ID   ANFK_AZOVI     STANDARD;      PRT;   461 AA.
AC   P16267;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   04-JAN-2005, sequence version 2.
DT   07-FEB-2006, entry version 42.
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 [GENOMIC DNA].
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   MEDLINE=93319493; 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: This iron-iron protein is part of the nitrogenase
CC       complex that catalyzes the key enzymatic reactions in nitrogen
CC       fixation. Other nitrogenase complexes utilize a molybdenum-iron
CC       protein or a vanadium-iron protein.
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   -!- SUBUNIT: Hexamer of two alpha, two beta, and two delta chains.
CC   -!- SIMILARITY: Belongs to the nifD/nifK/nifE/nifN family.
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DR   EMBL; M23528; AAA82511.1; -; Genomic_DNA.
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; Iron-sulfur; Metal-binding;
KW   Nitrogen fixation; Oxidoreductase.
FT   INIT_MET      0      0
FT   CHAIN         1    461       Nitrogenase iron-iron protein beta chain.
FT                                /FTId=PRO_0000153092.
FT   METAL        19     19       Iron-sulfur (8Fe-7S) (shared with alpha
FT                                chain) (By similarity).
FT   METAL        44     44       Iron-sulfur (8Fe-7S) (shared with alpha
FT                                chain) (By similarity).
FT   METAL       103    103       Iron-sulfur (8Fe-7S) (shared with alpha
FT                                chain) (By similarity).
FT   METAL       142    142       Iron-sulfur (8Fe-7S) (shared with alpha
FT                                chain) (By similarity).
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
//