ID NIFH1_AZOVI STANDARD; PRT; 289 AA. AC P00459; DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot. DT 21-JUL-1986, sequence version 1. DT 17-OCT-2006, entry version 70. DE Nitrogenase iron protein 1 (EC 1.18.6.1) (Nitrogenase component II) DE (Nitrogenase Fe protein 1) (Nitrogenase reductase). GN Name=nifH1; OS Azotobacter vinelandii. OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales; OC Pseudomonadaceae; Azotobacter. OX NCBI_TaxID=354; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=89123097; PubMed=2644218; RA Jacobson M.R., Brigle K.E., Bennett L.T., Setterquist R.A., RA Wilson M.S., Cash V.L., Beynon J., Newton W.E., Dean D.R.; RT "Physical and genetic map of the major nif gene cluster from RT Azotobacter vinelandii."; RL J. Bacteriol. 171:1017-1027(1989). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=86031364; 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 RT nitrogenase structural gene cluster."; RL Gene 37:37-44(1985). RN [3] RP PROTEIN SEQUENCE. RX MEDLINE=82142349; PubMed=6801032; RA Hausinger R.P., Howard J.B.; RT "The amino acid sequence of the nitrogenase iron protein from RT Azotobacter vinelandii."; RL J. Biol. Chem. 257:2483-2490(1982). RN [4] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 270-289. RC STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIB 11614 / LMG 3878 / UW; RX MEDLINE=88144000; PubMed=3344210; RA Hiratsuka K., Roy K.L.; RT "Sequence of a 1.4 kb Eco RI fragment of Azotobacter vinelandii nif RT DNA."; RL Nucleic Acids Res. 16:1207-1207(1988). RN [5] RP MUTAGENESIS OF LYS-15. RX MEDLINE=92202214; PubMed=1313018; 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 RT nitrogenase of Azotobacter vinelandii. Lysine 15 of the iron protein RT plays a major role in MgATP interaction."; RL J. Biol. Chem. 267:6680-6688(1992). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS). RX MEDLINE=92410322; PubMed=1529353; RA Georgiadis M.M., Komiya H., Chakrabarti P., Woo D., Kornuc J.J., RA Rees D.C.; RT "Crystallographic structure of the nitrogenase iron protein from RT Azotobacter vinelandii."; RL Science 257:1653-1659(1992). RN [7] RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS). RX MEDLINE=97305952; 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 [8] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). RX MEDLINE=98344106; 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 RT proteins from Azotobacter vinelandii and Clostridium pasteurianum."; RL J. Mol. Biol. 280:669-685(1998). RN [9] RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS). RX MEDLINE=20552920; PubMed=11101289; DOI=10.1021/bi001705g; RA Jang S.B., Seefeldt L.C., Peters J.W.; RT "Insights into nucleotide signal transduction in nitrogenase: RT structure of an iron protein with MgADP bound."; RL Biochemistry 39:14745-14752(2000). RN [10] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). RX MEDLINE=21093029; PubMed=11170381; DOI=10.1021/bi0016467; RA Strop P., Takahara P.M., Chiu H., Angove H.C., Burgess B.K., RA Rees D.C.; RT "Crystal structure of the all-ferrous [4Fe-4S]0 form of the RT nitrogenase iron protein from Azotobacter vinelandii."; RL Biochemistry 40:651-656(2001). RN [11] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS). RX MEDLINE=21093028; 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 CC iron protein (component 2) and a component 1 which is either a CC molybdenum-iron protein, a vanadium-iron, or an iron-iron protein. CC -!