NIFD_METTM
ID NIFD_METTM Reviewed; 470 AA.
AC Q50788; D9PU60; P97185;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 30-NOV-2010, sequence version 3.
DT 03-AUG-2022, entry version 103.
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=MTBMA_c01490;
OS Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM
OS 14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium
OS thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=79929;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RA Hochheimer A.;
RL Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=20802048; DOI=10.1128/jb.00844-10;
RA Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H.,
RA Gottschalk G., Thauer R.K.;
RT "Complete genome sequence of Methanothermobacter marburgensis, a
RT methanoarchaeon model organism.";
RL J. Bacteriol. 192:5850-5851(2010).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-220.
RC STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC Marburg;
RX PubMed=8575452; DOI=10.1111/j.1432-1033.1995.910_a.x;
RA Hochheimer A., Schmitz R.A., Thauer R.K., Hedderich R.;
RT "The tungsten formylmethanofuran dehydrogenase from Methanobacterium
RT thermoautotrophicum contains sequence motifs characteristic for enzymes
RT containing molybdopterin dinucleotide.";
RL Eur. J. Biochem. 234:910-920(1995).
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; X87971; CAA61219.1; -; Genomic_DNA.
DR EMBL; CP001710; ADL57758.1; -; Genomic_DNA.
DR PIR; S63551; S63551.
DR RefSeq; WP_013294986.1; NC_014408.1.
DR AlphaFoldDB; Q50788; -.
DR SMR; Q50788; -.
DR STRING; 79929.MTBMA_c01490; -.
DR EnsemblBacteria; ADL57758; ADL57758; MTBMA_c01490.
DR GeneID; 9703854; -.
DR KEGG; mmg:MTBMA_c01490; -.
DR PATRIC; fig|79929.8.peg.145; -.
DR HOGENOM; CLU_025876_1_0_2; -.
DR OMA; CGQYSWA; -.
DR OrthoDB; 10827at2157; -.
DR Proteomes; UP000000345; 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.
FT CHAIN 1..470
FT /note="Nitrogenase molybdenum-iron protein alpha chain"
FT /id="PRO_0000153074"
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"
FT CONFLICT 348
FT /note="N -> I (in Ref. 1; CAA61219)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 470 AA; 53057 MW; 9419CE510DB68CD9 CRC64;
MPFELFGVDA EIPDRKKHIY VKKQGDPEGD IPACNTTTIP GCMTERGCAF AGAKGVITGA
IKDALHVIHS PVGCTAYGYG TKRYPTSQEM PDGSMFPIEK FNLKYITGTD LSESDVVFGG
MDKLKRCILE AVREFPEANA VYTYATCTTG LIGDDIDAIS REVSEEIGKD VVAINAPGFA
GPTQSKGHQV ANYTLFEDLV GTAEPPRTTE YDVNLIGEYN IDGDLWVLKK YFEEMGINVL
STFTGDCCHD EIKWMHRAKL SLVRCQRSAN YIAKLLEERY GVPYMKVDFF GIEYCRKNLM
AIGEYFGIPE RAERVIEDRM KKIGPEIQYF KDKLRGKRVW VFSGGPKNWH LPRPLEDELG
MEVVAVSTMF EHEDGYEKIK KRVREGTVIV DDPNSLELEE IIEKYRPDII LSGIKEKYLA
HKLGVPCILI HSYENGPYIG FEGFLNLARD MYAAIYNPVW DLLEFEEDVN
