NIFD_METMP
ID NIFD_METMP Reviewed; 477 AA.
AC P0CW51; P71526;
DT 03-MAY-2011, integrated into UniProtKB/Swiss-Prot.
DT 03-MAY-2011, sequence version 1.
DT 03-AUG-2022, entry version 46.
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=MMP0856;
OS Methanococcus maripaludis (strain S2 / LL).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=267377;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=S2 / LL;
RX PubMed=15466049; DOI=10.1128/jb.186.20.6956-6969.2004;
RA Hendrickson E.L., Kaul R., Zhou Y., Bovee D., Chapman P., Chung J.,
RA Conway de Macario E., Dodsworth J.A., Gillett W., Graham D.E., Hackett M.,
RA Haydock A.K., Kang A., Land M.L., Levy R., Lie T.J., Major T.A.,
RA Moore B.C., Porat I., Palmeiri A., Rouse G., Saenphimmachak C., Soell D.,
RA Van Dien S., Wang T., Whitman W.B., Xia Q., Zhang Y., Larimer F.W.,
RA Olson M.V., Leigh J.A.;
RT "Complete genome sequence of the genetically tractable hydrogenotrophic
RT methanogen Methanococcus maripaludis.";
RL J. Bacteriol. 186:6956-6969(2004).
CC -!- FUNCTION: This molybdenum-iron protein is part of the nitrogenase
CC complex that catalyzes the key enzymatic reactions in nitrogen
CC fixation. {ECO:0000250}.
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) (By similarity).
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NifD/NifK/NifE/NifN family. {ECO:0000305}.
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DR EMBL; BX950229; CAF30412.1; -; Genomic_DNA.
DR RefSeq; WP_011170800.1; NC_005791.1.
DR AlphaFoldDB; P0CW51; -.
DR SMR; P0CW51; -.
DR STRING; 267377.MMP0856; -.
DR EnsemblBacteria; CAF30412; CAF30412; MMP0856.
DR GeneID; 2761670; -.
DR KEGG; mmp:MMP0856; -.
DR PATRIC; fig|267377.15.peg.881; -.
DR eggNOG; arCOG00598; Archaea.
DR HOGENOM; CLU_025876_1_0_2; -.
DR OMA; CGQYSWA; -.
DR OrthoDB; 10827at2157; -.
DR BioCyc; MMAR267377:MMP_RS04455-MON; -.
DR Proteomes; UP000000590; Chromosome.
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; IPR005974; Nase_asu.
DR InterPro; IPR010143; Nase_comp1_asu.
DR InterPro; IPR000318; Nase_comp1_CS.
DR PANTHER; PTHR43457; PTHR43457; 1.
DR Pfam; PF00148; Oxidored_nitro; 1.
DR TIGRFAMs; TIGR01284; alt_nitrog_alph; 1.
DR TIGRFAMs; TIGR01862; N2-ase-Ialpha; 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..477
FT /note="Nitrogenase molybdenum-iron protein alpha chain"
FT /id="PRO_0000408202"
FT BINDING 49
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 75
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 149
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 267
FT /ligand="[7Fe-Mo-9S-C-homocitryl] cluster"
FT /ligand_id="ChEBI:CHEBI:30409"
FT /evidence="ECO:0000250"
FT BINDING 433
FT /ligand="[7Fe-Mo-9S-C-homocitryl] cluster"
FT /ligand_id="ChEBI:CHEBI:30409"
FT /evidence="ECO:0000250"
SQ SEQUENCE 477 AA; 53632 MW; 2773022686D9440C CRC64;
MPFCLLDVDK DIPEREQHIY IKDSKEPKGH CKQRCNTNTI PGSMTERGCA FAGVKGVITG
AIKDVLHVVH SPVGCTAYGN GTTKRYPTRP EMPDGSVFPV ENFNLKHIVG TDLTESDVVF
GGMNKLKKVI REASKEFPFV NAIYVYATCT TGLIGDDLDA VCKEMQAELG KDVVAFNAPG
FAGPTQSKGH HVGNYTIFEK LVGTKEPPKT TDYDINLIGE YNIDGDYWVL EKYFEDMGIN
VLSKFTGDAT HGELCWMHKA KLSLVRCQRS ATYVAKLIEE KYGVPYLKVD FFGPEYCAEN
LRAVGKYFGK EIEAEAVIKK EMEKIQPELD FYKSKLQGKK IWISAGGPKS WHLSKPIEQY
LGMDVVALSG LFEHEDGYEK MQERAKDGTI IIDDPNTLEM EEVVEKYQPE IVLGGIKEKY
FFHKLGVPSV MIHSYENGPY IGFEGFVNMA RDIYTAIYNP AWKLMEFEEE EPGDSNE
