ID   CFBD_METAC              Reviewed;         370 AA.
AC   Q8TJZ8;
DT   22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2002, sequence version 1.
DT   03-AUG-2022, entry version 92.
DE   RecName: Full=Ni-sirohydrochlorin a,c-diamide reductive cyclase complex, component CfbD {ECO:0000303|PubMed:27846569};
DE            EC=6.3.3.7 {ECO:0000269|PubMed:27846569};
DE   AltName: Full=NifD homolog component CfbD {ECO:0000303|PubMed:27846569};
GN   Name=cfbD {ECO:0000303|PubMed:27846569}; Synonyms=nifD;
GN   OrderedLocusNames=MA_3628 {ECO:0000312|EMBL:AAM06983.1};
OS   Methanosarcina acetivorans (strain ATCC 35395 / DSM 2834 / JCM 12185 /
OS   C2A).
OC   Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC   Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX   NCBI_TaxID=188937;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A
RC   {ECO:0000312|Proteomes:UP000002487};
RX   PubMed=11932238; DOI=10.1101/gr.223902;
RA   Galagan J.E., Nusbaum C., Roy A., Endrizzi M.G., Macdonald P., FitzHugh W.,
RA   Calvo S., Engels R., Smirnov S., Atnoor D., Brown A., Allen N., Naylor J.,
RA   Stange-Thomann N., DeArellano K., Johnson R., Linton L., McEwan P.,
RA   McKernan K., Talamas J., Tirrell A., Ye W., Zimmer A., Barber R.D.,
RA   Cann I., Graham D.E., Grahame D.A., Guss A.M., Hedderich R.,
RA   Ingram-Smith C., Kuettner H.C., Krzycki J.A., Leigh J.A., Li W., Liu J.,
RA   Mukhopadhyay B., Reeve J.N., Smith K., Springer T.A., Umayam L.A.,
RA   White O., White R.H., de Macario E.C., Ferry J.G., Jarrell K.F., Jing H.,
RA   Macario A.J.L., Paulsen I.T., Pritchett M., Sowers K.R., Swanson R.V.,
RA   Zinder S.H., Lander E., Metcalf W.W., Birren B.;
RT   "The genome of Methanosarcina acetivorans reveals extensive metabolic and
RT   physiological diversity.";
RL   Genome Res. 12:532-542(2002).
RN   [2]
RP   FUNCTION, CATALYTIC ACTIVITY, AND SUBUNIT.
RC   STRAIN=ATCC 35395 / DSM 2834 / JCM 12185 / C2A;
RX   PubMed=27846569; DOI=10.1126/science.aag2947;
RA   Zheng K., Ngo P.D., Owens V.L., Yang X.P., Mansoorabadi S.O.;
RT   "The biosynthetic pathway of coenzyme F430 in methanogenic and
RT   methanotrophic archaea.";
RL   Science 354:339-342(2016).
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:27846569}.
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:27846569};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000250|UniProtKB:Q46FL2};
CC   -!- SUBUNIT: Homodimer or monomer (By similarity). The Ni-sirohydrochlorin
CC       a,c-diamide reductive cyclase complex is composed of a NifH homolog
CC       component CfbC and a NifD homolog component CfbD (PubMed:27846569).
CC       {ECO:0000250|UniProtKB:Q46FL2, ECO:0000269|PubMed:27846569}.
CC   -!- SIMILARITY: Belongs to the NifD/NifK/NifE/NifN family. {ECO:0000305}.
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DR   EMBL; AE010299; AAM06983.1; -; Genomic_DNA.
DR   RefSeq; WP_011023536.1; NC_003552.1.
DR   AlphaFoldDB; Q8TJZ8; -.
DR   SMR; Q8TJZ8; -.
DR   STRING; 188937.MA_3628; -.
DR   DNASU; 1475521; -.
DR   EnsemblBacteria; AAM06983; AAM06983; MA_3628.
DR   GeneID; 1475521; -.
DR   KEGG; mac:MA_3628; -.
DR   HOGENOM; CLU_782144_0_0_2; -.
DR   InParanoid; Q8TJZ8; -.
DR   OMA; CASMIIG; -.
DR   OrthoDB; 56870at2157; -.
DR   PhylomeDB; Q8TJZ8; -.
DR   BioCyc; MetaCyc:MON-20116; -.
DR   Proteomes; UP000002487; 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   1: Evidence at protein level;
KW   ATP-binding; Iron; Iron-sulfur; Ligase; Metal-binding; Methanogenesis;
KW   Nucleotide-binding; Reference proteome.
FT   CHAIN           1..370
FT                   /note="Ni-sirohydrochlorin a,c-diamide reductive cyclase
FT                   complex, component CfbD"
FT                   /id="PRO_0000442426"
SQ   SEQUENCE   370 AA;  40917 MW;  CF9D54C5D3E6EAB3 CRC64;
     MTQKEISIIH PRPSSIVAAL YTLRDLNVDV AILHGPPGCS FKHARLLEED GIHVVTTGLD
     ENGFVFGGHD RLVEVINKSI ELFNPKILGV VGTCASMIIG EEMHDAVLEA NPDIPVIEVE
     VHAGYHNNTR GVLFALESAL DAGIIDRKEF ERQEYLLIKA TEVEKRFGAA SKEYLAPSRG
     DLKYKVAKRL IELLKEGKKG LVIMNAKKET GYMFADITLA VSEVAAALGK KENLVNMANI
     DPELGLPRVR QHAQYIMRDF IAHGVEIHEI IGGMDEYPIA GEKVSELIKE KYSDYDFAVI
     TGVPHAIPME NLQHMELISI TNGPRQVLPL KEMGHEHVLV EIDLHPKTLG VSEIVESEFG
     ATLREVAKEA