RIBL_METAC
ID RIBL_METAC Reviewed; 151 AA.
AC Q8TPT5;
DT 05-APR-2011, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 95.
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=MA_1820;
OS Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS C2A).
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=188937;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX PubMed=11932238; DOI=10.1101/gr.223902;
RA Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT physiological diversity.";
RL Genome Res. 12:532-542(2002).
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; AE010299; AAM05226.1; -; Genomic_DNA.
DR RefSeq; WP_011021822.1; NC_003552.1.
DR AlphaFoldDB; Q8TPT5; -.
DR SMR; Q8TPT5; -.
DR STRING; 188937.MA_1820; -.
DR EnsemblBacteria; AAM05226; AAM05226; MA_1820.
DR GeneID; 1473709; -.
DR KEGG; mac:MA_1820; -.
DR HOGENOM; CLU_034585_2_1_2; -.
DR InParanoid; Q8TPT5; -.
DR OMA; FAKKHAD; -.
DR OrthoDB; 79845at2157; -.
DR PhylomeDB; Q8TPT5; -.
DR UniPathway; UPA00277; UER00407.
DR Proteomes; UP000002487; 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..151
FT /note="FAD synthase"
FT /id="PRO_0000406268"
FT BINDING 21..22
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02115"
FT BINDING 26..29
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02115"
FT BINDING 104
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02115"
SQ SEQUENCE 151 AA; 16805 MW; 0A5799CC78D024D4 CRC64;
MLAGCYPRPG DLLTRVLATG TFDILHPGHV YFLTQARALG DELFVIIARD SNVTHKPKPI
VPEEQRLEMV NALGTVDKAL LGSEKDMFEP LKEIRPDIIV LGYDQHFDIE LLEEELTKRG
LPAKVVRVPL SKECPLCSTG AIIKAVLKRY G
