ID   NIFK_ACIFI              Reviewed;         518 AA.
AC   P15052;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-APR-1990, sequence version 1.
DT   03-AUG-2022, entry version 84.
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;
OS   Acidithiobacillus ferridurans.
OC   Bacteria; Proteobacteria; Acidithiobacillia; Acidithiobacillales;
OC   Acidithiobacillaceae; Acidithiobacillus.
OX   NCBI_TaxID=1232575;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC 33020 / DSM 29468 / JCM 18981 / 11Fe;
RX   PubMed=3234769; DOI=10.1016/0378-1119(88)90444-1;
RA   Rawlings D.E.;
RT   "Sequence and structural analysis of the alpha- and beta-dinitrogenase
RT   subunits of Thiobacillus ferrooxidans.";
RL   Gene 69:337-343(1988).
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   -!- SIMILARITY: Belongs to the NifD/NifK/NifE/NifN family. {ECO:0000305}.
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DR   EMBL; M15238; AAA27376.1; -; Genomic_DNA.
DR   PIR; JT0341; NIBCBT.
DR   AlphaFoldDB; P15052; -.
DR   SMR; P15052; -.
DR   PRIDE; P15052; -.
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.
FT   CHAIN           1..518
FT                   /note="Nitrogenase molybdenum-iron protein beta chain"
FT                   /id="PRO_0000153110"
FT   BINDING         70
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   BINDING         187
FT                   /ligand="[8Fe-7S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21143"
FT                   /ligand_note="ligand shared with alpha chain"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   518 AA;  57893 MW;  B273250124813430 CRC64;
     MSQNADKIVD HFNLFKQPDY QEMFKNKQKT FENRLPADQV ARGQEWTKTW EYREKNFARE
     ALSVNPDKAC QPLGRIFARG FDGTRPFVHG SQGCVAYFRS HFNRHFKEPS SCVSSSMTED
     PAVFGGLNNM IDGLAISYSL YKPKMIAVST TCMAEVIGDD LNAFIKTAKE KGNVPESFDV
     PFAHTPSFVG SHITGYDNMM KGILTHFWDG KAGTVPALER KPDEKINFIG GFDGYTVGNM
     REIKRLFSLM NVDYTILGDG SDVWDTPADG EFRMYDGGTT FAEAEAALNA KATVCMQGIS
     TEKTMAYIQE KGQEVVALHC PIGVTGTDHF LQEVSGISGK PISEELKKER GRLVDAIGTS
     ISYLHGKKFA IKGDPDFCLG VAGFLLELGA EPVHVVCTRG NKDWAEKMNA LFASSPFGTG
     CHAYPGKDLW HMRSLVFTEP VDFLIGNSYT KYLERDTGTP MIHIGFPIHD RHHHHRYPIW
     GYQGAVNVLV WILDRIHLEL DRNTLGIGTT DFSYDLVR