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Database: UniProt
Entry: I1XHF0_METNJ
LinkDB: I1XHF0_METNJ
Original site: I1XHF0_METNJ 
ID   I1XHF0_METNJ            Unreviewed;       160 AA.
AC   I1XHF0;
DT   11-JUL-2012, integrated into UniProtKB/TrEMBL.
DT   11-JUL-2012, sequence version 1.
DT   24-JAN-2024, entry version 66.
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   OrderedLocusNames=Q7A_977 {ECO:0000313|EMBL:AFI83819.1};
GN   ORFNames=CDW43_04845 {ECO:0000313|EMBL:AUZ83938.1};
OS   Methylophaga nitratireducenticrescens.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC   Piscirickettsiaceae; Methylophaga.
OX   NCBI_TaxID=754476 {ECO:0000313|EMBL:AFI83819.1, ECO:0000313|Proteomes:UP000009144};
RN   [1] {ECO:0000313|EMBL:AFI83819.1, ECO:0000313|Proteomes:UP000009144}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JAM1 {ECO:0000313|EMBL:AFI83819.1,
RC   ECO:0000313|Proteomes:UP000009144};
RX   PubMed=22815445; DOI=10.1128/JB.00726-12;
RA   Villeneuve C., Martineau C., Mauffrey F., Villemur R.;
RT   "Complete genome sequences of Methylophaga sp. strain JAM1 and Methylophaga
RT   sp. strain JAM7.";
RL   J. Bacteriol. 194:4126-4127(2012).
RN   [2] {ECO:0000313|EMBL:AFI83819.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JAM1 {ECO:0000313|EMBL:AFI83819.1};
RX   PubMed=23148104; DOI=10.1099/ijs.0.044545-0;
RA   Villeneuve C., Martineau C., Mauffrey F., Villemur R.;
RT   "Methylophaga nitratireducenticrescens sp. nov. and Methylophaga frappieri
RT   sp. nov., isolated from the biofilm of the methanol-fed denitrification
RT   system treating the seawater at the Montreal Biodome.";
RL   Int. J. Syst. Evol. Microbiol. 63:2216-2222(2013).
RN   [3] {ECO:0000313|EMBL:AFI83819.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JAM1 {ECO:0000313|EMBL:AFI83819.1};
RA   Villeneuve C., Villemur R.;
RL   Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:AUZ83938.1, ECO:0000313|Proteomes:UP000238402}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=GP59 {ECO:0000313|EMBL:AUZ83938.1,
RC   ECO:0000313|Proteomes:UP000238402};
RA   Villemur R.;
RT   "The sequence of the genome of Methylophaga nitratireducenticrescens GP59
RT   and its two plasmids.";
RL   Submitted (JUN-2017) 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; CP003390; AFI83819.1; -; Genomic_DNA.
DR   EMBL; CP021973; AUZ83938.1; -; Genomic_DNA.
DR   RefSeq; WP_014706194.1; NZ_CP021973.1.
DR   AlphaFoldDB; I1XHF0; -.
DR   STRING; 754476.Q7A_977; -.
DR   KEGG; mej:Q7A_977; -.
DR   PATRIC; fig|754476.3.peg.963; -.
DR   eggNOG; COG0054; Bacteria.
DR   HOGENOM; CLU_089358_1_1_6; -.
DR   OMA; CQGVTQG; -.
DR   OrthoDB; 9809709at2; -.
DR   UniPathway; UPA00275; UER00404.
DR   Proteomes; UP000009144; Chromosome.
DR   Proteomes; UP000238402; 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; 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        91
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
FT   BINDING         25
FT                   /ligand="5-amino-6-(D-ribitylamino)uracil"
FT                   /ligand_id="ChEBI:CHEBI:15934"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
FT   BINDING         59..61
FT                   /ligand="5-amino-6-(D-ribitylamino)uracil"
FT                   /ligand_id="ChEBI:CHEBI:15934"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
FT   BINDING         83..85
FT                   /ligand="5-amino-6-(D-ribitylamino)uracil"
FT                   /ligand_id="ChEBI:CHEBI:15934"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
FT   BINDING         88..89
FT                   /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58830"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
FT   BINDING         116
FT                   /ligand="5-amino-6-(D-ribitylamino)uracil"
FT                   /ligand_id="ChEBI:CHEBI:15934"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
FT   BINDING         130
FT                   /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT                   /ligand_id="ChEBI:CHEBI:58830"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
SQ   SEQUENCE   160 AA;  16722 MW;  E102F5CD3F9306C4 CRC64;
     MSNIKTFSGD FSAKGIRVGI VAGRFNDFIV DNLIAGAVDT LLRHGAAEKD IEIARVPGAV
     EIPLAVQRMG KTGKYDAIIA LGAVIRGGTP HFEYVAGECS KGLGQLTLQL DLPIAFGVLT
     VDTIEQAIER AGTKAGNKGA EAAMGMIEMV NVLRQIGAAK
//
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