ID NIFH1_AZOVI Reviewed; 290 AA. AC P00459; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 2. DT 27-MAR-2024, entry version 160. DE RecName: Full=Nitrogenase iron protein 1; DE EC=1.18.6.1; DE AltName: Full=Nitrogenase Fe protein 1; DE AltName: Full=Nitrogenase component II; DE AltName: Full=Nitrogenase reductase; GN Name=nifH1; OS Azotobacter vinelandii. OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Azotobacter. OX NCBI_TaxID=354; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIMB 11614 / LMG 3878 / UW; RX PubMed=2644218; DOI=10.1128/jb.171.2.1017-1027.1989; RA Jacobson M.R., Brigle K.E., Bennett L.T., Setterquist R.A., Wilson M.S., RA Cash V.L., Beynon J., Newton W.E., Dean D.R.; RT "Physical and genetic map of the major nif gene cluster from Azotobacter RT vinelandii."; RL J. Bacteriol. 171:1017-1027(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIMB 11614 / LMG 3878 / UW; RX PubMed=3863780; DOI=10.1016/0378-1119(85)90255-0; RA Brigle K.E., Newton W.E., Dean D.R.; RT "Complete nucleotide sequence of the Azotobacter vinelandii nitrogenase RT structural gene cluster."; RL Gene 37:37-44(1985). RN [3] RP PROTEIN SEQUENCE OF 2-290. RX PubMed=6801032; DOI=10.1016/s0021-9258(18)34949-4; RA Hausinger R.P., Howard J.B.; RT "The amino acid sequence of the nitrogenase iron protein from Azotobacter RT vinelandii."; RL J. Biol. Chem. 257:2483-2490(1982). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 271-290. RC STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIMB 11614 / LMG 3878 / UW; RX PubMed=3344210; DOI=10.1093/nar/16.3.1207; RA Hiratsuka K., Roy K.L.; RT "Sequence of a 1.4 kb Eco RI fragment of Azotobacter vinelandii nif DNA."; RL Nucleic Acids Res. 16:1207-1207(1988). RN [5] RP MUTAGENESIS OF LYS-16. RC STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIMB 11614 / LMG 3878 / UW; RX PubMed=1313018; DOI=10.1016/s0021-9258(19)50480-x; RA Seefeldt L.C., Morgan T.V., Dean D.R., Mortenson L.E.; RT "Mapping the site(s) of MgATP and MgADP interaction with the nitrogenase of RT Azotobacter vinelandii. Lysine 15 of the iron protein plays a major role in RT MgATP interaction."; RL J. Biol. Chem. 267:6680-6688(1992). RN [6] RP ACTIVITY REGULATION, AND INDUCTION. RC STRAIN=CA; RX PubMed=7830548; DOI=10.1111/j.1365-2958.1994.tb01270.x; RA Moshiri F., Kim J.W., Fu C., Maier R.J.; RT "The FeSII protein of Azotobacter vinelandii is not essential for aerobic RT nitrogen fixation, but confers significant protection to oxygen-mediated RT inactivation of nitrogenase in vitro and in vivo."; RL Mol. Microbiol. 14:101-114(1994). RN [7] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS). RX PubMed=1529353; DOI=10.1126/science.1529353; RA Georgiadis M.M., Komiya H., Chakrabarti P., Woo D., Kornuc J.J., Rees D.C.; RT "Crystallographic structure of the nitrogenase iron protein from RT Azotobacter vinelandii."; RL Science 257:1653-1659(1992). RN [8] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS). RX PubMed=9163420; DOI=10.1038/387370a0; RA Schindelin H., Kisker C., Schlessman J.L., Howard J.B., Rees D.C.; RT "Structure of ADP x [AlF(4)](-)-stabilized nitrogenase complex and its RT implications for signal transduction."; RL Nature 387:370-376(1997). