RISC_METTM
ID RISC_METTM Reviewed; 153 AA.
AC Q59587; D9PVD1;
DT 01-DEC-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 25-MAY-2022, entry version 106.
DE RecName: Full=Riboflavin synthase;
DE EC=2.5.1.9;
GN Name=ribC; OrderedLocusNames=MTBMA_c05840;
OS Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM
OS 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium
OS thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=79929;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-42 AND
RP 129-151.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=9139911; DOI=10.1128/jb.179.9.2938-2943.1997;
RA Eberhardt S., Korn S., Lottspeich F., Bacher A.;
RT "Biosynthesis of riboflavin: an unusual riboflavin synthase of
RT Methanobacterium thermoautotrophicum.";
RL J. Bacteriol. 179:2938-2943(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=20802048; DOI=10.1128/jb.00844-10;
RA Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H.,
RA Gottschalk G., Thauer R.K.;
RT "Complete genome sequence of Methanothermobacter marburgensis, a
RT methanoarchaeon model organism.";
RL J. Bacteriol. 192:5850-5851(2010).
CC -!- FUNCTION: The relatively low activity of this enzyme suggested that
CC 6,7-dimethyl-8-ribityllumazine might not be its natural substrate.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 6,7-dimethyl-8-(1-D-ribityl)lumazine + H(+) = 5-amino-6-(D-
CC ribitylamino)uracil + riboflavin; Xref=Rhea:RHEA:20772,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15934, ChEBI:CHEBI:57986,
CC ChEBI:CHEBI:58201; EC=2.5.1.9;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420;
CC -!- ACTIVITY REGULATION: Inhibited by EDTA.
CC -!- PATHWAY: Cofactor biosynthesis; riboflavin biosynthesis; riboflavin
CC from 2-hydroxy-3-oxobutyl phosphate and 5-amino-6-(D-
CC ribitylamino)uracil: step 2/2.
CC -!- SUBUNIT: Homooligomer.
CC -!- SIMILARITY: Belongs to the DMRL synthase family. {ECO:0000305}.
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DR EMBL; X94292; CAA63959.1; -; Genomic_DNA.
DR EMBL; CP001710; ADL58179.1; -; Genomic_DNA.
DR AlphaFoldDB; Q59587; -.
DR SMR; Q59587; -.
DR STRING; 79929.MTBMA_c05840; -.
DR EnsemblBacteria; ADL58179; ADL58179; MTBMA_c05840.
DR KEGG; mmg:MTBMA_c05840; -.
DR PATRIC; fig|79929.8.peg.568; -.
DR HOGENOM; CLU_1682776_0_0_2; -.
DR OMA; QLMTNTH; -.
DR BRENDA; 2.5.1.9; 3256.
DR UniPathway; UPA00275; UER00405.
DR Proteomes; UP000000345; Chromosome.
DR GO; GO:0009349; C:riboflavin synthase complex; IEA:InterPro.
DR GO; GO:0004746; F:riboflavin synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0009231; P:riboflavin biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd09210; Riboflavin_synthase_archaeal; 1.
DR Gene3D; 3.40.50.960; -; 1.
DR InterPro; IPR002180; LS/RS.
DR InterPro; IPR036467; LS/RS_sf.
DR InterPro; IPR006399; Ribfl_synth_arc.
DR Pfam; PF00885; DMRL_synthase; 1.
DR PIRSF; PIRSF015750; Ribfl_synth_arc; 1.
DR SUPFAM; SSF52121; SSF52121; 1.
DR TIGRFAMs; TIGR01506; ribC_arch; 1.
PE 1: Evidence at protein level;
KW Direct protein sequencing; Magnesium; Riboflavin biosynthesis; Transferase.
FT CHAIN 1..153
FT /note="Riboflavin synthase"
FT /id="PRO_0000134862"
SQ SEQUENCE 153 AA; 16969 MW; CAAE34FDA348F534 CRC64;
MIKVGICDTT FARYDMGGAA IDEIKKHATG IKIIRRTVPG IKDLPVACKK LIEEEGCEMV
MALGMPGPEE KDKVCAHEAS TGLIQAQLMT NTHILEVFVH EDEEDDPEDL KVLADNRARE
HAQNLIMMLF RPERLTRDAG MGMREGKPDV GPL
