ID   NIFD_BRASP              Reviewed;         500 AA.
AC   P06120;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   03-AUG-2022, entry version 87.
DE   RecName: Full=Nitrogenase molybdenum-iron protein alpha chain;
DE            EC=1.18.6.1;
DE   AltName: Full=Dinitrogenase;
DE   AltName: Full=Nitrogenase component I;
GN   Name=nifD;
OS   Bradyrhizobium sp. (strain ANU 289).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC   Bradyrhizobiaceae; Bradyrhizobium; unclassified Bradyrhizobium.
OX   NCBI_TaxID=186901;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=6095197; DOI=10.1093/nar/12.22.8329;
RA   Weinman J.J., Fellows F.F., Gresshoff P.M., Shine J., Scott K.F.;
RT   "Structural analysis of the genes encoding the molybdenum-iron protein of
RT   nitrogenase in the Parasponia rhizobium strain ANU289.";
RL   Nucleic Acids Res. 12:8329-8344(1984).
CC   -!- FUNCTION: This molybdenum-iron protein is part of the nitrogenase
CC       complex that catalyzes the key enzymatic reactions in nitrogen
CC       fixation.
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=[8Fe-7S] cluster; Xref=ChEBI:CHEBI:21143; Evidence={ECO:0000250};
CC       Note=Binds 1 [8Fe-7S] cluster per heterodimer. {ECO:0000250};
CC   -!- COFACTOR:
CC       Name=[7Fe-Mo-9S-C-homocitryl] cluster; Xref=ChEBI:CHEBI:30409;
CC         Evidence={ECO:0000250};
CC       Note=Binds 1 [7Fe-Mo-9S-C-homocitryl] cluster per subunit.
CC       {ECO:0000250};
CC   -!- SUBUNIT: Tetramer of two alpha and two beta chains. Forms complex with
CC       the iron protein (nitrogenase component 2).
CC   -!- SIMILARITY: Belongs to the NifD/NifK/NifE/NifN family. {ECO:0000305}.
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DR   EMBL; X01139; CAA25596.1; -; Genomic_DNA.
DR   AlphaFoldDB; P06120; -.
DR   SMR; P06120; -.
DR   PRIDE; P06120; -.
DR   GO; GO:0016612; C:molybdenum-iron nitrogenase complex; IEA:InterPro.
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:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
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   CDD; cd01976; Nitrogenase_MoFe_alpha; 1.
DR   InterPro; IPR000510; Nase/OxRdtase_comp1.
DR   InterPro; IPR010143; Nase_comp1_asu.
DR   InterPro; IPR000318; Nase_comp1_CS.
DR   InterPro; IPR005972; Nase_Mo-Fe_asu.
DR   PANTHER; PTHR43457; PTHR43457; 1.
DR   Pfam; PF00148; Oxidored_nitro; 1.
DR   TIGRFAMs; TIGR01862; N2-ase-Ialpha; 1.
DR   TIGRFAMs; TIGR01282; nifD; 1.
DR   PROSITE; PS00699; NITROGENASE_1_1; 1.
DR   PROSITE; PS00090; NITROGENASE_1_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Iron; Iron-sulfur; Metal-binding; Molybdenum;
KW   Nitrogen fixation; Nucleotide-binding; Oxidoreductase.
FT   CHAIN           1..500
FT                   /note="Nitrogenase molybdenum-iron protein alpha chain"
FT                   /id="PRO_0000153062"
FT   BINDING         67
FT                   /ligand="[8Fe-7S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21143"
FT                   /ligand_note="ligand shared with beta chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         93
FT                   /ligand="[8Fe-7S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21143"
FT                   /ligand_note="ligand shared with beta chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         159
FT                   /ligand="[8Fe-7S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21143"
FT                   /ligand_note="ligand shared with beta chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         283
FT                   /ligand="[7Fe-Mo-9S-C-homocitryl] cluster"
FT                   /ligand_id="ChEBI:CHEBI:30409"
FT                   /evidence="ECO:0000250"
FT   BINDING         451
FT                   /ligand="[7Fe-Mo-9S-C-homocitryl] cluster"
FT                   /ligand_id="ChEBI:CHEBI:30409"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   500 AA;  56142 MW;  150B438DE18B9F41 CRC64;
     MSLATTQSIA EIRARNKELI EEVLKVYPEK TAKRRAKHLN VHQAGKSDCG VKSNIKSIPG
     VMTIRGCAYA GSKGVVWGPI KDMVHISHGP VGCGQYSWGS RRNYYVGTTG VDSFVTLQFT
     SDFQEKDIVF GGDKKLIKVL DEIQELFPLN NGITIQSECP IGLIGDDIEA VSRSKSKEYG
     GKTIVPVRCE GFRGVSQSLG HHIANDAVRD WIFDKLEPEG EPKFQPTPYD VAIIGDYNIG
     GDAWSSRILL EEMGLRVIAQ WSGDGSLAEL EATPKAKLNI LHCYRSMNYI SRHMEEKFGI
     PWCEYNFFGP SKIAESLRKI AGYFDDKIKE GAERVIEKYQ PLVDAVIAKY RPRLEGKTVM
     LYVGGLRPRH VIGAYEDLGM EVVGTGYEFG HNDDYQRTAQ HYVKDSTLIY DDVNGYEFER
     FVEKVQPDLV GSGIKEKYVF QKMGVPFPEM HSWDYSGPYH GYDGFAIFAR DMDMAVNSPI
     WKKTKAPWKE AAKPKLLAAE