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). RX PubMed=9677296; DOI=10.1006/jmbi.1998.1898; RA Schlessman J.L., Woo D., Joshua-Tor L., Howard J.B., Rees D.C.; RT "Conformational variability in structures of the nitrogenase iron proteins RT from Azotobacter vinelandii and Clostridium pasteurianum."; RL J. Mol. Biol. 280:669-685(1998). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS). RX PubMed=11101289; DOI=10.1021/bi001705g; RA Jang S.B., Seefeldt L.C., Peters J.W.; RT "Insights into nucleotide signal transduction in nitrogenase: structure of RT an iron protein with MgADP bound."; RL Biochemistry 39:14745-14752(2000). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). RX PubMed=11170381; DOI=10.1021/bi0016467; RA Strop P., Takahara P.M., Chiu H., Angove H.C., Burgess B.K., Rees D.C.; RT "Crystal structure of the all-ferrous [4Fe-4S]0 form of the nitrogenase RT iron protein from Azotobacter vinelandii."; RL Biochemistry 40:651-656(2001). RN [12] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). RX PubMed=11170380; DOI=10.1021/bi001645e; RA Chiu H.-J., Peters J.W., Lanzilotta W.N., Ryle M.J., Seefeldt L.C., RA Howard J.B., Rees D.C.; RT "MgATP-bound and nucleotide-free structures of a nitrogenase protein RT complex between the Leu 127Delta-Fe-protein and the MoFe-protein."; RL Biochemistry 40:641-650(2001). CC -!- FUNCTION: The key enzymatic reactions in nitrogen fixation are CC catalyzed by the nitrogenase complex, which has 2 components: the iron CC protein (component 2) and a component 1 which is either a molybdenum- CC iron protein, a vanadium-iron, or an iron-iron protein. CC -!- CATALYTIC ACTIVITY: CC Reaction=16 ATP + 16 H2O + N2 + 8 reduced [2Fe-2S]-[ferredoxin] = 16 CC ADP + 6 H(+) + H2 + 2 NH4(+) + 8 oxidized [2Fe-2S]-[ferredoxin] + 16 CC phosphate; 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; CC -!- COFACTOR: CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; CC Note=Binds 1 [4Fe-4S] cluster per dimer.; CC -!- ACTIVITY REGULATION: Nitrogenase holoenzyme is subject to CC 'conformational protection' by FeSII; under oxidizing conditions FeSII CC binds to the holoenzyme and reversibly protects it from oxidation CC (PubMed:7830548). {ECO:0000269|PubMed:7830548}. CC -!- SUBUNIT: Homodimer. CC -!- INDUCTION: Constitutively expressed during log and stationary phase in CC sucrose-limited cultures, its levels decrease during stationary phase CC (at protein level). {ECO:0000269|PubMed:7830548}. CC -!- PTM: The reversible ADP-ribosylation of Arg-101 inactivates the CC nitrogenase reductase and regulates nitrogenase activity. CC {ECO:0000250}. CC -!- MISCELLANEOUS: This subunit is associated with the molybdenum-iron CC nitrogenase component 2. CC -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family. {ECO:0000305}. 