NIFK_METTH
ID NIFK_METTH Reviewed; 459 AA.
AC O27606;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JAN-1998, sequence version 1.
DT 03-AUG-2022, entry version 113.
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=MTH_1564;
OS Methanothermobacter thermautotrophicus (strain ATCC 29096 / DSM 1053 / JCM
OS 10044 / NBRC 100330 / Delta H) (Methanobacterium thermoautotrophicum).
OC Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX NCBI_TaxID=187420;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 29096 / DSM 1053 / JCM 10044 / NBRC 100330 / Delta H;
RX PubMed=9371463; DOI=10.1128/jb.179.22.7135-7155.1997;
RA Smith D.R., Doucette-Stamm L.A., Deloughery C., Lee H.-M., Dubois J.,
RA Aldredge T., Bashirzadeh R., Blakely D., Cook R., Gilbert K., Harrison D.,
RA Hoang L., Keagle P., Lumm W., Pothier B., Qiu D., Spadafora R., Vicare R.,
RA Wang Y., Wierzbowski J., Gibson R., Jiwani N., Caruso A., Bush D.,
RA Safer H., Patwell D., Prabhakar S., McDougall S., Shimer G., Goyal A.,
RA Pietrovski S., Church G.M., Daniels C.J., Mao J.-I., Rice P., Noelling J.,
RA Reeve J.N.;
RT "Complete genome sequence of Methanobacterium thermoautotrophicum deltaH:
RT functional analysis and comparative genomics.";
RL J. Bacteriol. 179:7135-7155(1997).
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}.
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; AE000666; AAB86038.1; -; Genomic_DNA.
DR PIR; G69075; G69075.
DR RefSeq; WP_010877173.1; NC_000916.1.
DR AlphaFoldDB; O27606; -.
DR SMR; O27606; -.
DR STRING; 187420.MTH_1564; -.
DR EnsemblBacteria; AAB86038; AAB86038; MTH_1564.
DR GeneID; 1471833; -.
DR KEGG; mth:MTH_1564; -.
DR PATRIC; fig|187420.15.peg.1527; -.
DR HOGENOM; CLU_025876_2_0_2; -.
DR OMA; GLNNMID; -.
DR Proteomes; UP000005223; 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; IPR000318; Nase_comp1_CS.
DR Pfam; PF00148; Oxidored_nitro; 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..459
FT /note="Nitrogenase molybdenum-iron protein beta chain"
FT /id="PRO_0000153104"
FT BINDING 21
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 46
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 104
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 143
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 459 AA; 51490 MW; F2CB731BCC675AC9 CRC64;
MSEINVMERT RELVVNPLVT CQPFGAMFAT LGIRRGLPIV HGSQGCSTFV RYGLNRHFRE
PAEIAVTSLH EDAAVFGGRS NLIDGVKNLV KRFRPELVGI VTTCSSEITG DDVDGFLRVA
EAELREELGE RFRTRMVSIS TPSFVEHHLR GYGNALKSFI DTLAVDEGDC NERINLIPGI
VNPGDIREIR HIFELMDVDP IILTDTSDPF DSPLRPSKTE KMPFYPKGGT VVSDIEESSN
SIGTLSMSMY GNEASETLKK RFNIPKEHHI PIGVRNTDDF VRSLARIAEV DVSEELLDER
GILIDSMADI SSRYLFGRTA AVYGDPDMVM GVSRFLCELG ITPLYACVGV DNEIFREGMK
RVASEADERI NVMINSDLRA LERELTEEPV DFMIGNSDGR LIARDLGIPL VRMGFPVYDR
VGYHRIPVVG YRGSVNLLNR ITNTVLREYY EPQHWKLQQ