NIFD_METTH
ID NIFD_METTH Reviewed; 469 AA.
AC O27605;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 117.
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=MTH_1563;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
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; AE000666; AAB86037.1; -; Genomic_DNA.
DR PIR; F69075; F69075.
DR RefSeq; WP_010877172.1; NC_000916.1.
DR AlphaFoldDB; O27605; -.
DR SMR; O27605; -.
DR STRING; 187420.MTH_1563; -.
DR EnsemblBacteria; AAB86037; AAB86037; MTH_1563.
DR GeneID; 1471832; -.
DR KEGG; mth:MTH_1563; -.
DR PATRIC; fig|187420.15.peg.1526; -.
DR HOGENOM; CLU_025876_1_0_2; -.
DR OMA; CGQYSWA; -.
DR Proteomes; UP000005223; 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..469
FT /note="Nitrogenase molybdenum-iron protein alpha chain"
FT /id="PRO_0000153073"
FT BINDING 48
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 74
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 147
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 265
FT /ligand="[7Fe-Mo-9S-C-homocitryl] cluster"
FT /ligand_id="ChEBI:CHEBI:30409"
FT /evidence="ECO:0000250"
FT BINDING 431
FT /ligand="[7Fe-Mo-9S-C-homocitryl] cluster"
FT /ligand_id="ChEBI:CHEBI:30409"
FT /evidence="ECO:0000250"
SQ SEQUENCE 469 AA; 52866 MW; 7D2CD5FFED9EC7B8 CRC64;
MPFKLFDVDA EIPERKKHVY IKKKEDPEED LPLCNTKTIP GCMTERGCAF AGAKGVITGA
IKDALHVIHS PVGCTAYGYG TKRYPTSQEM PDGSLFPIEN FNLKYITGTN LTETDVVFGG
MDKLKRCIIE AAKEFPEANA VYTYATCTTG LIGDDIEAVS REVSEEIGKD VVAINAPGFA
GPTQSKGHQV ANYTLFENLV GTAEPPVVTD YDVNLIGEYN IDGDLWVLKR YFEEMGINVL
STFTGDCCHD EIKWMHRAKL SLVRCQRSAT YIARLLEERY NVPYMKVDFF GIEYCKRNLM
ATGEYFGIPE RAEEVIKDRM EKIGPEIEYL RNKLAGKKVW VFSGGPKNWH LPRPLEDELG
MEVVAVSTMF EHEDGYEKIK KRVGENTVIV DDPNSLELEE IIEKYRPDII LSGIKEKYLA
HKLGVPCVLI HSYENGPYIG FEGFLNLARD MYASIYSPVW DLLEFEAGD
