NIFK_BRADU
ID NIFK_BRADU Reviewed; 518 AA.
AC P20621; Q9ANN4;
DT 01-FEB-1991, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2003, sequence version 3.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=Nitrogenase molybdenum-iron protein beta chain;
DE EC=1.18.6.1;
DE AltName: Full=Dinitrogenase;
DE AltName: Full=Nitrogenase component I;
GN Name=nifK; OrderedLocusNames=blr1744;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RA Thoeny B., Kaluza K., Hennecke H.;
RT "Structural and functional homology between the alpha and beta subunits of
RT the nitrogenase MoFe protein as revealed by sequencing the Rhizobium
RT japonicum nifK gene.";
RL Mol. Gen. Genet. 198:441-448(1985).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=USDA 110spc4;
RX PubMed=11157954; DOI=10.1128/jb.183.4.1405-1412.2001;
RA Goettfert M., Roethlisberger S., Kuendig C., Beck C., Marty R.,
RA Hennecke H.;
RT "Potential symbiosis-specific genes uncovered by sequencing a 410-kb DNA
RT region of the Bradyrhizobium japonicum chromosome.";
RL J. Bacteriol. 183:1405-1412(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-44.
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RA Kaluza K., Hennecke H.;
RT "Fine structure analysis of the nifDK operon encoding the alpha and beta
RT subunits of dinitrogenase from Rhizobium japonicum.";
RL Mol. Gen. Genet. 196:35-42(1984).
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 -!- SUBUNIT: Tetramer of two alpha and two beta chains. Forms complex with
CC the iron protein (nitrogenase component 2).
CC -!- MISCELLANEOUS: Ala-187 is present instead of the usual Ser that would
CC serve as a ligand for the 8Fe-7S cluster in the oxidized state.
CC -!- SIMILARITY: Belongs to the NifD/NifK/NifE/NifN family. {ECO:0000305}.
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DR EMBL; M64591; AAA26326.1; -; Genomic_DNA.
DR EMBL; AF322012; AAG60730.1; -; Genomic_DNA.
DR EMBL; BA000040; BAC47009.1; -; Genomic_DNA.
DR EMBL; X01045; CAA25524.1; -; Genomic_DNA.
DR PIR; S09548; S09548.
DR RefSeq; NP_768384.1; NC_004463.1.
DR RefSeq; WP_011084553.1; NZ_CP011360.1.
DR AlphaFoldDB; P20621; -.
DR SMR; P20621; -.
DR STRING; 224911.27349997; -.
DR EnsemblBacteria; BAC47009; BAC47009; BAC47009.
DR GeneID; 64067051; -.
DR KEGG; bja:blr1744; -.
DR PATRIC; fig|224911.44.peg.1209; -.
DR eggNOG; COG2710; Bacteria.
DR HOGENOM; CLU_025876_2_0_5; -.
DR InParanoid; P20621; -.
DR OMA; GLNNMID; -.
DR PhylomeDB; P20621; -.
DR Proteomes; UP000002526; Chromosome.
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 InterPro; IPR000510; Nase/OxRdtase_comp1.
DR InterPro; IPR000318; Nase_comp1_CS.
DR InterPro; IPR005976; Nase_Mo-Fe_CF_bsu.
DR InterPro; IPR024564; Nase_Mo-Fe_CF_bsu_N.
DR Pfam; PF11844; DUF3364; 1.
DR Pfam; PF00148; Oxidored_nitro; 1.
DR TIGRFAMs; TIGR01286; nifK; 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; Nitrogen fixation;
KW Nucleotide-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..518
FT /note="Nitrogenase molybdenum-iron protein beta chain"
FT /id="PRO_0000153094"
FT BINDING 69
FT /ligand="[8Fe-7S] cluster"
FT /ligand_id="ChEBI:CHEBI:21143"
FT /ligand_note="ligand shared with alpha chain"
FT /evidence="ECO:0000250"
FT BINDING 94
FT /ligand="[8Fe-7S] cluster"
FT /ligand_id="ChEBI:CHEBI:21143"
FT /ligand_note="ligand shared with alpha chain"
FT /evidence="ECO:0000250"
FT BINDING 152
FT /ligand="[8Fe-7S] cluster"
FT /ligand_id="ChEBI:CHEBI:21143"
FT /ligand_note="ligand shared with alpha chain"
FT /evidence="ECO:0000250"
FT CONFLICT 477
FT /note="S -> F (in Ref. 1; AAA26326)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 518 AA; 57433 MW; 6005D1230A4D083D CRC64;
MPQSAEHVLD HVELFRGPEY QQMLAKKKIF ENPRDPAEVE RIKEWTKTAE YREKNFAREA
LAVNPAKACQ PLGAVFASVG FERTLPFVHG SQGCVAYYRS HLSRHFKEPS SCVSSSMTED
AAVFGGLNNM TDGLANSYKM YKPKMIAVST TCMAEVIGDD LNAFIKTSKE KGSVPADFDV
PFAHTPAFVG SHVTGYDNAL KGILEHFWDG KAGTAPKLER KPNGAINIIG GFDGYTVGNL
REIKRILELM GIQHTVLADN SEVFDTPTDG EFRMYDGGTT LKDAANAIHA KATISMQQWC
TEKTLSFAAE HGQDVLSFNY PVGLSATDDF IVALSRISGK EIPEQLARER GRLVDAIADS
SAHVHGKKFA IYGDPDLCYG LAAFLLELGA EPTHVLSTNG NKAWQEKMQA LLASSPFGQG
CQVYPGRDLW HMRSLLFTEP VDFLIGNTYG KYLERDTATP LIRIGFPIFD RHHHHRSPIW
GYQGGLNVLV KILDKIFDEI DNKTNILGKT DYSFDIIR
