ID   CFBC_METBF              Reviewed;         265 AA.
AC   Q46FL1;
DT   22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 116.
DE   RecName: Full=Ni-sirohydrochlorin a,c-diamide reductive cyclase complex, component CfbC {ECO:0000303|PubMed:28225763};
DE            EC=6.3.3.7 {ECO:0000269|PubMed:28225763};
DE   AltName: Full=NifH homolog component CfbC {ECO:0000303|PubMed:28225763};
GN   Name=cfbC {ECO:0000303|PubMed:28225763};
GN   OrderedLocusNames=Mbar_A0347 {ECO:0000312|EMBL:AAZ69331.1};
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, CATALYTIC ACTIVITY, COFACTOR, AND SUBUNIT.
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 both the six-electron reduction of the
CC       tetrahydroporphyrin ring system and the gamma-lactamization of the c-
CC       acetamide side chain of Ni-sirohydrochlorin a,c-diamide to yield
CC       15,17(3)-seco-F430-17(3)-acid (seco-F430), the last intermediate in the
CC       biosynthesis of the coenzyme F430. {ECO:0000269|PubMed:28225763}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=3 AH2 + ATP + H2O + Ni-sirohydrochlorin a,c-diamide =
CC         15,17(3)-seco-F430-17(3)-acid + 3 A + ADP + phosphate;
CC         Xref=Rhea:RHEA:52900, ChEBI:CHEBI:13193, ChEBI:CHEBI:15377,
CC         ChEBI:CHEBI:17499, ChEBI:CHEBI:30616, ChEBI:CHEBI:43474,
CC         ChEBI:CHEBI:136887, ChEBI:CHEBI:136888, ChEBI:CHEBI:456216;
CC         EC=6.3.3.7; Evidence={ECO:0000269|PubMed:28225763};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000269|PubMed:28225763};
CC   -!- SUBUNIT: Homodimer. The Ni-sirohydrochlorin a,c-diamide reductive
CC       cyclase complex is composed of a NifH homolog component CfbC and a NifD
CC       homolog component CfbD. {ECO:0000269|PubMed:28225763}.
CC   -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family. {ECO:0000305}.
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DR   EMBL; CP000099; AAZ69331.1; -; Genomic_DNA.
DR   RefSeq; WP_011305384.1; NC_007355.1.
DR   AlphaFoldDB; Q46FL1; -.
DR   SMR; Q46FL1; -.
DR   STRING; 269797.Mbar_A0347; -.
DR   EnsemblBacteria; AAZ69331; AAZ69331; Mbar_A0347.
DR   GeneID; 3626591; -.
DR   KEGG; mba:Mbar_A0347; -.
DR   eggNOG; arCOG00590; Archaea.
DR   HOGENOM; CLU_059373_0_0_2; -.
DR   OMA; YVCDYYL; -.
DR   OrthoDB; 66372at2157; -.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   GO; GO:0015948; P:methanogenesis; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.300; -; 1.
DR   InterPro; IPR030655; NifH/chlL_CS.
DR   InterPro; IPR000392; NifH/frxC.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR42864; PTHR42864; 1.
DR   Pfam; PF00142; Fer4_NifH; 1.
DR   PIRSF; PIRSF000363; Nitrogenase_iron; 1.
DR   SUPFAM; SSF52540; SSF52540; 1.
DR   PROSITE; PS00746; NIFH_FRXC_1; 1.
DR   PROSITE; PS51026; NIFH_FRXC_3; 1.
PE   1: Evidence at protein level;
KW   ATP-binding; Iron; Iron-sulfur; Ligase; Metal-binding; Methanogenesis;
KW   Nucleotide-binding.
FT   CHAIN           1..265
FT                   /note="Ni-sirohydrochlorin a,c-diamide reductive cyclase
FT                   complex, component CfbC"
FT                   /id="PRO_0000442425"
SQ   SEQUENCE   265 AA;  28578 MW;  CF2E42B227CF3C00 CRC64;
     MKNQKIIAIY GKGGIGKSST ASNVAAACAE AGKKVMIIGC DPKSDSSITL LRGRRIPTIL
     DLLREGVDIK KEDVVFEGYA GVKCVEAGGP EPGIGCAGRG IIVAIQKLKS ISGNLLKEQD
     LIIYDVPGDI VCGGFVAPVR KGFVNEAYVL TSGEYMPLYA ANNICKGLSK IGMPLSGVIC
     NSRNVSREEE IVSKFSEEIG SQLMAFIPKR QVVQDCEREG YSVMEKAPES DIAEIYRKLG
     KAILENEKRV TADSLSDERL RELTK