- CATALYTIC ACTIVITY: 8 reduced ferredoxin + 8 H(+) + N(2) + 16 ATP CC + 16 H(2)O = 8 oxidized ferredoxin + H(2) + 2 NH(3) + 16 ADP + 16 CC phosphate. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per dimer. CC -!- SUBUNIT: Homodimer. CC -!- MISCELLANEOUS: This subunit is associated with the molybdenum-iron CC nitrogenase component 2. CC -!- SIMILARITY: Belongs to the nifH/bchL/chlL family. 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 PDB; 1DE0; X-ray; A/B=1-289. DR PDB; 1FP6; X-ray; A/B/C/D=1-289. DR PDB; 1G1M; X-ray; A/B=1-289. DR PDB; 1G20; X-ray; E/F/G/H=1-289. DR PDB; 1G21; X-ray; E/F/G/H=1-289. DR PDB; 1G5P; X-ray; A/B=1-289. DR PDB; 1M1Y; X-ray; E/F/G/H/M/N/O/P=1-289. DR PDB; 1M34; X-ray; E/F/G/H/M/N/O/P=1-289. DR PDB; 1N2C; X-ray; E/F/G/H=1-289. DR PDB; 1NIP; X-ray; A/B=1-289. DR PDB; 1RW4; X-ray; A=1-272. DR PDB; 1XCP; X-ray; A/B/C/D=1-289. DR PDB; 1XD8; X-ray; A/B=1-289. DR PDB; 1XD9; X-ray; A/B=1-289. DR PDB; 1XDB; X-ray; A/B=1-289. DR PDB; 2C8V; X-ray; A=1-289. DR PDB; 2NIP; X-ray; A/B=1-289. DR LinkHub; P00459; -. DR HAMAP; MF_00533; -; 1. DR InterPro; IPR005977; NifH. DR InterPro; IPR000392; NitrogenaseII. DR Pfam; PF00142; Fer4_NifH; 1. DR PIRSF; PIRSF000363; Nitrogenase_iron; 1. DR PRINTS; PR00091; NITROGNASEII. DR TIGRFAMs; TIGR01287; nifH; 1. DR PROSITE; PS00746; NIFH_FRXC_1; 1. DR PROSITE; PS00692; NIFH_FRXC_2; 1. DR PROSITE; PS51026; NIFH_FRXC_3; 1. KW 3D-structure; 4Fe-4S; ATP-binding; Direct protein sequencing; Iron; KW Iron-sulfur; Metal-binding; Nitrogen fixation; Nucleotide-binding; KW Oxidoreductase. FT INIT_MET 0 0 FT CHAIN 1 289 Nitrogenase iron protein 1. FT /FTId=PRO_0000139490. FT NP_BIND 9 16 ATP. FT METAL 97 97 Iron-sulfur (4Fe-4S) (shared with dimeric FT partner). FT METAL 132 132 Iron-sulfur (4Fe-4S) (shared with dimeric FT partner). FT MUTAGEN 15 15 K->Q,P: Loss of nitrogen fixation. FT CONFLICT 144 144 A -> P (in Ref. 2). FT STRAND 3 10 FT TURN 11 12 FT HELIX 15 28 FT TURN 29 30 FT STRAND 33 41 FT HELIX 46 49 FT TURN 50 50 FT STRAND 51 53 FT HELIX 57 64 FT HELIX 67 69 FT HELIX 72 75 FT HELIX 80 82 FT STRAND 84 87 FT TURN 93 94 FT TURN 98 99 FT HELIX 100 111 FT TURN 112 113 FT HELIX 114 116 FT STRAND 120 127 FT TURN 134 136 FT HELIX 137 140 FT TURN 141 142 FT STRAND 145 151 FT HELIX 155 170 FT TURN 171 174 FT STRAND 178 185 FT TURN 190 191 FT HELIX 192 203 FT TURN 204 204 FT STRAND 207 211 FT TURN 215 215 FT HELIX 216 221 FT TURN 222 224 FT HELIX 227 230 FT TURN 232 233 FT HELIX 235 249 FT HELIX 261 270 FT TURN 271 272 FT TURN 279 280 FT TURN 282 283 FT TURN 286 288 SQ SEQUENCE 289 AA; 31385 MW; B84738B2C82DA078 CRC64; AMRQCAIYGK GGIGKSTTTQ NLVAALAEMG KKVMIVGCDP KADSTRLILH SKAQNTIMEM AAEAGTVEDL ELEDVLKAGY GGVKCVESGG PEPGVGCAGR GVITAINFLE EEGAYEDDLD FVFYDVLGDV VCGGFAMPIR ENKAQEIYIV CSGEMMAMYA ANNISKGIVK YANSGSVRLG GLICNSRNTD REDELIIALA NKLGTQMIHF VPRDNVVQRA EIRRMTVIEY DPKAKQADEY RALARKVVDN KLLVIPNPIT MDELEELLME FGIMEVEDES IVGKTAEEV //