CFBC_METAC
ID CFBC_METAC Reviewed; 265 AA.
AC Q8TJZ9;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2002, sequence version 1.
DT 03-AUG-2022, entry version 126.
DE RecName: Full=Ni-sirohydrochlorin a,c-diamide reductive cyclase complex, component CfbC {ECO:0000303|PubMed:27846569};
DE EC=6.3.3.7 {ECO:0000269|PubMed:27846569};
DE AltName: Full=NifH homolog component CfbC {ECO:0000303|PubMed:27846569};
GN Name=cfbC {ECO:0000303|PubMed:27846569};
GN Synonyms=nifH {ECO:0000312|EMBL:AAM06982.1};
GN OrderedLocusNames=MA_3627 {ECO:0000312|EMBL:AAM06982.1};
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:Q46FL1};
CC -!- SUBUNIT: Homodimer (By similarity). 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 (PubMed:27846569).
CC {ECO:0000250|UniProtKB:Q46FL1, ECO:0000269|PubMed:27846569}.
CC -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family. {ECO:0000305}.
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DR EMBL; AE010299; AAM06982.1; -; Genomic_DNA.
DR RefSeq; WP_011023535.1; NC_003552.1.
DR AlphaFoldDB; Q8TJZ9; -.
DR SMR; Q8TJZ9; -.
DR STRING; 188937.MA_3627; -.
DR EnsemblBacteria; AAM06982; AAM06982; MA_3627.
DR GeneID; 1475520; -.
DR KEGG; mac:MA_3627; -.
DR HOGENOM; CLU_059373_0_0_2; -.
DR OMA; YVCDYYL; -.
DR OrthoDB; 66372at2157; -.
DR PhylomeDB; Q8TJZ9; -.
DR BioCyc; MetaCyc:MON-20115; -.
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 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; Reference proteome.
FT CHAIN 1..265
FT /note="Ni-sirohydrochlorin a,c-diamide reductive cyclase
FT complex, component CfbC"
FT /id="PRO_0000442424"
SQ SEQUENCE 265 AA; 28610 MW; DA78B9AF07A2D0DB CRC64;
MKKQKIVAIY GKGGIGKSST ASNVAAACAE AGKKVMIIGC DPKSDSSITL LRGKRIPTIL
DLLREGVDVQ EKDVVFEGYA GVKCVEAGGP EPGIGCAGRG IIVAIQKLKS ISGDLLKEQD
LIIYDVPGDI VCGGFVAPVR KGYVNEAYVL TSGEYMPLYA ANNICKGLSK IGMPLSGVIC
NSRNASREEE IVRKFSEEIG SQLMAFIPKR QIVQDCEREG YSVMEKAPDS DIAEVYRQLG
KSILTNEKKV MASHLSDERL REMTK
