RISB_METJA
ID RISB_METJA Reviewed; 141 AA.
AC Q57751;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=6,7-dimethyl-8-ribityllumazine synthase;
DE Short=DMRL synthase;
DE Short=LS;
DE Short=Lumazine synthase;
DE EC=2.5.1.78;
GN Name=ribH; OrderedLocusNames=MJ0303;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP PROTEIN SEQUENCE OF 1-10, FUNCTION, CATALYTIC ACTIVITY, KINETIC PARAMETERS,
RP SUBUNIT, MASS SPECTROMETRY, AND PATHWAY.
RX PubMed=12603336; DOI=10.1046/j.1432-1033.2003.03478.x;
RA Haase I., Mortl S., Kohler P., Bacher A., Fischer M.;
RT "Biosynthesis of riboflavin in archaea. 6,7-dimethyl-8-ribityllumazine
RT synthase of Methanococcus jannaschii.";
RL Eur. J. Biochem. 270:1025-1032(2003).
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:0000269|PubMed:12603336}.
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:0000269|PubMed:12603336};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=12.5 uM for 5-amino-6-(D-ribitylamino)uracil (at 37 degrees
CC Celsius and pH 7.0) {ECO:0000269|PubMed:12603336};
CC KM=52 uM for 3,4-dihydroxy-2-butanone 4-phosphate (at 37 degrees
CC Celsius and pH 7.0) {ECO:0000269|PubMed:12603336};
CC Vmax=11 nmol/min/mg enzyme (at 37 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:12603336};
CC Vmax=90 nmol/min/mg enzyme (at 70 degrees Celsius and pH 7.0)
CC {ECO:0000269|PubMed:12603336};
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:0000269|PubMed:12603336}.
CC -!- SUBUNIT: Forms an icosahedral capsid composed of 60 subunits, arranged
CC as a dodecamer of pentamers. {ECO:0000305|PubMed:12603336}.
CC -!- MASS SPECTROMETRY: Mass=15645; Method=Electrospray;
CC Evidence={ECO:0000269|PubMed:12603336};
CC -!- SIMILARITY: Belongs to the DMRL synthase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; L77117; AAB98290.1; -; Genomic_DNA.
DR PIR; H64337; H64337.
DR AlphaFoldDB; Q57751; -.
DR SMR; Q57751; -.
DR STRING; 243232.MJ_0303; -.
DR EnsemblBacteria; AAB98290; AAB98290; MJ_0303.
DR KEGG; mja:MJ_0303; -.
DR eggNOG; arCOG01323; Archaea.
DR HOGENOM; CLU_089358_3_1_2; -.
DR InParanoid; Q57751; -.
DR OMA; SGPGMTR; -.
DR PhylomeDB; Q57751; -.
DR BioCyc; MetaCyc:MON-14604; -.
DR BRENDA; 2.5.1.78; 3260.
DR SABIO-RK; Q57751; -.
DR UniPathway; UPA00275; UER00404.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0009349; C:riboflavin synthase complex; IEA:InterPro.
DR GO; GO:0000906; F:6,7-dimethyl-8-ribityllumazine synthase activity; IBA:GO_Central.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IBA:GO_Central.
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 1: Evidence at protein level;
KW Direct protein sequencing; Reference proteome; Riboflavin biosynthesis;
KW Transferase.
FT CHAIN 1..141
FT /note="6,7-dimethyl-8-ribityllumazine synthase"
FT /id="PRO_0000134843"
FT ACT_SITE 78
FT /note="Proton donor"
FT /evidence="ECO:0000255"
FT BINDING 14
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000250"
FT BINDING 46..48
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000250"
FT BINDING 70..72
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000250"
FT BINDING 75..76
FT /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58830"
FT /evidence="ECO:0000250"
FT BINDING 103
FT /ligand="5-amino-6-(D-ribitylamino)uracil"
FT /ligand_id="ChEBI:CHEBI:15934"
FT /evidence="ECO:0000250"
FT BINDING 118
FT /ligand="(2S)-2-hydroxy-3-oxobutyl phosphate"
FT /ligand_id="ChEBI:CHEBI:58830"
FT /evidence="ECO:0000250"
SQ SEQUENCE 141 AA; 15645 MW; 646C2C494E27F371 CRC64;
MVLMVNLGFV IAEFNRDITY MMEKVAEEHA EFLGATVKYK IVVPGVFDMP LAVKKLLEKD
DVDAVVTIGC VIEGETEHDE IVVHNAARKI ADLALQYDKP VTLGISGPGM TRLQAQERVD
YGKRAVEAAV KMVKRLKALE E
