ID   CFBD_METJA              Reviewed;         352 AA.
AC   Q58818;
DT   15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1996, sequence version 1.
DT   25-MAY-2022, entry version 100.
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:Q46FL2}; OrderedLocusNames=MJ1423;
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 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; L77117; AAB99434.1; -; Genomic_DNA.
DR   PIR; F64477; F64477.
DR   RefSeq; WP_010870941.1; NC_000909.1.
DR   AlphaFoldDB; Q58818; -.
DR   SMR; Q58818; -.
DR   STRING; 243232.MJ_1423; -.
DR   DNASU; 1452327; -.
DR   EnsemblBacteria; AAB99434; AAB99434; MJ_1423.
DR   GeneID; 1452327; -.
DR   KEGG; mja:MJ_1423; -.
DR   eggNOG; arCOG04888; Archaea.
DR   HOGENOM; CLU_782144_0_0_2; -.
DR   InParanoid; Q58818; -.
DR   OMA; CASMIIG; -.
DR   OrthoDB; 56870at2157; -.
DR   PhylomeDB; Q58818; -.
DR   Proteomes; UP000000805; 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..352
FT                   /note="Ni-sirohydrochlorin a,c-diamide reductive cyclase
FT                   complex, component CfbD"
FT                   /id="PRO_0000107317"
SQ   SEQUENCE   352 AA;  39470 MW;  F95B6F9C6095B0EB CRC64;
     MIFHPRPSPI AAAMYQLRDL GVDAIILHGP SGCCFRTARL LELDGVRVFT SNIDENAIVF
     GASENLKKAL DYAIEYLKKE LKKERPMIGI VGTCASMIIG EDLWEFVDDD RAIIIPVEVH
     SGSGDNTIGA IKAMESALKL GIIDEKEFER QKFLLKKATE VEKKRGMAKK EYIKPTYDDD
     LNEAIKVLKD LKEKDGKIAC VLNAKKETAY LFAHPLIVLN KYFNCVNIAN LDINKGLPKI
     RRDAQNILRR FKADYITGGL DEYPITGERA VEILKDLDVD AIVVSGVPHA LPIEEIDKDI
     IKIGISDGPR TYHPIKEIYD YAIVELDAHA KVLGKRDIVK SRFGEILDYA LE