ID Q6JT58_9BACT Unreviewed; 105 AA. AC Q6JT58; DT 05-JUL-2004, integrated into UniProtKB/TrEMBL. DT 05-JUL-2004, sequence version 1. DT 18-SEP-2019, entry version 48. DE RecName: Full=Nitrogenase {ECO:0000256|SAAS:SAAS01203839}; DE EC=1.18.6.1 {ECO:0000256|SAAS:SAAS01203839}; DE Flags: Fragment; GN Name=nifH {ECO:0000313|EMBL:AAQ76952.1}; OS uncultured bacterium. OC Bacteria; environmental samples. OX NCBI_TaxID=77133 {ECO:0000313|EMBL:AAQ76952.1}; RN [1] {ECO:0000313|EMBL:AAQ76952.1} RP NUCLEOTIDE SEQUENCE. RA Schultz L.C., Zwolinski M.D., Miller B.M., Nold S.C.; RT "Community composition of methane-oxidizing bacteria in northern RT peatlands."; RL Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases. CC -!- CATALYTIC ACTIVITY: CC Reaction=16 ATP + 16 H2O + N2 + 8 reduced [2Fe-2S]-[ferredoxin] = CC 16 ADP + 6 H(+) + H2 + 2 NH4(+) + 8 oxidized [2Fe-2S]- CC [ferredoxin] + 16 phosphate; Xref=Rhea:RHEA:21448, Rhea:RHEA- CC COMP:10000, Rhea:RHEA-COMP:10001, ChEBI:CHEBI:15377, CC ChEBI:CHEBI:15378, ChEBI:CHEBI:17997, ChEBI:CHEBI:18276, CC ChEBI:CHEBI:28938, ChEBI:CHEBI:30616, ChEBI:CHEBI:33737, CC ChEBI:CHEBI:33738, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; CC EC=1.18.6.1; Evidence={ECO:0000256|SAAS:SAAS01203838}; CC -!- PTM: The reversible ADP-ribosylation of Arg inactivates the CC nitrogenase reductase and regulates nitrogenase activity. CC {ECO:0000256|PIRSR:PIRSR605977-50}. CC -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family. CC {ECO:0000256|RuleBase:RU003688}. 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; AY309214; AAQ76952.1; -; Genomic_DNA. DR GO; GO:0016612; C:molybdenum-iron nitrogenase complex; IEA:InterPro. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0018697; F:carbonyl sulfide nitrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0016163; F:nitrogenase activity; IEA:UniProtKB-EC. DR GO; GO:0009399; P:nitrogen fixation; IEA:InterPro. DR CDD; cd02040; 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 PANTHER; PTHR42864; PTHR42864; 1. DR Pfam; PF00142; Fer4_NifH; 1. DR SUPFAM; SSF52540; SSF52540; 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 {ECO:0000256|RuleBase:RU003688, ECO:0000256|SAAS:SAAS01203841}; KW ADP-ribosylation {ECO:0000256|PIRSR:PIRSR605977-50}; KW ATP-binding {ECO:0000256|RuleBase:RU003688}; KW Iron {ECO:0000256|RuleBase:RU003688}; KW Iron-sulfur {ECO:0000256|RuleBase:RU003688}; KW Metal-binding {ECO:0000256|RuleBase:RU003688}; KW Nitrogen fixation {ECO:0000256|SAAS:SAAS01203845}; KW Nucleotide-binding {ECO:0000256|RuleBase:RU003688}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003688, KW ECO:0000256|SAAS:SAAS01203840}. FT MOD_RES 62 62 ADP-ribosylarginine; by dinitrogenase FT reductase ADP-ribosyltransferase. FT {ECO:0000256|PIRSR:PIRSR605977-50}. FT NON_TER 1 1 {ECO:0000313|EMBL:AAQ76952.1}. FT NON_TER 105 105 {ECO:0000313|EMBL:AAQ76952.1}. SQ SEQUENCE 105 AA; 11067 MW; EA8A5AA38D91AEB0 CRC64; DPKADSTRLI LHSKAQDTVL SLAAAAGSVE DLEIEDVMKV GYLDIRCVES GGPEPGVGCA GRGVITSINF LEENGAYEDT DYVSYDVLGD VVCGGFAMPI RENKA //