NIFD_SINFN
ID NIFD_SINFN Reviewed; 504 AA.
AC P19066;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 146.
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=nifD1; OrderedLocusNames=NGR_a01120; ORFNames=y4vL;
GN and
GN Name=nifD2; OrderedLocusNames=NGR_a00880; ORFNames=y4xB;
OS Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OG Plasmid sym pNGR234a.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=394;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234;
RX PubMed=9163424; DOI=10.1038/387394a0;
RA Freiberg C.A., Fellay R., Bairoch A., Broughton W.J., Rosenthal A.,
RA Perret X.;
RT "Molecular basis of symbiosis between Rhizobium and legumes.";
RL Nature 387:394-401(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234;
RX PubMed=19376903; DOI=10.1128/aem.00515-09;
RA Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT systems.";
RL Appl. Environ. Microbiol. 75:4035-4045(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-16 AND 199-393.
RC STRAIN=ANU 240;
RX PubMed=2744485; DOI=10.1016/0378-1119(89)90368-5;
RA Badenoch-Jones J., Holton T.A., Morrison C.M., Scott K.F., Shine J.;
RT "Structural and functional analysis of nitrogenase genes from the broad-
RT host-range Rhizobium strain ANU240.";
RL Gene 77:141-153(1989).
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; U00090; AAB91900.1; -; Genomic_DNA.
DR EMBL; U00090; AAB91924.1; -; Genomic_DNA.
DR EMBL; M26961; AAA26330.1; -; Genomic_DNA.
DR EMBL; M26962; AAA26328.1; -; Genomic_DNA.
DR PIR; PS0045; PS0045.
DR PIR; T10829; T10829.
DR RefSeq; NP_444113.1; NC_000914.2.
DR RefSeq; NP_444137.1; NC_000914.2.
DR RefSeq; WP_010875129.1; NC_000914.2.
DR AlphaFoldDB; P19066; -.
DR SMR; P19066; -.
DR STRING; 394.NGR_a00880; -.
DR EnsemblBacteria; AAB91900; AAB91900; NGR_a01120.
DR EnsemblBacteria; AAB91924; AAB91924; NGR_a00880.
DR KEGG; rhi:NGR_a00880; -.
DR KEGG; rhi:NGR_a01120; -.
DR PATRIC; fig|394.7.peg.77; -.
DR eggNOG; COG2710; Bacteria.
DR HOGENOM; CLU_025876_1_1_5; -.
DR OMA; CGQYSWA; -.
DR OrthoDB; 363662at2; -.
DR Proteomes; UP000001054; Plasmid sym pNGR234a.
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; Plasmid;
KW Reference proteome.
FT CHAIN 1..504
FT /note="Nitrogenase molybdenum-iron protein alpha chain"
FT /id="PRO_0000153079"
FT BINDING 72
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 98
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 164
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 287
FT /ligand="[7Fe-Mo-9S-C-homocitryl] cluster"
FT /ligand_id="ChEBI:CHEBI:30409"
FT /evidence="ECO:0000250"
FT BINDING 454
FT /ligand="[7Fe-Mo-9S-C-homocitryl] cluster"
FT /ligand_id="ChEBI:CHEBI:30409"
FT /evidence="ECO:0000250"
FT CONFLICT 201
FT /note="Q -> K (in Ref. 3; AAA26328)"
FT /evidence="ECO:0000305"
FT CONFLICT 303
FT /note="A -> G (in Ref. 3; AAA26328)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 504 AA; 56944 MW; D3BE3291A9D276DC CRC64;
MSLDYENDSA LHQELITQVL SQYPHKAAKR RQKHLSVASD REAVGEEGET LSECDVKSNI
KSIPGVMTIR GCAYAGSKGV VWGPVKDMVH ISHGPVGCGQ YSWSQRRNYY VGTTGVDTFV
TMQFTSDFQE KDIVFGGDKK LEQVIDEIEE LFPLNNGITI QSECPIGLIG DDIEAVSRKK
AAEHETTIVP VRCEGFRGVS QSLGHHIAND AIRDWVFDKA DGKTDVEFET GPYDVNVIGD
YNIGGDAWAS RILLEEIGLR VVGNWSGDAT LAEVERAPRA KLNLIHCYRS MNYICRHMEE
RYAIPWMEYN FFGPSQIEAS LRKIARHFGP TIEERAERVI AKYRPLVDAV IDKYWPRLQG
KRVMLYVGGL RPRHVITAYE DLGMQIVGTG YEFAHNDDYQ RTGHYVKTGT LIYDDATSYE
LDTFIERIRP DLVGSGIKEK YPVQKMGIPF RQMHSWDYSG PYHGYDGFAI FARDMDLAIN
NPVWDLYDAP WKKMTVPTAA VAAE
