ID Q32ZM9_9BURK Unreviewed; 219 AA. AC Q32ZM9; DT 06-DEC-2005, integrated into UniProtKB/TrEMBL. DT 06-DEC-2005, sequence version 1. DT 16-OCT-2019, entry version 46. DE SubName: Full=NifH {ECO:0000313|EMBL:AAT06095.1}; DE Flags: Fragment; GN Name=nifH {ECO:0000313|EMBL:AAT06095.1}; OS Burkholderia sp. Br3469. OC Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales; OC Burkholderiaceae; Burkholderia. OX NCBI_TaxID=273252 {ECO:0000313|EMBL:AAT06095.1}; RN [1] {ECO:0000313|EMBL:AAT06095.1} RP NUCLEOTIDE SEQUENCE. RC STRAIN=BR3469 {ECO:0000313|EMBL:AAT06095.1}; RX PubMed=16269788; DOI=10.1128/AEM.71.11.7461-7471.2005; RA Chen W.M., de Faria S.M., Straliotto R., Pitard R.M., RA Simoes-Araujo J.L., Chou J.H., Chou Y.J., Barrios E., Prescott A.R., RA Elliott G.N., Sprent J.I., Young J.P., James E.K.; RT "Proof that Burkholderia strains form effective symbioses with RT legumes: a study of novel Mimosa-nodulating strains from South RT America."; RL Appl. Environ. Microbiol. 71:7461-7471(2005). 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; AY533868; AAT06095.1; -; 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:UniProtKB-KW. 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 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}; 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 Nucleotide-binding {ECO:0000256|RuleBase:RU003688}; KW Oxidoreductase {ECO:0000256|RuleBase:RU003688}. FT MOD_RES 91 91 ADP-ribosylarginine; by dinitrogenase FT reductase ADP-ribosyltransferase. FT {ECO:0000256|PIRSR:PIRSR605977-50}. FT NON_TER 1 1 {ECO:0000313|EMBL:AAT06095.1}. FT NON_TER 219 219 {ECO:0000313|EMBL:AAT06095.1}. SQ SEQUENCE 219 AA; 23370 MW; BB4797A7391FBF65 CRC64; KGGIGKSTTS QNTLAALSDL GQKILIVGCD PKADSTRLIL HAKAQDTILS LAAEAGSVED LELDDVMKIG YKEIRCVESG GPEPGVGCAG RGVITSINFL EENGAYDGVD YVSYDVLGDV VCGGFAMPIR ENKAQEIYIV MSGEMMAMYA ANNISKGILK YANSGGVRLG GLICNERKTD KELELAESLA TMLGTRLIHF VPRDNIVQHA ELRRMTVIG //