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Database: UniProt
Entry: P06662
LinkDB: P06662
Original site: P06662 
ID   NIFD_ACIFR              Reviewed;         489 AA.
AC   P06662;
DT   01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 2.
DT   22-JAN-2014, entry version 74.
DE   RecName: Full=Nitrogenase molybdenum-iron protein alpha chain;
DE            EC=1.18.6.1;
DE   AltName: Full=Dinitrogenase;
DE   AltName: Full=Nitrogenase component I;
GN   Name=nifD;
OS   Acidithiobacillus ferrooxidans (Thiobacillus ferrooxidans).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Acidithiobacillales;
OC   Acidithiobacillaceae; Acidithiobacillus.
OX   NCBI_TaxID=920;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33020 / 11Fe;
RX   PubMed=3234769; DOI=10.1016/0378-1119(88)90444-1;
RA   Rawlings D.E.;
RT   "Sequence and structural analysis of the alpha- and beta-dinitrogenase
RT   subunits of Thiobacillus ferrooxidans.";
RL   Gene 69:337-343(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=3539923;
RA   Pretorius I.-M., Rawlings D.E., O'Neill E.G., Jones W.A., Kirby R.,
RA   Woods D.R.;
RT   "Nucleotide sequence of the gene encoding the nitrogenase iron protein
RT   of Thiobacillus ferrooxidans.";
RL   J. Bacteriol. 169:367-370(1987).
CC   -!- FUNCTION: This molybdenum-iron protein is part of the nitrogenase
CC       complex that catalyzes the key enzymatic reactions in nitrogen
CC       fixation.
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   -!- COFACTOR: Binds 1 7Fe-Mo-9S-C-homocitryl cluster per subunit (By
CC       similarity).
CC   -!- SUBUNIT: Tetramer of two alpha and two beta chains. Forms complex
CC       with the iron protein (nitrogenase component 2).
CC   -!- SIMILARITY: Belongs to the NifD/NifK/NifE/NifN family.
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DR   EMBL; M15238; AAA27375.1; -; Genomic_DNA.
DR   PIR; A91597; NIBCAT.
DR   ProteinModelPortal; P06662; -.
DR   SMR; P06662; 19-489.
DR   GO; GO:0016612; C:molybdenum-iron nitrogenase complex; IEA:InterPro.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0018697; F:carbonyl sulfide nitrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0016163; F:nitrogenase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR   InterPro; IPR000510; Nase/OxRdtase_comp1.
DR   InterPro; IPR010143; Nase_comp1_asu.
DR   InterPro; IPR000318; Nase_comp1_CS.
DR   InterPro; IPR005972; Nase_Mo-Fe_asu.
DR   Pfam; PF00148; Oxidored_nitro; 1.
DR   TIGRFAMs; TIGR01862; N2-ase-Ialpha; 1.
DR   TIGRFAMs; TIGR01282; nifD; 1.
DR   PROSITE; PS00699; NITROGENASE_1_1; 1.
DR   PROSITE; PS00090; NITROGENASE_1_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Iron; Iron-sulfur; Metal-binding; Molybdenum;
KW   Nitrogen fixation; Nucleotide-binding; Oxidoreductase.
FT   CHAIN         1    489       Nitrogenase molybdenum-iron protein alpha
FT                                chain.
FT                                /FTId=PRO_0000153084.
FT   METAL        71     71       Iron-sulfur (8Fe-7S); shared with beta
FT                                chain (By similarity).
FT   METAL        97     97       Iron-sulfur (8Fe-7S); shared with beta
FT                                chain (By similarity).
FT   METAL       163    163       Iron-sulfur (8Fe-7S); shared with beta
FT                                chain (By similarity).
FT   METAL       284    284       Molybdenum-iron-sulfur-carbon (7Fe-Mo-9S-
FT                                C-homocitryl) (By similarity).
FT   METAL       451    451       Molybdenum-iron-sulfur-carbon (7Fe-Mo-9S-
FT                                C-homocitryl); via pros nitrogen (By
FT                                similarity).
FT   CONFLICT     55     55       V -> C (in Ref. 2).
FT   CONFLICT    129    129       E -> V (in Ref. 2).
FT   CONFLICT    176    176       S -> F (in Ref. 2).
SQ   SEQUENCE   489 AA;  55056 MW;  5FE4F2166370EA4C CRC64;
     MSISAEDLST QPQRRKLPEI AELIDETLKA YPEKFAKRRA KHLNVYEEGK SECDVKSNIK
     SVPGVMTIRG CAYAGSYGVV WSPVKDMIHI SHGPVGCGHY ARAGRRAYYI GTTGVDTYTT
     MHFTSDFQEK DIVFGGDKKL AKLMDELEEL FPMSKGITVQ SECPIGLIGD DIEAVSKKKA
     AEFGKPVVPN RCEGFRGVSQ SLGHHIANDS IRDWVLDPAA DKHPDFESTP YDVTLLGDYN
     IGGDWGSRII LEEMGLRVIA QWSGDAPSRS STASSKSKLN LLHCYRSVNY ITRHMEEKYG
     IPYIEFNFFG PTKIKESLRQ IAAFFDESIQ EKAEKAIAKY QPQWDAVVEK FRPRLEGKKV
     MLFVGGLRPG HTIGAFEDLG MEVIGTGYEF GHNDDYQRTT HEIKGNTLIY DDVTGYEFEK
     FAEKLRPDLV ASGVKEKYIF QKMGFPFRQM HSWDYSGPYH GPDGFAIFAR DMDMAVNNPV
     WGLTQAPWK
//
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