ID   CFBE_METJA              Reviewed;         404 AA.
AC   Q57706;
DT   01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Coenzyme F(430) synthetase {ECO:0000250|UniProtKB:Q8TJZ6};
DE            EC=6.4.1.9 {ECO:0000250|UniProtKB:Q8TJZ6};
GN   Name=cfbE {ECO:0000250|UniProtKB:Q8TJZ6}; OrderedLocusNames=MJ0258;
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).
CC   -!- FUNCTION: Involved in the biosynthesis of the unique nickel-containing
CC       tetrapyrrole coenzyme F430, the prosthetic group of methyl-coenzyme M
CC       reductase (MCR), which plays a key role in methanogenesis and anaerobic
CC       methane oxidation. Catalyzes the activation the g-propionate side chain
CC       of 15,17(3)-seco-F430-17(3)-acid (seco-F430) for intramolecular C-C
CC       bond formation to yield the carbocyclic F ring of coenzyme F430.
CC       {ECO:0000250|UniProtKB:Q8TJZ6}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=15,17(3)-seco-F430-17(3)-acid + ATP = ADP + coenzyme F430 +
CC         phosphate; Xref=Rhea:RHEA:52904, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:60540, ChEBI:CHEBI:136888,
CC         ChEBI:CHEBI:456216; EC=6.4.1.9;
CC         Evidence={ECO:0000250|UniProtKB:Q8TJZ6};
CC   -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000305}.
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DR   EMBL; L77117; AAB98245.1; -; Genomic_DNA.
DR   PIR; C64332; C64332.
DR   AlphaFoldDB; Q57706; -.
DR   SMR; Q57706; -.
DR   STRING; 243232.MJ_0258; -.
DR   EnsemblBacteria; AAB98245; AAB98245; MJ_0258.
DR   KEGG; mja:MJ_0258; -.
DR   eggNOG; arCOG02822; Archaea.
DR   HOGENOM; CLU_047362_0_0_2; -.
DR   InParanoid; Q57706; -.
DR   OMA; VIAPVHC; -.
DR   PhylomeDB; Q57706; -.
DR   Proteomes; UP000000805; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.1190.10; -; 1.
DR   InterPro; IPR036565; Mur-like_cat_sf.
DR   InterPro; IPR013221; Mur_ligase_cen.
DR   Pfam; PF08245; Mur_ligase_M; 1.
DR   SUPFAM; SSF53623; SSF53623; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Methanogenesis; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..404
FT                   /note="Coenzyme F(430) synthetase"
FT                   /id="PRO_0000106760"
FT   BINDING         112..117
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   404 AA;  46913 MW;  C9FDE688807D0746 CRC64;
     MVFFMLIIDV NHGALTLAEE YLNLGYEVDV WDIYQKIKKS EDFKVKYQKL KEKFGNKLNL
     FFEQPNFEKY DRVIAPIHCP IDVDFIPFTD AVSKILKEKF GNIHKKIINV TGVKGKTTTT
     SLINHILKDK YSTYLHNSNF GSIAPPTILK VLNSLDIDKY DFFIFETSLG LIKCKYGAIT
     NVLENYKIAG GRKDALTAKF SSLKNAELSF INKRDINRYD LNINHKCLNV VDVDRAKILD
     KYPLKFKYFD EIFEFSKNIF GLHFVENSLF AIEICKNLVD MEEIRYRLKT FTIKNRMEIK
     EINKKILVKN INPGLDVKAI SYAIKDFLEV FGGDIYIGGD FGIVCEEIDV KKLSEVLKRF
     NCRYIFVGEI GKELLNYLNG GYIKSYDENK IKRDSLVILR EKIK