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; M20568; AAA64709.1; -; Genomic_DNA. DR EMBL; M11579; AAA22142.1; -; Genomic_DNA. DR EMBL; X06886; CAA30003.1; -; Genomic_DNA. DR PIR; A94666; NIAVF. DR RefSeq; WP_012698831.1; NZ_FPKM01000020.1. DR PDB; 1DE0; X-ray; 2.40 A; A/B=2-290. DR PDB; 1FP6; X-ray; 2.15 A; A/B/C/D=2-290. DR PDB; 1G1M; X-ray; 2.25 A; A/B=2-290. DR PDB; 1G20; X-ray; 2.20 A; E/F/G/H=1-290. DR PDB; 1G21; X-ray; 3.00 A; E/F/G/H=1-290. DR PDB; 1G5P; X-ray; 2.20 A; A/B=2-290. DR PDB; 1M1Y; X-ray; 3.20 A; E/F/G/H/M/N/O/P=2-290. DR PDB; 1M34; X-ray; 2.30 A; E/F/G/H/M/N/O/P=2-290. DR PDB; 1N2C; X-ray; 3.00 A; E/F/G/H=2-290. DR PDB; 1NIP; X-ray; 2.90 A; A/B=2-290. DR PDB; 1RW4; X-ray; 2.50 A; A=2-273. DR PDB; 1XCP; X-ray; 3.20 A; A/B/C/D=2-290. DR PDB; 1XD8; X-ray; 2.70 A; A/B=2-290. DR PDB; 1XD9; X-ray; 2.80 A; A/B=2-290. DR PDB; 1XDB; X-ray; 2.80 A; A/B=2-290. DR PDB; 2AFH; X-ray; 2.10 A; E/F=2-290. DR PDB; 2AFI; X-ray; 3.10 A; E/F/G/H/M/N/O/P=2-290. DR PDB; 2C8V; X-ray; 2.50 A; A=2-290. DR PDB; 2NIP; X-ray; 2.20 A; A/B=2-290. DR PDB; 4WZA; X-ray; 1.90 A; E/F/G/H=2-277. DR PDB; 4WZB; X-ray; 2.30 A; E/F/G/H=2-273. DR PDB; 6N4J; X-ray; 1.95 A; A/B=2-290. DR PDB; 6N4K; X-ray; 1.76 A; A/B=2-290. DR PDB; 6N4L; X-ray; 1.13 A; A=2-290. DR PDB; 6N4M; X-ray; 1.58 A; A=2-290. DR PDB; 7T4H; X-ray; 1.51 A; A=1-290. DR PDB; 7TNE; X-ray; 1.39 A; A=1-290. DR PDB; 7TPN; X-ray; 1.38 A; A=1-290. DR PDB; 7TPO; X-ray; 1.35 A; A=1-290. DR PDB; 7TPV; X-ray; 1.49 A; A=1-290. DR PDB; 7TPW; X-ray; 1.18 A; A=1-290. DR PDB; 7TPX; X-ray; 1.35 A; A=1-290. DR PDB; 7TPY; X-ray; 1.48 A; A=1-290. DR PDB; 7TPZ; X-ray; 1.71 A; A=1-290. DR PDB; 7TQ0; X-ray; 1.81 A; A=1-290. DR PDB; 7TQ9; X-ray; 1.60 A; A=1-290. DR PDB; 7TQC; X-ray; 1.53 A; A=1-290. DR PDB; 7TQE; X-ray; 1.59 A; A=1-290. DR PDB; 7TQF; X-ray; 1.45 A; A=1-290. DR PDB; 7TQH; X-ray; 1.49 A; A=1-290. DR PDB; 7TQI; X-ray; 1.47 A; A=1-290. DR PDB; 7TQJ; X-ray; 1.48 A; A=1-290. DR PDB; 7TQK; X-ray; 1.48 A; A=1-290. DR PDB; 7UT8; EM; 2.43 A; E/F=1-290. DR PDB; 7UT9; EM; 2.44 A; E/F=1-290. DR PDB; 7UTA; EM; 2.40 A; E/F/G/H=1-290. DR PDB; 8DFC; EM; 2.48 A; E/F=1-290. DR PDB; 8DFD; EM; 2.12 A; E/F/G/H=1-290. DR PDBsum; 1DE0; -. DR PDBsum; 1FP6; -. DR PDBsum; 1G1M; -. DR PDBsum; 1G20; -. DR PDBsum; 1G21; -. DR PDBsum; 1G5P; -. DR PDBsum; 1M1Y; -. DR PDBsum; 1M34; -. DR PDBsum; 1N2C; -. DR PDBsum; 1NIP; -. DR PDBsum; 1RW4; -. DR PDBsum; 1XCP; -. DR PDBsum; 1XD8; -. DR PDBsum; 1XD9; -. DR PDBsum; 1XDB; -. DR PDBsum; 2AFH; -. DR PDBsum; 2AFI; -. DR PDBsum; 2C8V; -. DR PDBsum; 2NIP; -. DR PDBsum; 4WZA; -. DR PDBsum; 4WZB; -. DR PDBsum; 6N4J; -. DR PDBsum; 6N4K; -. DR PDBsum; 6N4L; -. DR PDBsum; 6N4M; -. DR PDBsum; 7T4H; -. DR PDBsum; 7TNE; -. DR PDBsum; 7TPN; -. DR PDBsum; 7TPO; -. DR PDBsum; 7TPV; -. DR PDBsum; 7TPW; -. DR PDBsum; 7TPX; -. DR PDBsum; 7TPY; -. DR PDBsum; 7TPZ; -. DR PDBsum; 7TQ0; -. DR PDBsum; 7TQ9; -. DR PDBsum; 7TQC; -. DR PDBsum; 7TQE; -. DR PDBsum; 7TQF; -. DR PDBsum; 7TQH; -. DR PDBsum; 7TQI; -. DR PDBsum; 7TQJ; -. DR PDBsum; 7TQK; -. DR PDBsum; 7UT8; -. DR PDBsum; 7UT9; -. DR PDBsum; 7UTA; -. DR PDBsum; 8DFC; -. DR PDBsum; 8DFD; -. DR AlphaFoldDB; P00459; -. DR EMDB; EMD-27404; -. DR EMDB; EMD-27405; -. DR SMR; P00459; -. DR OMA; VIYKGYG; -. DR BioCyc; MetaCyc:MONOMER-19495; -. DR BRENDA; 1.18.6.1; 49. DR EvolutionaryTrace; P00459; -. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule. 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; IMP:CACAO. DR GO; GO:0009399; P:nitrogen fixation; 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; 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 1: Evidence at protein level; KW 3D-structure; 4Fe-4S; ADP-ribosylation; ATP-binding; KW Direct protein sequencing; Iron; Iron-sulfur; Metal-binding; KW Nitrogen fixation; Nucleotide-binding; Oxidoreductase. