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ID D4YXP6_SPHJU Unreviewed; 140 AA.
AC D4YXP6;
DT 15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT 15-JUN-2010, sequence version 1.
DT 08-MAY-2019, entry version 58.
DE RecName: Full=6,7-dimethyl-8-ribityllumazine synthase {ECO:0000256|HAMAP-Rule:MF_00178, ECO:0000256|SAAS:SAAS01078290};
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|HAMAP-Rule:MF_00178, ECO:0000256|SAAS:SAAS01078290};
GN Name=ribH {ECO:0000256|HAMAP-Rule:MF_00178,
GN ECO:0000313|EMBL:BAI95128.1};
GN OrderedLocusNames=SJA_C1-02940 {ECO:0000313|EMBL:BAI95128.1};
OS Sphingobium japonicum (strain DSM 16413 / CCM 7287 / MTCC 6362 / UT26
OS / NBRC 101211 / UT26S).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingobium.
OX NCBI_TaxID=452662 {ECO:0000313|EMBL:BAI95128.1, ECO:0000313|Proteomes:UP000007753};
RN [1] {ECO:0000313|EMBL:BAI95128.1, ECO:0000313|Proteomes:UP000007753}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16413 / CCM 7287 / MTCC 6362 / UT26 / NBRC 101211 / UT26S
RC {ECO:0000313|Proteomes:UP000007753};
RX PubMed=20817768; DOI=10.1128/JB.00961-10;
RA Nagata Y., Ohtsubo Y., Endo R., Ichikawa N., Ankai A., Oguchi A.,
RA Fukui S., Fujita N., Tsuda M.;
RT "Complete genome sequence of the representative gamma-
RT hexachlorocyclohexane-degrading bacterium Sphingobium japonicum
RT UT26.";
RL J. Bacteriol. 192:5852-5853(2010).
CC -!- FUNCTION: Catalyzes the formation of 6,7-dimethyl-8-
CC ribityllumazine by condensation of 5-amino-6-(D-
CC ribitylamino)uracil with 3,4-dihydroxy-2-butanone 4-phosphate.
CC This is the penultimate step in the biosynthesis of riboflavin.
CC {ECO:0000256|HAMAP-Rule:MF_00178, ECO:0000256|SAAS:SAAS01078298}.
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 +
CC H(+) + 2 H2O + phosphate; Xref=Rhea:RHEA:26152,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15934,
CC ChEBI:CHEBI:43474, ChEBI:CHEBI:58201, ChEBI:CHEBI:58830;
CC EC=2.5.1.78; Evidence={ECO:0000256|HAMAP-Rule:MF_00178,
CC ECO:0000256|SAAS:SAAS01115780};
CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis;
CC riboflavin from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-
CC ribitylamino)uracil: step 1/2. {ECO:0000256|HAMAP-Rule:MF_00178,
CC ECO:0000256|SAAS:SAAS01078315}.
CC -!- SIMILARITY: Belongs to the DMRL synthase family.
CC {ECO:0000256|HAMAP-Rule:MF_00178, ECO:0000256|SAAS:SAAS00579181}.
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DR EMBL; AP010803; BAI95128.1; -; Genomic_DNA.
DR RefSeq; WP_007686994.1; NC_014006.1.
DR STRING; 452662.SJA_C1-02940; -.
DR EnsemblBacteria; BAI95128; BAI95128; SJA_C1-02940.
DR GeneID; 29271997; -.
DR KEGG; sjp:SJA_C1-02940; -.
DR eggNOG; ENOG4108UTT; Bacteria.
DR eggNOG; COG0054; LUCA.
DR HOGENOM; HOG000229250; -.
DR KO; K00794; -.
DR OMA; HGNKGTE; -.
DR UniPathway; UPA00275; UER00404.
DR Proteomes; UP000007753; 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; -; 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 3: Inferred from homology;
DR PRODOM; D4YXP6.
DR SWISS-2DPAGE; D4YXP6.
KW Coiled coil {ECO:0000256|SAM:Coils};
KW Complete proteome {ECO:0000313|Proteomes:UP000007753};
KW Reference proteome {ECO:0000313|Proteomes:UP000007753};
KW Riboflavin biosynthesis {ECO:0000256|HAMAP-Rule:MF_00178,
KW ECO:0000256|SAAS:SAAS00470718};
KW Transferase {ECO:0000256|HAMAP-Rule:MF_00178,
KW ECO:0000256|SAAS:SAAS00106446, ECO:0000313|EMBL:BAI95128.1}.
FT REGION 42 44 5-amino-6-(D-ribitylamino)uracil binding.
FT {ECO:0000256|HAMAP-Rule:MF_00178}.
FT REGION 66 68 5-amino-6-(D-ribitylamino)uracil binding.
FT {ECO:0000256|HAMAP-Rule:MF_00178}.
FT REGION 71 72 1-deoxy-L-glycero-tetrulose 4-phosphate
FT binding. {ECO:0000256|HAMAP-Rule:
FT MF_00178}.
FT COILED 100 120 {ECO:0000256|SAM:Coils}.
FT ACT_SITE 74 74 Proton donor. {ECO:0000256|HAMAP-Rule:
FT MF_00178}.
FT BINDING 11 11 5-amino-6-(D-ribitylamino)uracil.
FT {ECO:0000256|HAMAP-Rule:MF_00178}.
FT BINDING 98 98 5-amino-6-(D-ribitylamino)uracil; via
FT amide nitrogen and carbonyl oxygen.
FT {ECO:0000256|HAMAP-Rule:MF_00178}.
FT BINDING 112 112 1-deoxy-L-glycero-tetrulose 4-phosphate.
FT {ECO:0000256|HAMAP-Rule:MF_00178}.
SQ SEQUENCE 140 AA; 14919 MW; 61220563CF8F0136 CRC64;
MAKFLIVEAR FYEHLNDLLI EGAVAALEDE GHKYEVVTVP GALEIPGAVA LAAETGRYDG
FIAIGVVIRG ETYHFEVVSN ESARGLMALS MDGIPIGNGI LTVENEAQAL TRAKKQEKDK
GGEAAKAAMA MLALREKFGA
//
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