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   27-MAR-2024, entry version 153.
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; Pseudomonadota; 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}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; U00090; AAB91900.1; -; Genomic_DNA.
DR   EMBL; U00090; AAB91924.1; -; Genomic_DNA.
DR   EMBL; AH000924; AAA26328.1; -; Genomic_DNA.
DR   EMBL; AH000924; AAA26330.1; -; 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   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   OrthoDB; 9762718at2; -.
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   Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 3.
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   NCBIfam; TIGR01862; N2-ase-Ialpha; 1.
DR   NCBIfam; TIGR01282; nifD; 1.
DR   PANTHER; PTHR43457; NITROGENASE MOLYBDENUM-IRON PROTEIN ALPHA CHAIN; 1.
DR   PANTHER; PTHR43457:SF1; NITROGENASE MOLYBDENUM-IRON PROTEIN ALPHA CHAIN; 1.
DR   Pfam; PF00148; Oxidored_nitro; 1.
DR   SUPFAM; SSF53807; Helical backbone' metal receptor; 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
//