NIFH1_AZOVI
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 03-AUG-2022, entry version 153.
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; Proteobacteria; 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}.
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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 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 AlphaFoldDB; P00459; -.
DR SMR; P00459; -.
DR OMA; YVCDYYL; -.
DR BioCyc; MetaCyc:MON-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 Gene3D; 3.40.50.300; -; 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 PANTHER; PTHR42864; PTHR42864; 1.
DR Pfam; PF00142; Fer4_NifH; 1.
DR PIRSF; PIRSF000363; Nitrogenase_iron; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
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.
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
