ID NIFH_METMJ Reviewed; 272 AA. AC A3CWW3; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 20-MAR-2007, sequence version 1. DT 02-SEP-2026, entry version 101. DE RecName: Full=Nitrogenase iron protein {ECO:0000255|HAMAP-Rule:MF_00533}; DE EC=1.18.6.1 {ECO:0000255|HAMAP-Rule:MF_00533}; DE AltName: Full=Nitrogenase Fe protein {ECO:0000255|HAMAP-Rule:MF_00533}; DE AltName: Full=Nitrogenase component II {ECO:0000255|HAMAP-Rule:MF_00533}; DE AltName: Full=Nitrogenase reductase {ECO:0000255|HAMAP-Rule:MF_00533}; GN Name=nifH {ECO:0000255|HAMAP-Rule:MF_00533}; GN OrderedLocusNames=Memar_1937; OS Methanoculleus marisnigri (strain ATCC 35101 / DSM 1498 / JR1). OC Archaea; Methanobacteriati; Methanobacteriota; Stenosarchaea group; OC Methanomicrobia; Methanomicrobiales; Methanomicrobiaceae; Methanoculleus. OX NCBI_TaxID=368407; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=ATCC 35101 / DSM 1498 / JR1; RX PubMed=21304656; DOI=10.4056/sigs.32535; RA Anderson I.J., Sieprawska-Lupa M., Lapidus A., Nolan M., Copeland A., RA Glavina Del Rio T., Tice H., Dalin E., Barry K., Saunders E., Han C., RA Brettin T., Detter J.C., Bruce D., Mikhailova N., Pitluck S., Hauser L., RA Land M., Lucas S., Richardson P., Whitman W.B., Kyrpides N.C.; RT "Complete genome sequence of Methanoculleus marisnigri Romesser et al. 1981 RT type strain JR1."; RL Stand. Genomic Sci. 1:189-196(2009). CC -!- FUNCTION: The key enzymatic reactions in nitrogen fixation are CC catalyzed by the nitrogenase complex, which has 2 components: the iron CC protein and the molybdenum-iron protein. {ECO:0000255|HAMAP- CC Rule:MF_00533}. CC -!- CATALYTIC ACTIVITY: CC Reaction=N2 + 8 reduced [2Fe-2S]-[ferredoxin] + 16 ATP + 16 H2O = H2 + CC 8 oxidized [2Fe-2S]-[ferredoxin] + 2 NH4(+) + 16 ADP + 16 phosphate + CC 6 H(+); Xref=Rhea:RHEA:21448, Rhea:RHEA-COMP:10000, Rhea:RHEA- CC COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17997, CC ChEBI:CHEBI:18276, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:43474, CC ChEBI:CHEBI:456216; EC=1.18.6.1; Evidence={ECO:0000255|HAMAP- CC Rule:MF_00533}; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Evidence={ECO:0000255|HAMAP-Rule:MF_00533}; CC Note=Binds 1 [4Fe-4S] cluster per dimer. {ECO:0000255|HAMAP- CC Rule:MF_00533}; CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00533}. CC -!- PTM: The reversible ADP-ribosylation of Arg-98 inactivates the CC nitrogenase reductase and regulates nitrogenase activity. CC {ECO:0000255|HAMAP-Rule:MF_00533}. CC -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family. {ECO:0000255|HAMAP- CC Rule:MF_00533}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; CP000562; ABN57863.1; -; Genomic_DNA. DR RefSeq; WP_011844772.1; NC_009051.1. DR AlphaFoldDB; A3CWW3; -. DR SMR; A3CWW3; -. DR STRING; 368407.Memar_1937; -. DR GeneID; 4847172; -. DR KEGG; mem:Memar_1937; -. DR eggNOG; arCOG00590; Archaea. DR HOGENOM; CLU_059373_0_0_2; -. DR OrthoDB; 145464at2157; -. DR Proteomes; UP000002146; Chromosome. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. DR GO; GO:0016163; F:nitrogenase activity; IEA:UniProtKB-UniRule. DR CDD; cd02040; NifH; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1. DR HAMAP; MF_00533; NifH; 1. DR InterPro; IPR030655; NifH/chlL_CS. DR InterPro; IPR000392; NifH/frxC. DR InterPro; IPR005977; Nitrogenase_Fe_NifH. DR InterPro; IPR027417; P-loop_NTPase. DR NCBIfam; NF033200; F430_CfbC; 1. DR NCBIfam; TIGR01287; nifH; 1. DR PANTHER; PTHR42864; LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE IRON-SULFUR ATP-BINDING PROTEIN; 1. DR PANTHER; PTHR42864:SF2; LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE IRON-SULFUR ATP-BINDING PROTEIN; 1. DR Pfam; PF00142; Fer4_NifH; 1. DR PIRSF; PIRSF000363; Nitrogenase_iron; 1. DR PRINTS; PR00091; NITROGNASEII. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 1. DR PROSITE; PS00746; NIFH_FRXC_1; 1. DR PROSITE; PS00692; NIFH_FRXC_2; 1. DR PROSITE; PS51026; NIFH_FRXC_3; 1. PE 3: Inferred from homology; KW 4Fe-4S; ADP-ribosylation; ATP-binding; Iron; Iron-sulfur; Metal-binding; KW Nitrogen fixation; Nucleotide-binding; Oxidoreductase; Reference proteome. FT CHAIN 1..272 FT /note="Nitrogenase iron protein" FT /id="PRO_1000211875" FT BINDING 8..15 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00533" FT BINDING 95 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00533" FT BINDING 128 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="ligand shared between dimeric partners" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00533" FT MOD_RES 98 FT /note="ADP-ribosylarginine; by dinitrogenase reductase ADP- FT ribosyltransferase" FT /evidence="ECO:0000255|HAMAP-Rule:MF_00533" SQ SEQUENCE 272 AA; 29646 MW; 412E1422A02E1AD9 CRC64; MKQIALYGKG GIGKSTTAAN LSAALAGEGL DILQIGCDPK HDSTRMLMHG TWIPTVLDLI RERGDEKITV DDVVYRGFRG VRCVEAGGPE PGIGCAGRGI IATFQLLERL NALKGDVIVY DVLGDVVCGG FAMPMREGYA QEIYLVTSGE LMSIYAANNI AKAIARLSRR VRSRCTLGGV ICNAKNIEGE RELVDEFARR IGSRLIAYIP RSRIVQVAEL QKQTVVEYAP ESDQAAVYQE LARTVYGNET TSIPTPLEMD ELESFALEFV QV //