ID   NIFD_RHICP              Reviewed;         500 AA.
AC   P06769;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-JAN-1988, sequence version 1.
DT   13-SEP-2023, entry version 97.
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   Rhizobium sp. cowpea (strain IRc78).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX   NCBI_TaxID=400;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=16578778; DOI=10.1073/pnas.81.23.7358;
RA   Yun A.C., Szalay A.A.;
RT   "Structural genes of dinitrogenase and dinitrogenase reductase are
RT   transcribed from two separate promoters in the broad host range cowpea
RT   Rhizobium strain IRc78.";
RL   Proc. Natl. Acad. Sci. U.S.A. 81:7358-7362(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; M10203; AAA26308.1; -; Genomic_DNA.
DR   AlphaFoldDB; P06769; -.
DR   SMR; P06769; -.
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   Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 3.
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   NCBIfam; TIGR01862; N2-ase-Ialpha; 1.
DR   NCBIfam; TIGR01282; nifD; 1.
DR   PANTHER; PTHR43457; NITROGENASE MOLYBDENUM-IRON PROTEIN ALPHA CHAIN; 1.
DR   PANTHER; PTHR43457:SF1; NITROGENASE MOLYBDENUM-IRON PROTEIN ALPHA CHAIN; 1.
DR   Pfam; PF00148; Oxidored_nitro; 1.
DR   SUPFAM; SSF53807; Helical backbone' metal receptor; 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_0000153078"
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;  56136 MW;  5F7FA8DDE2174CDF CRC64;
     MSLASTQSIA EIRARNKELI QEVLKVYPEK TAKRRAKHLN VHQAGKSDCG VKSNIKSIPG
     VMTIRGCAYA GSKGVVWGPI KDMVHISHGP VGCGQYSWGS RRNYYVGTTG IDSFVTLQFT
     FDFREKDIVF GGDKKLVKIL DEIQELFPLN NGITIQSECP IGLIGDDIEA VSRAKSKEYG
     GKTIVPVRCE GFRGVSQSLG HHIANDAVRD WIFDQVEADG KPKVEPTPYD VAIIGDYNIG
     GDAWSSRILL EEMGLRVIAQ WSGDGSLAEL EANVEGKLNI LHCYRSMNYI SRHMEEKFGI
     PWCEYNFFGP SKIAESLRRI AGYFDDKIKE GAERVIEKYQ PLVNAVIAKY RPRLEGKTVM
     LYVGGLRSRH VIGAYEDLGM EVIGTGYEFG HNDDYQRTAQ HYVKDGTLIH DDVNGYEFER
     FVEKLQPDLV GSGIKEKYVF QKMGGPFRQM HSWDYSGPYH GYDGFAIFAR DMDMAINSPV
     WKKTKAPWKE ASRAKLLAAE
//