ID   NIFH_HERSE     STANDARD;      PRT;   292 AA.
AC   P77873;
DT   28-FEB-2003 (Rel. 41, Created)
DT   28-FEB-2003 (Rel. 41, Last sequence update)
DT   25-OCT-2004 (Rel. 45, Last annotation update)
DE   Nitrogenase iron protein (EC 1.18.6.1) (Nitrogenase component II)
DE   (Nitrogenase Fe protein) (Nitrogenase reductase).
GN   Name=nifH;
OS   Herbaspirillum seropedicae.
OC   Bacteria; Proteobacteria; Betaproteobacteria; Burkholderiales;
OC   Oxalobacteraceae; Herbaspirillum.
OX   NCBI_TaxID=964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=Z78;
RX   MEDLINE=97365591; PubMed=9222418;
RA   Machado I.M.P., Yates M.G., Machado H.B., Souza E.M., Pedrosa F.O.;
RT   "Cloning and sequencing of the nitrogenase structural genes nifHDK of
RT   Herbaspirillum seropedicae.";
RL   Braz. J. Med. Biol. Res. 29:1599-1602(1996).
RN   [2]
RP   NUCLEOTIDE SEQUENCE OF 18-129.
RC   STRAIN=Z67;
RX   MEDLINE=97352671; PubMed=9209030;
RA   Hurek T., Egener T., Reinhold-Hurek B.;
RT   "Divergence in nitrogenases of Azoarcus spp., Proteobacteria of the
RT   beta subclass.";
RL   J. Bacteriol. 179:4172-4178(1997).
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   -!- COFACTOR: Binds one 4Fe-4S cluster per dimer.
CC   -!- SUBUNIT: Homodimer (By similarity).
CC   -!- SIMILARITY: Belongs to the nifH / bchL / chlL 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; Z54207; CAA90932.1; -.
DR   EMBL; U97121; AAB63038.1; -.
DR   HSSP; P00459; 1G20.
DR   HAMAP; MF_00533; -; 1.
DR   InterPro; IPR005977; NifH.
DR   InterPro; IPR000392; NitrogenaseII.
DR   Pfam; PF00142; Fer4_NifH; 1.
DR   PRINTS; PR00091; NITROGNASEII.
DR   TIGRFAMs; TIGR01287; nifH; 1.
DR   PROSITE; PS00746; NIFH_FRXC_1; 1.
DR   PROSITE; PS00692; NIFH_FRXC_2; 1.
DR   PROSITE; PS51026; NIFH_FRXC_3; 1.
KW   4Fe-4S; ATP-binding; Iron-sulfur; Nitrogen fixation; Oxidoreductase.
FT   NP_BIND      11     18       ATP (Potential).
FT   METAL        99     99       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       133    133       Iron-sulfur (4Fe-4S) (By similarity).
SQ   SEQUENCE   292 AA;  31360 MW;  F34492139646A567 CRC64;
     MASLRQIAFY GKGGIGKSTT SQNTLAALAQ MGQRILIVGC DPKADSTRLI LHAKAQDTIL
     SLAADAGSVE DLELEDVMKI GYQNIRCVES GGPEPGVGCA GRGVITSINF LEEEGAYDDT
     DYVSYDVLGD VVCGGFAMPI RENKAQEIYI VMSGEMMAMY AANNISKGIL KYANSGGVRL
     GGLICNERKT DKELELATAL AAKLNSKLIH FVPRDNIVQH AELRRMTVLE YAPDSKQAGE
     YRTLANKIHE NAGNGTIPTP ITMDELEDLL MQHGLMPVVD ESMVGKSAEV AA
//