ID   NIFD_AZOBR     STANDARD;      PRT;   482 AA.
AC   P25313;
DT   01-MAY-1992 (Rel. 22, Created)
DT   01-MAY-1992 (Rel. 22, Last sequence update)
DT   25-OCT-2004 (Rel. 45, Last annotation update)
DE   Nitrogenase molybdenum-iron protein alpha chain (EC 1.18.6.1)
DE   (Nitrogenase component I) (Dinitrogenase).
GN   Name=nifD;
OS   Azospirillum brasilense.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Azospirillum.
OX   NCBI_TaxID=192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=92370074; 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 OF 1-28.
RC   STRAIN=Sp7 / ATCC 29145;
RX   MEDLINE=90114114; 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: The key enzymatic reactions in nitrogen fixation are
CC       catalyzed by the nitrogenase complex, which has 2 components: the
CC       iron protein and the molybdenum-iron protein.
CC   -!- CATALYTIC ACTIVITY: 3 reduced ferredoxin + 6 H(+) + N(2) + n ATP =
CC       3 oxidized ferredoxin + 2 NH(3) + n ADP + n phosphate.
CC   -!- SUBUNIT: Tetramer of two alpha and two beta chains that binds 30-
CC       32 Fe, 2 Mo, and inorganic sulfur.
CC   -!- SIMILARITY: Belongs to the nifD/nifK/nifE/nifN family.
CC   --------------------------------------------------------------------------
CC   This Swiss-Prot entry is copyright. It is produced through a collaboration
CC   between  the Swiss Institute of Bioinformatics  and the  EMBL outstation -
CC   the European Bioinformatics Institute.  There are no  restrictions on  its
CC   use as long as its content is in no way modified and this statement is not
CC   removed.
CC   --------------------------------------------------------------------------
DR   EMBL; M64344; AAB02343.1; -.
DR   EMBL; X51500; CAA35869.2; -.
DR   PIR; S27474; S15748.
DR   HSSP; P07328; 1L5H.
DR   InterPro; IPR010143; N2-ase-Ialpha.
DR   InterPro; IPR005972; NifD.
DR   InterPro; IPR000318; Nitrognse_comp1.
DR   InterPro; IPR000510; Oxred_nitrognse1.
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.
KW   Iron-sulfur; Molybdenum; Nitrogen fixation; Oxidoreductase.
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
//