RIBL_METPS
ID RIBL_METPS Reviewed; 139 AA.
AC D1YZF2;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 09-FEB-2010, sequence version 1.
DT 03-AUG-2022, entry version 51.
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=MCP_1752;
OS Methanocella paludicola (strain DSM 17711 / JCM 13418 / NBRC 101707 /
OS SANAE).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanocellales; Methanocellaceae; Methanocella.
OX NCBI_TaxID=304371;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17711 / JCM 13418 / NBRC 101707 / SANAE;
RX PubMed=21829548; DOI=10.1371/journal.pone.0022898;
RA Sakai S., Takaki Y., Shimamura S., Sekine M., Tajima T., Kosugi H.,
RA Ichikawa N., Tasumi E., Hiraki A.T., Shimizu A., Kato Y., Nishiko R.,
RA Mori K., Fujita N., Imachi H., Takai K.;
RT "Genome sequence of a mesophilic hydrogenotrophic methanogen Methanocella
RT paludicola, the first cultivated representative of the order
RT Methanocellales.";
RL PLoS ONE 6:E22898-E22898(2011).
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; AP011532; BAI61824.1; -; Genomic_DNA.
DR AlphaFoldDB; D1YZF2; -.
DR SMR; D1YZF2; -.
DR STRING; 304371.MCP_1752; -.
DR EnsemblBacteria; BAI61824; BAI61824; MCP_1752.
DR KEGG; mpd:MCP_1752; -.
DR PATRIC; fig|304371.9.peg.1790; -.
DR eggNOG; arCOG01222; Archaea.
DR OMA; FAKKHAD; -.
DR UniPathway; UPA00277; UER00407.
DR Proteomes; UP000001882; 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..139
FT /note="FAD synthase"
FT /id="PRO_0000406251"
FT BINDING 9..10
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02115"
FT BINDING 14..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02115"
FT BINDING 92
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02115"
SQ SEQUENCE 139 AA; 15924 MW; 2C7195B6571C5310 CRC64;
MTRVVATGTF DILHPGHVLY LSEAGKLGDE LYVIVARDST IKHKRKPLVP ENQRLFMVRA
LKCVDHAMLG SEDDMFKPIR EIDPDIITIG FNQHWDEEAL QRQLIERGLK AKVVRITKCD
TAPYASSRHI REKIKESDC
