RIBL_METJA
ID RIBL_METJA Reviewed; 149 AA.
AC Q58579;
DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 106.
DE RecName: Full=FAD synthase {ECO:0000255|HAMAP-Rule:MF_02115};
DE EC=2.7.7.2 {ECO:0000269|PubMed:20822113};
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; OrderedLocusNames=MJ1179;
OS Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM
OS 10045 / NBRC 100440) (Methanococcus jannaschii).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanocaldococcaceae; Methanocaldococcus.
OX NCBI_TaxID=243232;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=8688087; DOI=10.1126/science.273.5278.1058;
RA Bult C.J., White O., Olsen G.J., Zhou L., Fleischmann R.D., Sutton G.G.,
RA Blake J.A., FitzGerald L.M., Clayton R.A., Gocayne J.D., Kerlavage A.R.,
RA Dougherty B.A., Tomb J.-F., Adams M.D., Reich C.I., Overbeek R.,
RA Kirkness E.F., Weinstock K.G., Merrick J.M., Glodek A., Scott J.L.,
RA Geoghagen N.S.M., Weidman J.F., Fuhrmann J.L., Nguyen D., Utterback T.R.,
RA Kelley J.M., Peterson J.D., Sadow P.W., Hanna M.C., Cotton M.D.,
RA Roberts K.M., Hurst M.A., Kaine B.P., Borodovsky M., Klenk H.-P.,
RA Fraser C.M., Smith H.O., Woese C.R., Venter J.C.;
RT "Complete genome sequence of the methanogenic archaeon, Methanococcus
RT jannaschii.";
RL Science 273:1058-1073(1996).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, KINETIC
RP PARAMETERS, ACTIVITY REGULATION, GENE NAME, PATHWAY, SUBUNIT, AND
RP MUTAGENESIS OF CYS-126 AND CYS-143.
RC STRAIN=ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440;
RX PubMed=20822113; DOI=10.1021/bi100817q;
RA Mashhadi Z., Xu H., Grochowski L.L., White R.H.;
RT "Archaeal RibL: a new FAD synthetase that is air sensitive.";
RL Biochemistry 49:8748-8755(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. To a lesser extent, is also able to utilize other nucleotides
CC such as CTP and GTP as substrates, producing the modified coenzymes,
CC flavin cytosine dinucleotide (FCD) and flavin guanine dinucleotide
CC (FGD), respectively. Does not catalyze the reverse reaction to produce
CC FMN and ATP from FAD and PPi. Does not function as a glycerol-3-
CC phosphate cytidylyltransferase, as previously annotated in the complete
CC genome. {ECO:0000269|PubMed:20822113}.
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:0000269|PubMed:20822113};
CC -!- COFACTOR:
CC Name=Co(2+); Xref=ChEBI:CHEBI:48828;
CC Evidence={ECO:0000269|PubMed:20822113};
CC Note=Divalent metal cations. The best activity is observed with Co(2+),
CC where the activity is 4 and 2.5 times greater than that with Mg(2+) and
CC Mn(2+), respectively. {ECO:0000269|PubMed:20822113};
CC -!- ACTIVITY REGULATION: Is inhibited by the product PPi.
CC {ECO:0000269|PubMed:20822113}.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=25 uM for ATP {ECO:0000269|PubMed:20822113};
CC KM=63 uM for FMN {ECO:0000269|PubMed:20822113};
CC KM=480 uM for CTP {ECO:0000269|PubMed:20822113};
CC Vmax=14 nmol/min/mg enzyme with ATP and FMN as substrates
CC {ECO:0000269|PubMed:20822113};
CC Vmax=10 nmol/min/mg enzyme with CTP and FMN as substrates
CC {ECO:0000269|PubMed:20822113};
CC -!- PATHWAY: Cofactor biosynthesis; FAD biosynthesis; FAD from FMN: step
CC 1/1. {ECO:0000269|PubMed:20822113}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:20822113}.
CC -!- MISCELLANEOUS: Alkylation of both Cys-126 and Cys-143 results in
CC complete loss of enzymatic activity. {ECO:0000269|PubMed:20822113}.
CC -!- SIMILARITY: Belongs to the archaeal FAD synthase family. {ECO:0000305}.
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DR EMBL; L77117; AAB99182.1; -; Genomic_DNA.
DR PIR; B64447; B64447.
DR RefSeq; WP_010870692.1; NC_000909.1.
DR AlphaFoldDB; Q58579; -.
DR SMR; Q58579; -.
DR STRING; 243232.MJ_1179; -.
DR EnsemblBacteria; AAB99182; AAB99182; MJ_1179.
DR GeneID; 1452077; -.
DR KEGG; mja:MJ_1179; -.
DR eggNOG; arCOG01222; Archaea.
DR HOGENOM; CLU_034585_2_1_2; -.
DR InParanoid; Q58579; -.
DR OMA; FAKKHAD; -.
DR OrthoDB; 79845at2157; -.
DR PhylomeDB; Q58579; -.
DR BioCyc; MetaCyc:MON-16487; -.
DR BRENDA; 2.7.7.2; 3260.
DR SABIO-RK; Q58579; -.
DR UniPathway; UPA00277; UER00407.
DR Proteomes; UP000000805; Chromosome.
DR GO; GO:0005524; F:ATP binding; IDA:UniProtKB.
DR GO; GO:0002135; F:CTP binding; IDA:UniProtKB.
DR GO; GO:0003919; F:FMN adenylyltransferase activity; IDA:UniProtKB.
DR GO; GO:0010181; F:FMN binding; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0006747; P:FAD biosynthetic process; IDA:UniProtKB.
DR GO; GO:0046444; P:FMN metabolic process; IDA:UniProtKB.
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 1: Evidence at protein level;
KW ATP-binding; FAD; Flavoprotein; FMN; Nucleotide-binding;
KW Nucleotidyltransferase; Reference proteome; Transferase.
FT CHAIN 1..149
FT /note="FAD synthase"
FT /id="PRO_0000107202"
FT BINDING 10..11
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02115"
FT BINDING 15..18
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 123
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_02115"
FT MUTAGEN 126
FT /note="C->S: 2-fold increase in activity with Mg(2+) but
FT loss of activity with Co(2+) as cofactor."
FT /evidence="ECO:0000269|PubMed:20822113"
FT MUTAGEN 143
FT /note="C->S: Nearly no change in activity with Mg(2+) but
FT loss of activity with Co(2+) as cofactor."
FT /evidence="ECO:0000269|PubMed:20822113"
SQ SEQUENCE 149 AA; 17288 MW; 55FD11671ED94594 CRC64;
MKKRVVTAGT FDILHPGHYE ILKFAKSLGD ELIVIVARDE TVKKLKGRKP IIPEEQRREM
VEALKPVDKA ILGSLKNKLE PILELKPDII VLGPDQTTFD EETLKKELAK YNLYPEIVRF
RGYKKCPFHS SFDIVKEIIR RFCNKEIKI
