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Entry: A9A633_NITMS
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ID   A9A633_NITMS            Unreviewed;       138 AA.
AC   A9A633;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   27-MAR-2024, entry version 83.
DE   RecName: Full=6,7-dimethyl-8-ribityllumazine synthase {ECO:0000256|ARBA:ARBA00012664};
DE            EC=2.5.1.78 {ECO:0000256|ARBA:ARBA00012664};
GN   OrderedLocusNames=Nmar_1615 {ECO:0000313|EMBL:ABX13511.1};
OS   Nitrosopumilus maritimus (strain SCM1).
OC   Archaea; Nitrososphaerota; Nitrososphaeria; Nitrosopumilales;
OC   Nitrosopumilaceae; Nitrosopumilus.
OX   NCBI_TaxID=436308 {ECO:0000313|EMBL:ABX13511.1, ECO:0000313|Proteomes:UP000000792};
RN   [1] {ECO:0000313|EMBL:ABX13511.1, ECO:0000313|Proteomes:UP000000792}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SCM1 {ECO:0000313|EMBL:ABX13511.1,
RC   ECO:0000313|Proteomes:UP000000792};
RX   PubMed=20421470; DOI=10.1073/pnas.0913533107;
RA   Walker C.B., de la Torre J.R., Klotz M.G., Urakawa H., Pinel N., Arp D.J.,
RA   Brochier-Armanet C., Chain P.S., Chan P.P., Gollabgir A., Hemp J.,
RA   Hugler M., Karr E.A., Konneke M., Shin M., Lawton T.J., Lowe T.,
RA   Martens-Habbena W., Sayavedra-Soto L.A., Lang D., Sievert S.M.,
RA   Rosenzweig A.C., Manning G., Stahl D.A.;
RT   "Nitrosopumilus maritimus genome reveals unique mechanisms for
RT   nitrification and autotrophy in globally distributed marine crenarchaea.";
RL   Proc. Natl. Acad. Sci. U.S.A. 107:8818-8823(2010).
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};
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   -!- SIMILARITY: Belongs to the DMRL synthase family.
CC       {ECO:0000256|ARBA:ARBA00007424}.
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DR   EMBL; CP000866; ABX13511.1; -; Genomic_DNA.
DR   AlphaFoldDB; A9A633; -.
DR   STRING; 436308.Nmar_1615; -.
DR   EnsemblBacteria; ABX13511; ABX13511; Nmar_1615.
DR   KEGG; nmr:Nmar_1615; -.
DR   eggNOG; arCOG01323; Archaea.
DR   HOGENOM; CLU_089358_3_1_2; -.
DR   InParanoid; A9A633; -.
DR   OrthoDB; 7610at2157; -.
DR   PhylomeDB; A9A633; -.
DR   UniPathway; UPA00275; UER00404.
DR   Proteomes; UP000000792; 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   CDD; cd09211; Lumazine_synthase_archaeal; 1.
DR   Gene3D; 3.40.50.960; Lumazine/riboflavin synthase; 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:UP000000792};
KW   Riboflavin biosynthesis {ECO:0000256|ARBA:ARBA00022619};
KW   Transferase {ECO:0000256|ARBA:ARBA00022679}.
SQ   SEQUENCE   138 AA;  14994 MW;  452BA5F973543B06 CRC64;
     MNIAIVVSEF NDEVTSRMLS VAQEKADSLK LKITYTCSVP GAYDMPIIVD TLLQKNDVDA
     VVTLGAIIKG QTKHDEVISH AAAQALTDLS IKHQKPVSLG ISGPGMQERH AHARIRPVAE
     RAVEAVVKIS SELKRIQK
//
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