ID   CFBE_METBF              Reviewed;         528 AA.
AC   Q46FL3;
DT   22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   03-AUG-2022, entry version 85.
DE   RecName: Full=Coenzyme F(430) synthetase {ECO:0000303|PubMed:28225763};
DE            EC=6.4.1.9 {ECO:0000269|PubMed:28225763};
GN   Name=cfbE {ECO:0000303|PubMed:28225763};
GN   OrderedLocusNames=Mbar_A0345 {ECO:0000312|EMBL:AAZ69329.1};
OS   Methanosarcina barkeri (strain Fusaro / DSM 804).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=269797;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=16980466; DOI=10.1128/jb.00810-06;
RA   Maeder D.L., Anderson I., Brettin T.S., Bruce D.C., Gilna P., Han C.S.,
RA   Lapidus A., Metcalf W.W., Saunders E., Tapia R., Sowers K.R.;
RT   "The Methanosarcina barkeri genome: comparative analysis with
RT   Methanosarcina acetivorans and Methanosarcina mazei reveals extensive
RT   rearrangement within methanosarcinal genomes.";
RL   J. Bacteriol. 188:7922-7931(2006).
RN   [2]
RP   FUNCTION, AND CATALYTIC ACTIVITY.
RC   STRAIN=Fusaro / DSM 804;
RX   PubMed=28225763; DOI=10.1038/nature21427;
RA   Moore S.J., Sowa S.T., Schuchardt C., Deery E., Lawrence A.D., Ramos J.V.,
RA   Billig S., Birkemeyer C., Chivers P.T., Howard M.J., Rigby S.E., Layer G.,
RA   Warren M.J.;
RT   "Elucidation of the biosynthesis of the methane catalyst coenzyme F430.";
RL   Nature 543:78-82(2017).
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:0000269|PubMed:28225763}.
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:0000269|PubMed:28225763};
CC   -!- SIMILARITY: Belongs to the MurCDEF family. {ECO:0000305}.
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DR   EMBL; CP000099; AAZ69329.1; -; Genomic_DNA.
DR   RefSeq; WP_011305382.1; NC_007355.1.
DR   AlphaFoldDB; Q46FL3; -.
DR   SMR; Q46FL3; -.
DR   STRING; 269797.Mbar_A0345; -.
DR   EnsemblBacteria; AAZ69329; AAZ69329; Mbar_A0345.
DR   GeneID; 3626589; -.
DR   KEGG; mba:Mbar_A0345; -.
DR   eggNOG; arCOG02822; Archaea.
DR   HOGENOM; CLU_047362_0_0_2; -.
DR   OMA; VIAPVHC; -.
DR   OrthoDB; 50390at2157; -.
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   1: Evidence at protein level;
KW   ATP-binding; Ligase; Methanogenesis; Nucleotide-binding.
FT   CHAIN           1..528
FT                   /note="Coenzyme F(430) synthetase"
FT                   /id="PRO_0000442423"
FT   REGION          300..348
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        304..345
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   BINDING         119..125
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255"
SQ   SEQUENCE   528 AA;  56050 MW;  C95B5F9646D93578 CRC64;
     MDLYRKKFAV LDLTHGGIPI AKSLAAAGNE VSGIDVYRTV KPETLLELEE KYGIHCSKTP
     LPASGFDLIV APVHLDPAYP MLLEARAQKK KVLSHHEIVG EILKGDSRLS SIKTVEVTGV
     KAKTSTASLL ADMLSRQFEV VLHTSRGLEC WKAGASSLIY KGLSITPGSI LVAVEKTFEA
     GFRPDFFIFE ISIGGTGTAD LGILTTLSPD YGIANNTALA SEAKLQLIKH AKSGSTLLIN
     AGAEKALKAA KKDQVKVLTF RDPFNDQLSA TSVQIADFVL ETVPETSALS VPSELVMPSG
     LQKPAGLSGS SEPDSLSGSS TSAGLSDSSM PAGSTEFQAS PTPSGSDIRF MRRGKKILSA
     SLRPGYNVSA YRTAFVAASA AAIELGTKPE AIISAIEGFR GLSGRMQEKE MNGVSLIDNS
     NSGMDILSAE KALDYALLKR KDEKKEGIIL VLGEESSQVC EGLPPELVQG FIEKFGAKCK
     QVILVGERMK AVNGKNISYA RDLTEGLSKA SEFAGGDDII LSSVKCFR