ID W8PYE4_9PSED Unreviewed; 158 AA.
AC W8PYE4;
DT 14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT 14-MAY-2014, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=6,7-dimethyl-8-ribityllumazine synthase {ECO:0000256|ARBA:ARBA00012664, ECO:0000256|HAMAP-Rule:MF_00178};
DE Short=DMRL synthase {ECO:0000256|HAMAP-Rule:MF_00178};
DE Short=LS {ECO:0000256|HAMAP-Rule:MF_00178};
DE Short=Lumazine synthase {ECO:0000256|HAMAP-Rule:MF_00178};
DE EC=2.5.1.78 {ECO:0000256|ARBA:ARBA00012664, ECO:0000256|HAMAP-Rule:MF_00178};
GN Name=ribH {ECO:0000256|HAMAP-Rule:MF_00178,
GN ECO:0000313|EMBL:AHL36177.1};
GN Synonyms=ribE {ECO:0000313|EMBL:NUT83288.1};
GN ORFNames=BK652_22005 {ECO:0000313|EMBL:ROM78618.1}, BK654_13970
GN {ECO:0000313|EMBL:ROM76625.1}, CD58_26385
GN {ECO:0000313|EMBL:AHL36177.1}, GFU70_25435
GN {ECO:0000313|EMBL:QGA52324.1}, HNO85_20285
GN {ECO:0000313|EMBL:NUT83288.1};
OS Pseudomonas brassicacearum.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=930166 {ECO:0000313|EMBL:AHL36177.1, ECO:0000313|Proteomes:UP000019521};
RN [1] {ECO:0000313|EMBL:AHL36177.1, ECO:0000313|Proteomes:UP000019521}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DF41 {ECO:0000313|EMBL:AHL36177.1,
RC ECO:0000313|Proteomes:UP000019521};
RX PubMed=24812222;
RA Loewen P.C., Switala J., Fernando W.G., de Kievit T.;
RT "Genome Sequence of Pseudomonas brassicacearum DF41.";
RL Genome Announc. 2:e00390-14(2014).
RN [2] {ECO:0000313|Proteomes:UP000284049, ECO:0000313|Proteomes:UP000285519}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=36D4 {ECO:0000313|EMBL:ROM76625.1,
RC ECO:0000313|Proteomes:UP000285519}, and Wood3
RC {ECO:0000313|EMBL:ROM78618.1, ECO:0000313|Proteomes:UP000284049};
RA Tao X.-Y., Taylor C.G.;
RT "Comparative genome analysis of multiple Pseudomonas spp. focuses on
RT biocontrol and plant growth promoting traits.";
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:QGA52324.1, ECO:0000313|Proteomes:UP000329489}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S-1 {ECO:0000313|EMBL:QGA52324.1,
RC ECO:0000313|Proteomes:UP000329489};
RA Mandryk-Litvinkovich M.N., Muratova A., Nosonova T.L., Evdokimova O.V.,
RA Valentovich L.N., Titok M.A., Kolomiets E.I.;
RT "Molecular genetic analysis of determinants defining synthesis of 2,4-
RT diacetylphloroglucinol by Pseudomonas brassicacearum BIM B-446 bacteria.";
RL Prikl. Biokhim. Mikrobiol. 53:31-39(2017).
RN [4] {ECO:0000313|EMBL:NUT83288.1, ECO:0000313|Proteomes:UP000562723}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C2F7 {ECO:0000313|EMBL:NUT83288.1,
RC ECO:0000313|Proteomes:UP000562723};
RA Nordstedt N.P., Jones M.L.;
RT "Isolation of Rhizosphere Bacteria That Improve Quality and Water Stress
RT Tolerance in Greenhouse Ornamentals.";
RL Front. Plant Sci. 11:0-0(2020).
RN [5] {ECO:0000313|EMBL:QGA52324.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=S-1 {ECO:0000313|EMBL:QGA52324.1};
RA Muratova A.A., Valentovich L.N., Titok M.A., Kolomiets E.I.;
RL Submitted (SEP-2020) to the EMBL/GenBank/DDBJ databases.
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:0000256|HAMAP-Rule:MF_00178}.
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:0000256|ARBA:ARBA00001697, ECO:0000256|HAMAP-
CC Rule:MF_00178};
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:0000256|ARBA:ARBA00004917,
CC ECO:0000256|HAMAP-Rule:MF_00178}.
CC -!- SUBUNIT: Forms an icosahedral capsid composed of 60 subunits, arranged
CC as a dodecamer of pentamers. {ECO:0000256|HAMAP-Rule:MF_00178}.
CC -!- SIMILARITY: Belongs to the DMRL synthase family.
CC {ECO:0000256|ARBA:ARBA00007424, ECO:0000256|HAMAP-Rule:MF_00178}.
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DR EMBL; CP007410; AHL36177.1; -; Genomic_DNA.
DR EMBL; JABFMS010000045; NUT83288.1; -; Genomic_DNA.
DR EMBL; CP045701; QGA52324.1; -; Genomic_DNA.
DR EMBL; MOBE01000008; ROM76625.1; -; Genomic_DNA.
DR EMBL; MOBC01000012; ROM78618.1; -; Genomic_DNA.
DR RefSeq; WP_003206025.1; NZ_MOBH01000023.1.
DR GeneID; 76211554; -.
DR KEGG; pbc:CD58_26385; -.
DR PATRIC; fig|930166.13.peg.5821; -.
DR eggNOG; COG0054; Bacteria.
DR OMA; CQGVTQG; -.
DR OrthoDB; 9809709at2; -.
DR UniPathway; UPA00275; UER00404.
DR Proteomes; UP000019521; Chromosome.
DR Proteomes; UP000284049; Unassembled WGS sequence.
DR Proteomes; UP000285519; Unassembled WGS sequence.
DR Proteomes; UP000329489; Chromosome.
DR Proteomes; UP000562723; Unassembled WGS sequence.
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; Lumazine/riboflavin synthase; 1.
DR HAMAP; MF_00178; Lumazine_synth; 1.
DR InterPro; IPR034964; LS.
DR InterPro; IPR002180; LS/RS.
DR InterPro; IPR036467; LS/RS_sf.
DR NCBIfam; TIGR00114; lumazine-synth; 1.
DR PANTHER; PTHR21058:SF0; 6,7-DIMETHYL-8-RIBITYLLUMAZINE SYNTHASE; 1.
DR PANTHER; PTHR21058; 6,7-DIMETHYL-8-RIBITYLLUMAZINE SYNTHASE DMRL SYNTHASE LUMAZINE SYNTHASE; 1.
DR Pfam; PF00885; DMRL_synthase; 1.
DR SUPFAM; SSF52121; Lumazine synthase; 1.
PE 3: Inferred from homology;
KW Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619, ECO:0000256|HAMAP-
KW Rule:MF_00178};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|HAMAP-
KW Rule:MF_00178}.
FT ACT_SITE 90
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
FT BINDING 24
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
FT BINDING 58..60
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
FT BINDING 82..84
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
FT BINDING 87..88
FT /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58830"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
FT BINDING 115
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
FT BINDING 129
FT /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58830"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
SQ SEQUENCE 158 AA; 16404 MW; A0FA5CBAFDEAB476 CRC64;
MTLKTIEGTF IAPKGRYALV VGRFNSFVVE SLVGGAVDAL VRHGVSESDI TIIRAPGAFE
IPLVAQKVAQ KGEYAAIIAL GAVIRGGTPH FEYVAGECTK GLAQVSMEFG VPVAFGVLTV
DSIEQAIERS GTKAGNKGAE AALSALEMVS LLAQLEAK
//
