NIFD_NOSS1
ID NIFD_NOSS1 Reviewed; 497 AA.
AC P00464;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 121.
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; OrderedLocusNames=all1454;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16593347; DOI=10.1073/pnas.80.15.4723;
RA Lammers P.J., Haselkorn R.;
RT "Sequence of the nifD gene coding for the alpha subunit of dinitrogenase
RT from the cyanobacterium Anabaena.";
RL Proc. Natl. Acad. Sci. U.S.A. 80:4723-4727(1983).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
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}.
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DR EMBL; V01482; CAA24730.1; -; Genomic_DNA.
DR EMBL; BA000019; BAB73398.1; -; Genomic_DNA.
DR PIR; A00542; NIAIMA.
DR PIR; AF1986; AF1986.
DR AlphaFoldDB; P00464; -.
DR SMR; P00464; -.
DR STRING; 103690.17130788; -.
DR PRIDE; P00464; -.
DR EnsemblBacteria; BAB73398; BAB73398; BAB73398.
DR KEGG; ana:all1454; -.
DR eggNOG; COG2710; Bacteria.
DR OMA; ILTNRGC; -.
DR Proteomes; UP000002483; Chromosome.
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; Reference proteome.
FT CHAIN 1..497
FT /note="Nitrogenase molybdenum-iron protein alpha chain"
FT /id="PRO_0000153053"
FT BINDING 64
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 90
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 156
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 282
FT /ligand="[7Fe-Mo-9S-C-homocitryl] cluster"
FT /ligand_id="ChEBI:CHEBI:30409"
FT /evidence="ECO:0000250"
FT BINDING 449
FT /ligand="[7Fe-Mo-9S-C-homocitryl] cluster"
FT /ligand_id="ChEBI:CHEBI:30409"
FT /evidence="ECO:0000250"
FT CONFLICT 160
FT /note="L -> S (in Ref. 1; CAA24730)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="N -> T (in Ref. 1; CAA24730)"
FT /evidence="ECO:0000305"
FT CONFLICT 455..496
FT /note="GPYHGYDGFAIFARDMDLALNSPTWSLIGAPWKKAAAKAKAA -> ELGDGV
FT QMSDEVRFFCEGRKKSLFL (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 497 AA; 55889 MW; 062CF54FAC302694 CRC64;
MTPPENKNLV DENKELIQEV LKAYPEKSRK KREKHLNVHE ENKSDCGVKS NIKSVPGVMT
ARGCAYAGSK GVVWGPIKDM IHISHGPVGC GYWSWSGRRN YYVGVTGINS FGTMHFTSDF
QERDIVFGGD KKLTKLIEEL DVLFPLNRGV SIQSECPIGL IGDDIEAVAK KTSKQIGKPV
VPLRCEGFRG VSQSLGHHIA NDAIRDWIFP EYDKLKKENR LDFEPSPYDV ALIGDYNIGG
DAWASRMLLE EMGLRVVAQW SGDGTLNELI QGPAAKLVLI HCYRSMNYIC RSLEEQYGMP
WMEFNFFGPT KIAASLREIA AKFDSKIQEN AEKVIAKYTP VMNAVLDKYR PRLEGNTVML
YVGGLRPRHV VPAFEDLGIK VVGTGYEFAH NDDYKRTTHY IDNATIIYDD VTAYEFEEFV
KAKKPDLIAS GIKEKYVFQK MGLPFRQMHS WDYSGPYHGY DGFAIFARDM DLALNSPTWS
LIGAPWKKAA AKAKAAA
