ID   NIFD_AZOBR              Reviewed;         482 AA.
AC   P25313;
DT   01-MAY-1992, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1992, sequence version 1.
DT   03-APR-2013, entry version 68.
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   Azospirillum brasilense.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Azospirillum.
OX   NCBI_TaxID=192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1823284;
RA   Passaglia L.M.P., Nunes C.P., Zaha A., Schrank I.S.;
RT   "The nifHDK operon in the free-living nitrogen-fixing bacteria
RT   Azospirillum brasilense sequentially comprises genes H, D, K, an 353
RT   bp orf and gene Y.";
RL   Braz. J. Med. Biol. Res. 24:649-675(1991).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-28.
RC   STRAIN=ATCC 29145 / Sp7 / DSM 1690 / IMET 11303;
RX   PubMed=2608030;
RA   de Zamaroczy M., Delorme F., Elmerich C.;
RT   "Regulation of transcription and promoter mapping of the structural
RT   genes for nitrogenase (nifHDK) of Azospirillum brasilense Sp7.";
RL   Mol. Gen. Genet. 220:88-94(1989).
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: 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 8Fe-7S cluster per heterodimer (By similarity).
CC   -!- COFACTOR: Binds 1 7Fe-Mo-9S-X-homocitryl cluster per subunit. The
CC       identity of the X atom is not known, possibly carbon or oxygen (By
CC       similarity).
CC   -!- SUBUNIT: Tetramer of two alpha and two beta chains. Forms complex
CC       with the iron protein (nitrogenase component 2).
CC   -!- SIMILARITY: Belongs to the NifD/NifK/NifE/NifN family.
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DR   EMBL; M64344; AAB02343.1; -; Genomic_DNA.
DR   EMBL; X51500; CAA35869.2; -; Genomic_DNA.
DR   PIR; S27474; S15748.
DR   ProteinModelPortal; P25313; -.
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: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:EC.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
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   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    482       Nitrogenase molybdenum-iron protein alpha
FT                                chain.
FT                                /FTId=PRO_0000153054.
FT   METAL        62     62       Iron-sulfur (8Fe-7S); shared with beta
FT                                chain (By similarity).
FT   METAL        88     88       Iron-sulfur (8Fe-7S); shared with beta
FT                                chain (By similarity).
FT   METAL       154    154       Iron-sulfur (8Fe-7S); shared with beta
FT                                chain (By similarity).
FT   METAL       445    445       Molybdenum-iron-sulfur (7Fe-Mo-9S-X-
FT                                homocitryl); via pros nitrogen (By
FT                                similarity).
SQ   SEQUENCE   482 AA;  53902 MW;  FC43D87490BBD39B CRC64;
     MSLSVNEGVD VKGLVDKVLE AYPEKSRRRR AKHLNVLEAE AKDCGVKSNI KSIPGVMTIR
     GCAYAGSKGV VWGPIKDMIH ISHGPVGCGY YSWSGRRNYY VGDTGVDKLG TMHFTSDFQE
     KDIVFGGDKK LHKVIEEINE LFPLVNGISI QSECPIGLNG DDIEGVSKAK SEELGKPVVP
     VRCEGFRGVS QSLGHHIAND VIRDWILPKK TEPKEGFVST PYDVTIIGDY NIGGDAWASR
     ILLEEIGLRV IAQWSGDGTL AELENQPKAK VNLIHSYRSM NYIARHMEEK FGIPWMEYNF
     FGPSQIAESL RKIAALFDDT IKENAEKVIA KYQPMVDAVV GDAALRAHGT KGRVPLKPLG
     PRHRPIVDAY HDLGMEIVGT GYEFAHNDDY QRTQHYVKEG TLIYDDVTAF ELEKFVELMR
     PDLVASGIKE KYVFQKMGLP FRQMHSWDYS GPYHGYDGFA IFARDMDLAI NNPVWGIMKA
     PF
//