J.E.,
RA White O., Salzberg S.L., Thomason B., Friedlander A.M., Koehler T.M.,
RA Hanna P.C., Kolstoe A.-B., Fraser C.M.;
RT "The genome sequence of Bacillus anthracis Ames and comparison to closely
RT related bacteria.";
RL Nature 423:81-86(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ames ancestor;
RX PubMed=18952800; DOI=10.1128/jb.01347-08;
RA Ravel J., Jiang L., Stanley S.T., Wilson M.R., Decker R.S., Read T.D.,
RA Worsham P., Keim P.S., Salzberg S.L., Fraser-Liggett C.M., Rasko D.A.;
RT "The complete genome sequence of Bacillus anthracis Ames 'Ancestor'.";
RL J. Bacteriol. 191:445-446(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Sterne;
RA Brettin T.S., Bruce D., Challacombe J.F., Gilna P., Han C., Hill K.,
RA Hitchcock P., Jackson P., Keim P., Longmire J., Lucas S., Okinaka R.,
RA Richardson P., Rubin E., Tice H.;
RT "Complete genome sequence of Bacillus anthracis Sterne.";
RL Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP PROTEIN SEQUENCE OF 1-10, X-RAY CRYSTALLOGRAPHY (3.50 ANGSTROMS) IN
RP COMPLEXES WITH PHOSPHATE, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT, AND
RP ACTIVITY REGULATION.
RX PubMed=20823551; DOI=10.1107/s0907444910029690;
RA Morgunova E., Illarionov B., Saller S., Popov A., Sambaiah T., Bacher A.,
RA Cushman M., Fischer M., Ladenstein R.;
RT "Structural study and thermodynamic characterization of inhibitor binding
RT to lumazine synthase from Bacillus anthracis.";
RL Acta Crystallogr. D 66:1001-1011(2010).
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:20823551}.
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:20823551};
CC -!- ACTIVITY REGULATION: Activity is competitively inhibited by the
CC bisubstrate-type compounds TS23, JC33 and JC72, with Ki values in the
CC low nanomolar range. {ECO:0000269|PubMed:20823551}.
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 -!- SUBUNIT: Forms an icosahedral capsid composed of 60 subunits, arranged
CC as a dodecamer of pentamers. {ECO:0000255|HAMAP-Rule:MF_00178,
CC ECO:0000269|PubMed:20823551}.
CC -!- SIMILARITY: Belongs to the DMRL synthase family. {ECO:0000255|HAMAP-
CC Rule:MF_00178}.
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DR EMBL; AE016879; AAP28053.1; -; Genomic_DNA.
DR EMBL; AE017334; AAT33455.1; -; Genomic_DNA.
DR EMBL; AE017225; AAT56322.1; -; Genomic_DNA.
DR RefSeq; NP_846567.1; NC_003997.3.
DR RefSeq; WP_000230891.1; NZ_WXXJ01000027.1.
DR RefSeq; YP_030271.1; NC_005945.1.
DR PDB; 4V7G; X-ray; 3.50 A; A1/A2/A3/A4/AA/AB/AC/AD/AE/AF/AG/AH/AI/AJ/AK/AL/AM/AN/AO/AP/AQ/AR/AS/AT/AU/AV/AW/AX/AY/AZ/B1/B2/B3/B4/BA/BB/BC/BD/BE/BF/BG/BH/BI/BJ/BK/BL/BM/BN/BO/BP/BQ/BR/BS/BT/BU/BV/BW/BX/BY/BZ/C1/C2/C3/C4/CA/CB/CC/CD/CE/CF/CG=1-153.
DR PDBsum; 4V7G; -.
DR AlphaFoldDB; Q81MB5; -.
DR SMR; Q81MB5; -.
DR STRING; 260799.BAS4021; -.
DR DNASU; 1087551; -.
DR EnsemblBacteria; AAP28053; AAP28053; BA_4334.
DR EnsemblBacteria; AAT33455; AAT33455; GBAA_4334.
DR GeneID; 45024001; -.
DR KEGG; ban:BA_4334; -.
DR KEGG; bar:GBAA_4334; -.
DR KEGG; bat:BAS4021; -.
DR PATRIC; fig|198094.11.peg.4303; -.
DR eggNOG; COG0054; Bacteria.
DR HOGENOM; CLU_089358_1_1_9; -.
DR OMA; CQGVTQG; -.
DR UniPathway; UPA00275; UER00404.
DR Proteomes; UP000000427; Chromosome.
DR Proteomes; UP000000594; Chromosome.
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..153
FT /note="6,7-dimethyl-8-ribityllumazine synthase"
FT /id="PRO_0000134710"
FT ACT_SITE 87
FT /note="Proton donor"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT BINDING 21
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT BINDING 55..57
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT BINDING 79..81
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT BINDING 84..85
FT /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58830"
FT /evidence="ECO:0000305"
FT BINDING 112
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00178"
FT BINDING 126
FT /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58830"
FT /evidence="ECO:0000305"
FT STRAND 14..20
FT /evidence="ECO:0007829|PDB:4V7G"
FT HELIX 23..29
FT /evidence="ECO:0007829|PDB:4V7G"
FT HELIX 30..32
FT /evidence="ECO:0007829|PDB:4V7G"
FT HELIX 33..37
FT /evidence="ECO:0007829|PDB:4V7G"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:4V7G"
FT HELIX 44..46
FT /evidence="ECO:0007829|PDB:4V7G"
FT STRAND 47..54
FT /evidence="ECO:0007829|PDB:4V7G"
FT HELIX 55..57
FT /evidence="ECO:0007829|PDB:4V7G"
FT HELIX 58..66
FT /evidence="ECO:0007829|PDB:4V7G"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:4V7G"
FT STRAND 72..81
FT /evidence="ECO:0007829|PDB:4V7G"
FT HELIX 87..101
FT /evidence="ECO:0007829|PDB:4V7G"
FT STRAND 103..106
FT /evidence="ECO:0007829|PDB:4V7G"
FT STRAND 110..118
FT /evidence="ECO:0007829|PDB:4V7G"
FT HELIX 120..125
FT /evidence="ECO:0007829|PDB:4V7G"
FT STRAND 127..129
FT /evidence="ECO:0007829|PDB:4V7G"
FT HELIX 134..146
FT /evidence="ECO:0007829|PDB:4V7G"
FT TURN 147..150
FT /evidence="ECO:0007829|PDB:4V7G"
SQ SEQUENCE 153 AA; 16255 MW; AA5391784EA66839 CRC64;
MVFEGHLVGT GLKVGVVVGR FNEFITSKLL GGALDGLKRH GVEENDIDVA WVPGAFEIPL
IAKKMANSGK YDAVITLGTV IRGATTHYDY VCNEVAKGVA SLSLQTDIPV IFGVLTTETI
EQAIERAGTK AGNKGYESAV AAIEMAHLSK HWA
