ID   NIFH_AZOBR     STANDARD;      PRT;   293 AA.
AC   P17303;
DT   01-AUG-1990 (Rel. 15, Created)
DT   01-AUG-1990 (Rel. 15, Last sequence update)
DT   01-FEB-2005 (Rel. 46, 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   Azospirillum brasilense.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Azospirillum.
OX   NCBI_TaxID=192;
RN   [1]
RP   NUCLEOTIDE SEQUENCE.
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).
RN   [2]
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=2608029;
RA   Fani R., Allotta G., Bazzicalupo M., Ricci F., Schipani C.,
RA   Polsinelli M.;
RT   "Nucleotide sequence of the gene encoding the nitrogenase iron protein
RT   (nifH) of Azospirillum brasilense and identification of a region
RT   controlling nifH transcription.";
RL   Mol. Gen. Genet. 220:81-87(1989).
RN   [3]
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).
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.
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; X51500; CAA35868.1; -.
DR   EMBL; M64344; AAB02342.1; ALT_SEQ.
DR   PIR; S15747; S15747.
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      10     17       ATP (Potential).
FT   METAL        98     98       Iron-sulfur (4Fe-4S) (By similarity).
FT   METAL       132    132       Iron-sulfur (4Fe-4S) (By similarity).
FT   CONFLICT    160    160       A -> E (in Ref. 2).
FT   CONFLICT    209    209       H -> T (in Ref. 2).
FT   CONFLICT    239    239       E -> Q (in Ref. 2).
SQ   SEQUENCE   293 AA;  31729 MW;  1CEC281B3030802F CRC64;
     MSLRQIAFYG KGGIGKSTTS QNTLAALVEL DQKILIVGCD PKADSTRLIL HAKAQDTVLH
     LAAEAGSVED LELEDVLKIG YKGIKCVESG GPEPGVGCAG RGVITSINFL EENGAYDDVD
     YVSYDVLGDV VCGGFAMPIR ENKAQEIYIV MSGEMMALYA ANNIAKGILK YAHSGGVRLG
     GLICNERQTD KEIDLASALA ARLGTQLIHF VPRDNIVQHA ELRRMTVIEY APDSQQAQEY
     RQLANKVHAN KGKGTIPTPI TMEELEEMLM DFGIMKSEEQ QLAELQAKEA AKA
//