RIBL_METRM
ID RIBL_METRM Reviewed; 150 AA.
AC D3DZ18;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 23-MAR-2010, sequence version 1.
DT 03-AUG-2022, entry version 58.
DE RecName: Full=FAD synthase {ECO:0000255|HAMAP-Rule:MF_02115};
DE EC=2.7.7.2 {ECO:0000255|HAMAP-Rule:MF_02115};
DE AltName: Full=FMN adenylyltransferase {ECO:0000255|HAMAP-Rule:MF_02115};
DE AltName: Full=Flavin adenine dinucleotide synthase {ECO:0000255|HAMAP-Rule:MF_02115};
GN Name=ribL {ECO:0000255|HAMAP-Rule:MF_02115}; OrderedLocusNames=mru_1718;
OS Methanobrevibacter ruminantium (strain ATCC 35063 / DSM 1093 / JCM 13430 /
OS OCM 146 / M1) (Methanobacterium ruminantium).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanobrevibacter.
OX NCBI_TaxID=634498;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35063 / DSM 1093 / JCM 13430 / OCM 146 / M1;
RX PubMed=20126622; DOI=10.1371/journal.pone.0008926;
RA Leahy S.C., Kelly W.J., Altermann E., Ronimus R.S., Yeoman C.J.,
RA Pacheco D.M., Li D., Kong Z., McTavish S., Sang C., Lambie S.C.,
RA Janssen P.H., Dey D., Attwood G.T.;
RT "The genome sequence of the rumen methanogen Methanobrevibacter ruminantium
RT reveals new possibilities for controlling ruminant methane emissions.";
RL PLoS ONE 5:E8926-E8926(2010).
CC -!- FUNCTION: Catalyzes the transfer of the AMP portion of ATP to flavin
CC mononucleotide (FMN) to produce flavin adenine dinucleotide (FAD)
CC coenzyme. {ECO:0000255|HAMAP-Rule:MF_02115}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + FMN + H(+) = diphosphate + FAD; Xref=Rhea:RHEA:17237,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:30616, ChEBI:CHEBI:33019,
CC ChEBI:CHEBI:57692, ChEBI:CHEBI:58210; EC=2.7.7.2;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02115};
CC -!- COFACTOR:
CC Name=a divalent metal cation; Xref=ChEBI:CHEBI:60240;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_02115};
CC -!- PATHWAY: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step
CC 1/1. {ECO:0000255|HAMAP-Rule:MF_02115}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_02115}.
CC -!- SIMILARITY: Belongs to the archaeal FAD synthase family.
CC {ECO:0000255|HAMAP-Rule:MF_02115}.
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DR EMBL; CP001719; ADC47568.1; -; Genomic_DNA.
DR AlphaFoldDB; D3DZ18; -.
DR SMR; D3DZ18; -.
DR STRING; 634498.mru_1718; -.
DR PRIDE; D3DZ18; -.
DR EnsemblBacteria; ADC47568; ADC47568; mru_1718.
DR KEGG; mru:mru_1718; -.
DR PATRIC; fig|634498.28.peg.1719; -.
DR eggNOG; arCOG01222; Archaea.
DR HOGENOM; CLU_034585_2_1_2; -.
DR OMA; FAKKHAD; -.
DR UniPathway; UPA00277; UER00407.
DR Proteomes; UP000008680; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003919; F:FMN adenylyltransferase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0006747; P:FAD biosynthetic process; IEA:UniProtKB-UniRule.
DR GO; GO:0046444; P:FMN metabolic process; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.620; -; 1.
DR HAMAP; MF_02115; FAD_synth_arch; 1.
DR InterPro; IPR004821; Cyt_trans-like.
DR InterPro; IPR024902; FAD_synth_RibL.
DR InterPro; IPR014729; Rossmann-like_a/b/a_fold.
DR Pfam; PF01467; CTP_transf_like; 1.
DR TIGRFAMs; TIGR00125; cyt_tran_rel; 1.
PE 3: Inferred from homology;
KW ATP-binding; FAD; Flavoprotein; FMN; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..150
FT /note="FAD synthase"
FT /id="PRO_0000406245"
FT BINDING 8..9
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02115"
FT BINDING 13..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02115"
FT BINDING 95
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02115"
FT BINDING 122
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02115"
SQ SEQUENCE 150 AA; 16979 MW; 13F291B37F32730C CRC64;
MKVMATGAFD ILHPGHGLYL EKAKELGGED AVLAVVIARD STVKKKKRIP VIDENQRLEM
IKYLKPVDEA YIGHDGDMFE IVEEIKPDII AIGFDQGHDV NKLQEELDKR GIKAKAMRVE
AHRIADLDST CKIIKKIRNS DFEEDYVNCD