ID A0A3D8IY05_9HELI Unreviewed; 156 AA.
AC A0A3D8IY05;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 19.
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:VEJ24661.1};
GN ORFNames=CQA62_01750 {ECO:0000313|EMBL:RDU70159.1}, NCTC13205_00814
GN {ECO:0000313|EMBL:VEJ24661.1};
OS Helicobacter cholecystus.
OC Bacteria; Campylobacterota; Epsilonproteobacteria; Campylobacterales;
OC Helicobacteraceae; Helicobacter.
OX NCBI_TaxID=45498 {ECO:0000313|EMBL:RDU70159.1, ECO:0000313|Proteomes:UP000257067};
RN [1] {ECO:0000313|EMBL:RDU70159.1, ECO:0000313|Proteomes:UP000257067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700242 {ECO:0000313|EMBL:RDU70159.1,
RC ECO:0000313|Proteomes:UP000257067};
RA Mannion A.J., Shen Z., Fox J.G.;
RT "Novel Campyloabacter and Helicobacter Species and Strains.";
RL Submitted (APR-2018) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:VEJ24661.1, ECO:0000313|Proteomes:UP000272814}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NCTC13205 {ECO:0000313|EMBL:VEJ24661.1,
RC ECO:0000313|Proteomes:UP000272814};
RG Pathogen Informatics;
RL Submitted (DEC-2018) 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 -!- SIMILARITY: Belongs to the DMRL synthase family.
CC {ECO:0000256|ARBA:ARBA00007424, ECO:0000256|HAMAP-Rule:MF_00178}.
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DR EMBL; NXLU01000001; RDU70159.1; -; Genomic_DNA.
DR EMBL; LR134518; VEJ24661.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D8IY05; -.
DR KEGG; hcl:NCTC13205_00814; -.
DR OrthoDB; 9809709at2; -.
DR UniPathway; UPA00275; UER00404.
DR Proteomes; UP000257067; Unassembled WGS sequence.
DR Proteomes; UP000272814; Chromosome 1.
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 Reference proteome {ECO:0000313|Proteomes:UP000257067};
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 89
FT /note="Proton donor"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
FT BINDING 23
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
FT BINDING 57..59
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
FT BINDING 81..83
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
FT BINDING 86..87
FT /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58830"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
FT BINDING 114
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
FT BINDING 128
FT /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58830"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00178"
SQ SEQUENCE 156 AA; 16961 MW; 93E2634C5B960444 CRC64;
MQVIEGKLKL EGNEKIAILS SRFNHIITDR LIEGAKDCFL RHGGEEDKLS LILAPGAYEI
PFVLQRLLAS KVYDGVCCVG AIIRGGTPHF DYVSAEATKG IANMALQYNQ AVSFGVLTTD
NIEQAIERAG SKAGNKGFEA MSSVIELINL YKTLKV
//
