ID   NIFD_METMI              Reviewed;         477 AA.
AC   P0CW50; P71526;
DT   03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT   03-MAY-2011, sequence version 1.
DT   03-AUG-2022, entry version 29.
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   Methanococcus maripaludis (Methanococcus deltae).
OC   Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC   Methanococcaceae; Methanococcus.
OX   NCBI_TaxID=39152;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 43000 / DSM 2067 / JCM 10722 / JJ;
RX   PubMed=8990309; DOI=10.1128/jb.179.2.541-543.1997;
RA   Kessler P.S., McLarnan J., Leigh J.A.;
RT   "Nitrogenase phylogeny and the molybdenum dependence of nitrogen fixation
RT   in Methanococcus maripaludis.";
RL   J. Bacteriol. 179:541-543(1997).
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; U75887; AAC45515.1; -; Genomic_DNA.
DR   PIR; T10093; T10093.
DR   AlphaFoldDB; P0CW50; -.
DR   SMR; P0CW50; -.
DR   DIP; DIP-61201N; -.
DR   IntAct; P0CW50; 3.
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   InterPro; IPR000510; Nase/OxRdtase_comp1.
DR   InterPro; IPR005974; Nase_asu.
DR   InterPro; IPR010143; Nase_comp1_asu.
DR   InterPro; IPR000318; Nase_comp1_CS.
DR   PANTHER; PTHR43457; PTHR43457; 1.
DR   Pfam; PF00148; Oxidored_nitro; 1.
DR   TIGRFAMs; TIGR01284; alt_nitrog_alph; 1.
DR   TIGRFAMs; TIGR01862; N2-ase-Ialpha; 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..477
FT                   /note="Nitrogenase molybdenum-iron protein alpha chain"
FT                   /id="PRO_0000153072"
FT   BINDING         49
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         75
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         149
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         267
FT                   /ligand="[7Fe-Mo-9S-C-homocitryl] cluster"
FT                   /ligand_id="ChEBI:CHEBI:30409"
FT                   /evidence="ECO:0000250"
FT   BINDING         433
FT                   /ligand="[7Fe-Mo-9S-C-homocitryl] cluster"
FT                   /ligand_id="ChEBI:CHEBI:30409"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   477 AA;  53314 MW;  B069080E6867A1FD CRC64;
     MPFCLLDVDK DIPEREQHIY IKDSKEPKGH CKQRCNTNTI PGSMTERGCA FAGVKGVITG
     AIKDVLHVVH SPVGCTAYGN GTTKRYPTRP EMPDGSVFPV ENFNLKHIVG TDLTESDVVF
     GGMNKLKKVI REASKEFPFV NAIYVYATCT TGLIGDDLDA VCKEMQAELG KDVVAFNAPG
     FAGPTQSKGH HVGNYTIFEN LVGTKEPPKT TDYDINLIGE YNIDGDYWVL EKYFEDMGIN
     VLSKFTGDAT HGELCWMHKA KLSLVRCQRS ATYVAKLIEE KYGVPYLKVD FFGPEYCAEN
     LRAVGKYFGK EIEAEAVIQK EMEKIQPELD FYQSKLQGKK IWISAGGPKS WHLSKPIEQY
     LGMDVVALSG LFEHEDGYEK MQERAKDGTI IIDDPNTLEM EEVVEKYQPE IVLGGIKEKY
     FFHKLGVPSV MIHSYENGPY IGFGGFVNMA RDIFTAIYNP AWKLMGFGEG EPGDSNE