ID   ANFK_AZOVI     STANDARD;      PRT;   461 AA.
AC   P16267;
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 beta chain (EC 1.18.6.1) (Nitrogenase
DE   component I) (Dinitrogenase 3 beta subunit).
GN   Name=anfK;
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; AAA82511.1; -.
DR   PIR; D32057; D32057.
DR   HSSP; P11347; 1MIO.
DR   InterPro; IPR000318; Nitrognse_comp1.
DR   InterPro; IPR000510; Oxred_nitrognse1.
DR   Pfam; PF00148; Oxidored_nitro; 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
SQ   SEQUENCE   461 AA;  51049 MW;  8A90B88D522E72D1 CRC64;
     TCEVKEKGRV GTINPIFTCQ PAGAQFVSIG IKDCIGIVHG GQGCVMFVRL IFSQHYKESF
     ELASSSLHED GAVFGACGRV EEAVDVLLSR YPDVKVVPII TTCSTEIIGD DVDGVIKKLN
     EGLLKEKFPD REVHLIAMHT PSFVGSMISG YDVAVRDVVR HFAKREAPND KINLLTGWVN
     PGDVKELKHL LGEMDIEANV LFEIESFDSP ILPDGSAVSH GNTTIEDLID TGNARATFAL
     NRYEGTKAAE YLQKKFEIPA IIGPTPIGIR NTDIFLQNLK KATGKPIPQS LAHERGVAID
     ALADLTHMFL AEKRVAIYGA PDLVIGLAEF CLDLEMKPVL LLLGDDNSKY VDDPRIKALQ
     ENVDYGMEIV TNADFWELEN RIKNEGLELD LILGHSKGRF ISIDYNIPML RVGFPTYDRA
     GLFRYPTVGY GGAIWLAEQM ANTLFADMEH KKNKEWVLNV W
//