ID NIFD_THIFE Reviewed; 489 AA.
AC P06662;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 2.
DT 03-APR-2013, entry version 71.
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 Thiobacillus ferrooxidans (Acidithiobacillus 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-X-homocitryl cluster per subunit. The
CC identity of the X atom is not known, possibly carbon or oxygen (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: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: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 (7Fe-Mo-9S-X-
FT homocitryl) (By similarity).
FT METAL 451 451 Molybdenum-iron-sulfur (7Fe-Mo-9S-X-
FT 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
//