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000269|PubMed:6801032" FT CHAIN 2..290 FT /note="Nitrogenase iron protein 1" FT /id="PRO_0000139490" FT BINDING 10..17 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT BINDING 98 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="ligand shared between dimeric partners" FT BINDING 133 FT /ligand="[4Fe-4S] cluster" FT /ligand_id="ChEBI:CHEBI:49883" FT /ligand_note="ligand shared between dimeric partners" FT MOD_RES 101 FT /note="ADP-ribosylarginine; by dinitrogenase reductase ADP- FT ribosyltransferase" FT /evidence="ECO:0000250" FT MUTAGEN 16 FT /note="K->Q,P: Loss of nitrogen fixation." FT /evidence="ECO:0000269|PubMed:1313018" FT CONFLICT 145 FT /note="A -> P (in Ref. 2; AAA22142)" FT /evidence="ECO:0000305" FT STRAND 4..9 FT /evidence="ECO:0007829|PDB:6N4L" FT HELIX 12..14 FT /evidence="ECO:0007829|PDB:1G20" FT HELIX 16..29 FT /evidence="ECO:0007829|PDB:6N4L" FT STRAND 34..40 FT /evidence="ECO:0007829|PDB:6N4L" FT STRAND 41..43 FT /evidence="ECO:0007829|PDB:2AFH" FT TURN 44..46 FT /evidence="ECO:0007829|PDB:1XCP" FT HELIX 47..50 FT /evidence="ECO:0007829|PDB:6N4L" FT STRAND 51..53 FT /evidence="ECO:0007829|PDB:4WZA" FT HELIX 58..65 FT /evidence="ECO:0007829|PDB:6N4L" FT HELIX 68..70 FT /evidence="ECO:0007829|PDB:6N4L" FT HELIX 73..76 FT /evidence="ECO:0007829|PDB:6N4L" FT STRAND 77..80 FT /evidence="ECO:0007829|PDB:1XD8" FT HELIX 81..83 FT /evidence="ECO:0007829|PDB:6N4L" FT STRAND 85..88 FT /evidence="ECO:0007829|PDB:6N4L" FT TURN 94..96 FT /evidence="ECO:0007829|PDB:6N4K" FT HELIX 101..112 FT /evidence="ECO:0007829|PDB:6N4L" FT TURN 113..117 FT /evidence="ECO:0007829|PDB:6N4K" FT STRAND 122..127 FT /evidence="ECO:0007829|PDB:6N4L" FT HELIX 129..131 FT /evidence="ECO:0007829|PDB:1NIP" FT HELIX 134..141 FT /evidence="ECO:0007829|PDB:6N4L" FT STRAND 146..152 FT /evidence="ECO:0007829|PDB:6N4L" FT HELIX 156..171 FT /evidence="ECO:0007829|PDB:6N4L" FT TURN 172..174 FT /evidence="ECO:0007829|PDB:6N4L" FT STRAND 179..186 FT /evidence="ECO:0007829|PDB:6N4L" FT STRAND 188..190 FT /evidence="ECO:0007829|PDB:1RW4" FT HELIX 193..204 FT /evidence="ECO:0007829|PDB:6N4L" FT STRAND 208..212 FT /evidence="ECO:0007829|PDB:6N4L" FT HELIX 217..223 FT /evidence="ECO:0007829|PDB:6N4L" FT HELIX 228..231 FT /evidence="ECO:0007829|PDB:6N4L" FT STRAND 233..235 FT /evidence="ECO:0007829|PDB:1XDB" FT HELIX 236..250 FT /evidence="ECO:0007829|PDB:6N4L" FT HELIX 262..271 FT /evidence="ECO:0007829|PDB:6N4L" FT TURN 272..276 FT /evidence="ECO:0007829|PDB:6N4L" FT HELIX 280..282 FT /evidence="ECO:0007829|PDB:2AFH" FT HELIX 287..289 FT /evidence="ECO:0007829|PDB:6N4J" SQ SEQUENCE 290 AA; 31516 MW; C36EFC0D9A27F64D CRC64; MAMRQCAIYG KGGIGKSTTT QNLVAALAEM GKKVMIVGCD PKADSTRLIL HSKAQNTIME MAAEAGTVED LELEDVLKAG YGGVKCVESG GPEPGVGCAG RGVITAINFL EEEGAYEDDL DFVFYDVLGD VVCGGFAMPI RENKAQEIYI VCSGEMMAMY AANNISKGIV KYANSGSVRL GGLICNSRNT DREDELIIAL ANKLGTQMIH FVPRDNVVQR AEIRRMTVIE YDPKAKQADE YRALARKVVD NKLLVIPNPI TMDELEELLM EFGIMEVEDE SIVGKTAEEV //