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CFBD_METBF
ID   CFBD_METBF              Reviewed;         370 AA.
AC   Q46FL2;
DT   22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT   13-SEP-2005, sequence version 1.
DT   25-MAY-2022, entry version 93.
DE   RecName: Full=Ni-sirohydrochlorin a,c-diamide reductive cyclase complex, component CfbD {ECO:0000303|PubMed:28225763};
DE            EC=6.3.3.7 {ECO:0000269|PubMed:28225763};
DE   AltName: Full=NifD homolog component CfbD {ECO:0000303|PubMed:28225763};
DE   AltName: Full=Nitrogenase-like protein {ECO:0000303|PubMed:28225763};
GN   Name=cfbD {ECO:0000303|PubMed:28225763};
GN   OrderedLocusNames=Mbar_A0346 {ECO:0000312|EMBL:AAZ69330.1};
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 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:0000269|PubMed:28225763}.
CC   -!- SIMILARITY: Belongs to the NifD/NifK/NifE/NifN family. {ECO:0000305}.
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DR   EMBL; CP000099; AAZ69330.1; -; Genomic_DNA.
DR   RefSeq; WP_011305383.1; NC_007355.1.
DR   AlphaFoldDB; Q46FL2; -.
DR   SMR; Q46FL2; -.
DR   STRING; 269797.Mbar_A0346; -.
DR   EnsemblBacteria; AAZ69330; AAZ69330; Mbar_A0346.
DR   GeneID; 3626590; -.
DR   KEGG; mba:Mbar_A0346; -.
DR   eggNOG; arCOG04888; Archaea.
DR   HOGENOM; CLU_782144_0_0_2; -.
DR   OMA; CASMIIG; -.
DR   OrthoDB; 56870at2157; -.
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   1: Evidence at protein level;
KW   ATP-binding; Iron; Iron-sulfur; Ligase; Metal-binding; Methanogenesis;
KW   Nucleotide-binding.
FT   CHAIN           1..370
FT                   /note="Ni-sirohydrochlorin a,c-diamide reductive cyclase
FT                   complex, component CfbD"
FT                   /id="PRO_0000442427"
SQ   SEQUENCE   370 AA;  40796 MW;  E22F4396BE14D019 CRC64;
     MAEKEISIIH PRPSSIVAAL YTLRDLNVDV AIMHGPPGCS FKHARLLEED GIHVVTTGLD
     ENNFVFGGHD KLVQLINKSV ELFNPKLIGI VGTCPSMIIG EEMHDAVLEA NPDVPVIEVE
     VHAGYHDNTK GVLFALESAL DAGIIDHKEF ERQKYLLEKA TEVEKKFGAA SREYLAPSRG
     DVKYKAAQRV IQLLKEGKKG LVIMNAKKET GYMFADITLA VNEVAEALGN KENLINMANI
     DPELGLPRVR QHAEYITRDL KAHGVEVHEI IGGMDEYPIA GEKVSELIKE KYSDFDFAVI
     SGVPHAIPME NIKNMELISI TNGPRQVLPL KEMGHEYVLV EIDLHPKTLG VSGIVESEFG
     ATLREVAKEA
 
 
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