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Entry: A0A317FBX1_9PROT
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ID   A0A317FBX1_9PROT        Unreviewed;       158 AA.
AC   A0A317FBX1;
DT   10-OCT-2018, integrated into UniProtKB/TrEMBL.
DT   10-OCT-2018, 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:PWS36365.1};
GN   ORFNames=DFH01_14435 {ECO:0000313|EMBL:PWS36365.1};
OS   Falsiroseomonas bella.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Acetobacteraceae; Falsiroseomonas.
OX   NCBI_TaxID=2184016 {ECO:0000313|EMBL:PWS36365.1, ECO:0000313|Proteomes:UP000245765};
RN   [1] {ECO:0000313|Proteomes:UP000245765}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CQN31 {ECO:0000313|Proteomes:UP000245765};
RA   Du Z., Wang X.;
RL   Submitted (MAY-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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:PWS36365.1}.
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DR   EMBL; QGNA01000003; PWS36365.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A317FBX1; -.
DR   OrthoDB; 9809709at2; -.
DR   UniPathway; UPA00275; UER00404.
DR   Proteomes; UP000245765; 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   Reference proteome {ECO:0000313|Proteomes:UP000245765};
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         28
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   158 AA;  16659 MW;  2E2FE21E09F2B213 CRC64;
     MSTKDSPERA RAALDGPAPR VLVILAPYYA DVVGGMVRGA RGVLAEVGAT IDVADVAGAY
     ELPAALRMAL RRGGWDGFLL LGCVVRGETD HYTFICEAVC QGVMDLSVET GAPLGFGLLT
     VDTIEQAVAR SRDDRMNKGA EAAHALVQQI ALARRFAS
//
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