NIFD_ACIFI
ID NIFD_ACIFI Reviewed; 489 AA.
AC P06662;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-APR-1990, sequence version 2.
DT 03-AUG-2022, entry version 90.
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 ferridurans.
OC Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC Acidithiobacillaceae; Acidithiobacillus.
OX NCBI_TaxID=1232575;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 33020 / DSM 29468 / JCM 18981 / 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].
RC STRAIN=ATCC 33020 / DSM 29468 / JCM 18981 / 11Fe;
RX PubMed=3539923; DOI=10.1128/jb.169.1.367-370.1987;
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 of
RT 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:
CC Reaction=16 ATP + 16 H2O + N2 + 8 reduced [2Fe-2S]-[ferredoxin] = 16
CC ADP + 6 H(+) + H2 + 2 NH4(+) + 8 oxidized [2Fe-2S]-[ferredoxin] + 16
CC phosphate; Xref=Rhea:RHEA:21448, Rhea:RHEA-COMP:10000, Rhea:RHEA-
CC COMP:10001, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:17997,
CC ChEBI:CHEBI:18276, ChEBI:CHEBI:28938, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:43474,
CC ChEBI:CHEBI:456216; EC=1.18.6.1;
CC -!- COFACTOR:
CC Name=[8Fe-7S] cluster; Xref=ChEBI:CHEBI:21143; Evidence={ECO:0000250};
CC Note=Binds 1 [8Fe-7S] cluster per heterodimer. {ECO:0000250};
CC -!- COFACTOR:
CC Name=[7Fe-Mo-9S-C-homocitryl] cluster; Xref=ChEBI:CHEBI:30409;
CC Evidence={ECO:0000250};
CC Note=Binds 1 [7Fe-Mo-9S-C-homocitryl] cluster per subunit.
CC {ECO:0000250};
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains. Forms complex with
CC the iron protein (nitrogenase component 2).
CC -!- SIMILARITY: Belongs to the NifD/NifK/NifE/NifN family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; M15238; AAA27375.1; -; Genomic_DNA.
DR PIR; A91597; NIBCAT.
DR AlphaFoldDB; P06662; -.
DR SMR; P06662; -.
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 CDD; cd01976; Nitrogenase_MoFe_alpha; 1.
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 PANTHER; PTHR43457; PTHR43457; 1.
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
FT /note="Nitrogenase molybdenum-iron protein alpha chain"
FT /id="PRO_0000153084"
FT BINDING 71
FT /ligand="[8Fe-7S] cluster"
FT /ligand_id="ChEBI:CHEBI:21143"
FT /ligand_note="ligand shared with beta chain"
FT /evidence="ECO:0000250"
FT BINDING 97
FT /ligand="[8Fe-7S] cluster"
FT /ligand_id="ChEBI:CHEBI:21143"
FT /ligand_note="ligand shared with beta chain"
FT /evidence="ECO:0000250"
FT BINDING 163
FT /ligand="[8Fe-7S] cluster"
FT /ligand_id="ChEBI:CHEBI:21143"
FT /ligand_note="ligand shared with beta chain"
FT /evidence="ECO:0000250"
FT BINDING 284
FT /ligand="[7Fe-Mo-9S-C-homocitryl] cluster"
FT /ligand_id="ChEBI:CHEBI:30409"
FT /evidence="ECO:0000250"
FT BINDING 451
FT /ligand="[7Fe-Mo-9S-C-homocitryl] cluster"
FT /ligand_id="ChEBI:CHEBI:30409"
FT /evidence="ECO:0000250"
FT CONFLICT 55
FT /note="V -> C (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 129
FT /note="E -> V (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 176
FT /note="S -> F (in Ref. 2)"
FT /evidence="ECO:0000305"
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
