ID   CFBD_METTH              Reviewed;         359 AA.
AC   O27566;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1998, sequence version 1.
DT   25-MAY-2022, entry version 98.
DE   RecName: Full=Ni-sirohydrochlorin a,c-diamide reductive cyclase complex, component CfbD {ECO:0000250|UniProtKB:Q46FL2};
DE            EC=6.3.3.7 {ECO:0000250|UniProtKB:Q46FL2};
DE   AltName: Full=NifD homolog component CfbD {ECO:0000250|UniProtKB:Q46FL2};
GN   Name=cfbD {ECO:0000250|UniProtKB:Q8TJZ8}; OrderedLocusNames=MTH_1522;
OS   Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS   10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=187420;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX   PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA   Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA   Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA   Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA   Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA   Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA   Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA   Reeve J.N.;
RT   "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT   functional analysis and comparative genomics.";
RL   J. Bacteriol. 179:7135-7155(1997).
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:0000250|UniProtKB:Q46FL2}.
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:0000250|UniProtKB:Q46FL2};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:Q46FL2};
CC   -!- SUBUNIT: Homodimer or monomer. The Ni-sirohydrochlorin a,c-diamide
CC       reductive cyclase complex is composed of a NifH homolog component CfbC
CC       and a NifD homolog component CfbD. {ECO:0000250|UniProtKB:Q46FL2}.
CC   -!- SIMILARITY: Belongs to the NifD/NifK/NifE/NifN family.
CC       {ECO:0000250|UniProtKB:Q46FL2}.
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DR   EMBL; AE000666; AAB85997.1; -; Genomic_DNA.
DR   PIR; B69070; B69070.
DR   RefSeq; WP_010877132.1; NC_000916.1.
DR   AlphaFoldDB; O27566; -.
DR   SMR; O27566; -.
DR   STRING; 187420.MTH_1522; -.
DR   EnsemblBacteria; AAB85997; AAB85997; MTH_1522.
DR   GeneID; 1471791; -.
DR   KEGG; mth:MTH_1522; -.
DR   PATRIC; fig|187420.15.peg.1485; -.
DR   HOGENOM; CLU_782144_0_0_2; -.
DR   OMA; CASMIIG; -.
DR   Proteomes; UP000005223; Chromosome.
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   InterPro; IPR017675; CfbD.
DR   InterPro; IPR000510; Nase/OxRdtase_comp1.
DR   Pfam; PF00148; Oxidored_nitro; 1.
DR   TIGRFAMs; TIGR03282; methan_mark_13; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Iron; Iron-sulfur; Ligase; Metal-binding; Methanogenesis;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..359
FT                   /note="Ni-sirohydrochlorin a,c-diamide reductive cyclase
FT                   complex, component CfbD"
FT                   /id="PRO_0000107318"
SQ   SEQUENCE   359 AA;  39102 MW;  12B1FF882D80D28F CRC64;
     MHPRPSPIAA SLYTLRDLDA DVIILHGPHG CCFRTGRLLE TDGVRVLTTA MSEQDFIFGA
     SDKLTETLRK AYEMFSPKLV GVVGTCASMI IGEDLKEAVQ RAGIPARVLA VESHGGFGEG
     DNTEGAIIVL EAAAEQGIIP EEEAERQIKM LKLATEIEKT RGMAQGKYIR PSYGDDKDEV
     ALRVLEAIME GRRVAFVLNA KKETSYLFAD TLTLPFGSLN PDNPPIIIAN LDKGIGLPRI
     RRHAENILSE IERSGNRVEH ITGGLDEYPI TGARAAEILR NEEIEFAVVS GVPHALPVEE
     LGLESVAVTD GPRLVEPLRG LGYTHVVAEL DAHARTLGQR SIVESDFGDA LRRNIKKVI