ID   ANFD_AZOVI     STANDARD;      PRT;   517 AA.
AC   P16266;
DT   01-APR-1990 (Rel. 14, Created)
DT   01-FEB-2005 (Rel. 46, Last sequence update)
DT   01-FEB-2005 (Rel. 46, Last annotation update)
DE   Nitrogenase iron-iron protein alpha chain (EC 1.18.6.1) (Nitrogenase
DE   component I) (Dinitrogenase 3 alpha subunit).
GN   Name=anfD;
OS   Azotobacter vinelandii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RX   MEDLINE=89123105; PubMed=2644222;
RA   Joerger R.D., Jacobson M.R., Premakumar R., Wolfinger E.D.,
RA   Bishop P.E.;
RT   "Nucleotide sequence and mutational analysis of the structural genes
RT   (anfHDGK) for the second alternative nitrogenase from Azotobacter
RT   vinelandii.";
RL   J. Bacteriol. 171:1075-1086(1989).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-6.
RC   STRAIN=RP306;
RX   PubMed=8392330;
RA   Pau R.N., Eldridge M.E., Lowe D.J., Mitchenall L.A., Eady R.R.;
RT   "Molybdenum-independent nitrogenases of Azotobacter vinelandii: a
RT   functional species of alternative nitrogenase-3 isolated from a
RT   molybdenum-tolerant strain contains an iron-molybdenum cofactor.";
RL   Biochem. J. 293:101-107(1993).
CC   -!- FUNCTION: The key enzymatic reactions in nitrogen fixation are
CC       catalyzed by the nitrogenase complex, which has 2 components: the
CC       iron protein (component 2) and a component 1 which is either a
CC       molybdenum-iron protein, a vanadium-iron, or an iron-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   -!- COFACTOR: Iron-sulfur.
CC   -!- SUBUNIT: Hexamer of two alpha, two beta, and two delta chains.
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; M23528; AAA82509.1; -.
DR   PIR; B32057; B32057.
DR   HSSP; P00467; 1MIO.
DR   InterPro; IPR010143; N2-ase-Ialpha.
DR   InterPro; IPR005974; Nitrog_alpha.
DR   InterPro; IPR000318; Nitrognse_comp1.
DR   InterPro; IPR000510; Oxred_nitrognse1.
DR   Pfam; PF00148; Oxidored_nitro; 1.
DR   TIGRFAMs; TIGR01284; alt_nitrog_alph; 1.
DR   TIGRFAMs; TIGR01861; ANFD; 1.
DR   TIGRFAMs; TIGR01862; N2-ase-Ialpha; 1.
DR   PROSITE; PS00699; NITROGENASE_1_1; 1.
DR   PROSITE; PS00090; NITROGENASE_1_2; 1.
KW   Direct protein sequencing; Iron-sulfur; Nitrogen fixation;
KW   Oxidoreductase.
FT   INIT_MET      0      0
FT   CONFLICT      3      3       H -> E (in Ref. 2).
SQ   SEQUENCE   517 AA;  58282 MW;  D84B513BD2E66F8B CRC64;
     PHHEFECSKV IPERKKHAVI KGKGETLADA LPQGYLNTIP GSISERGCAY CGAKHVIGTP
     MKDVIHISHG PVGCTYDTWQ TKRYISDNDN FQLKYTYATD VKEKHIVFGA EKLLKQNIIE
     AFKAFPQIKR MTIYQTCATA LIGDDINAIA EEVMEEMPEV DIFVCNSPGF AGPSQSGGHH
     KINIAWINQK VGTVEPEITG DHVINYVGEY NIQGDQEVMV DYFKRMGIQV LSTFTGNGSY
     DGLRAMHRAH LNVLECARSA EYICNELRVR YGIPRLDIDG FGFKPLADSL RKIGMFFGIE
     DRAKAIIDEE VARWKPELDW YKERLMGKKV CLWPGGSKLW HWAHVIEEEM GLKVVSVYIK
     FGHQGDMEKG IARCGEGTLA IDDPNELEGL EALEMLKPDI ILTGKRPGEV AKKVRVPYLN
     AHAYHNGPYK GFEGWVRFAR DIYNAIYSPI HQLSGIDITK DNAPEWGNGF RTRQMLSDGN
     LSDAVRNSET LRQYTGGYDS VSKLREREYP AFERKVG
//