(data stored in ACNUC7421 zone)

SWISSPROT: D4YXP6_SPHJU

ID   D4YXP6_SPHJU            Unreviewed;       140 AA.
AC   D4YXP6;
DT   15-JUN-2010, integrated into UniProtKB/TrEMBL.
DT   15-JUN-2010, sequence version 1.
DT   05-JUL-2017, entry version 49.
DE   RecName: Full=6,7-dimethyl-8-ribityllumazine synthase {ECO:0000256|HAMAP-Rule:MF_00178, ECO:0000256|SAAS:SAAS00819689};
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:SAAS00819689};
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 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=NBRC 101211 / UT26S {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:SAAS00819691}.
CC   -!- CATALYTIC ACTIVITY: 1-deoxy-L-glycero-tetrulose 4-phosphate + 5-
CC       amino-6-(D-ribitylamino)uracil = 6,7-dimethyl-8-(D-
CC       ribityl)lumazine + 2 H(2)O + phosphate. {ECO:0000256|HAMAP-
CC       Rule:MF_00178, ECO:0000256|SAAS:SAAS00819686}.
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:SAAS00819687}.
CC   -!- SIMILARITY: Belongs to the DMRL synthase family.
CC       {ECO:0000256|HAMAP-Rule:MF_00178, ECO:0000256|SAAS:SAAS00654790}.
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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   OrthoDB; POG091H021R; -.
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-HAMAP.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-HAMAP.
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   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   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:SAAS00654787};
KW   Transferase {ECO:0000256|HAMAP-Rule:MF_00178,
KW   ECO:0000256|SAAS:SAAS00654778, 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   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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