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NIFK_METTM
ID   NIFK_METTM              Reviewed;         459 AA.
AC   P95296; D9PU61;
DT   30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 93.
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=MTBMA_c01500;
OS   Methanothermobacter marburgensis (strain ATCC BAA-927 / DSM 2133 / JCM
OS   14651 / NBRC 100331 / OCM 82 / Marburg) (Methanobacterium
OS   thermoautotrophicum).
OC   Archaea; Euryarchaeota; Methanomada group; Methanobacteria;
OC   Methanobacteriales; Methanobacteriaceae; Methanothermobacter.
OX   NCBI_TaxID=79929;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RA   Hochheimer A.;
RL   Submitted (FEB-1997) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-927 / DSM 2133 / JCM 14651 / NBRC 100331 / OCM 82 /
RC   Marburg;
RX   PubMed=20802048; DOI=10.1128/jb.00844-10;
RA   Liesegang H., Kaster A.K., Wiezer A., Goenrich M., Wollherr A., Seedorf H.,
RA   Gottschalk G., Thauer R.K.;
RT   "Complete genome sequence of Methanothermobacter marburgensis, a
RT   methanoarchaeon model organism.";
RL   J. Bacteriol. 192:5850-5851(2010).
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; X87971; CAA61220.1; -; Genomic_DNA.
DR   EMBL; CP001710; ADL57759.1; -; Genomic_DNA.
DR   RefSeq; WP_013294987.1; NC_014408.1.
DR   AlphaFoldDB; P95296; -.
DR   SMR; P95296; -.
DR   STRING; 79929.MTBMA_c01500; -.
DR   PRIDE; P95296; -.
DR   EnsemblBacteria; ADL57759; ADL57759; MTBMA_c01500.
DR   GeneID; 9703855; -.
DR   KEGG; mmg:MTBMA_c01500; -.
DR   PATRIC; fig|79929.8.peg.146; -.
DR   HOGENOM; CLU_025876_2_0_2; -.
DR   OMA; GLNNMID; -.
DR   OrthoDB; 15283at2157; -.
DR   Proteomes; UP000000345; 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.
FT   CHAIN           1..459
FT                   /note="Nitrogenase molybdenum-iron protein beta chain"
FT                   /id="PRO_0000153105"
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;  51158 MW;  04FC3EA9CE3E9E37 CRC64;
     MPEINVMERG RELVVNPLVT CQPFGAMFAT LGIRRGLPLV HGSQGCSTFV RYGLNRHFRE
     PAEIAVTSLH EDAAVFGGRS NIINGVKNLV KRFRPDLVGI VTTCSSEIIG DDVDGFMRVA
     ETELREELGD RFQTKLVHIS TPSFVENHFR GYGNAIKSFI ETLSREDGDC NHKLNIIPGI
     VNPGDIREIG HMLGLMDITP IILTDTSDPF DSPLRPSKTE QMPFYPPGGT AVPEIEDSSN
     SMGTLSLTMY GDEALNTLEK RFRVPGEYSM PIGVRNTDDF VRRAARISEK DVSDELLDER
     GILIDSMADL SSRYLFGRTA AVYGDPDMVA GISRFLCELG ITPLHTCTGT DNELFIDRMK
     TVAAEADERI NVMVKSDLRA LEERLSEEPV DLMIGNSDGR LIAQDLGIPL VRVGYPVYDR
     VGYQRVPITG YRGAVNLLNR ITNTVLREYY EPQHWKLQQ
 
 
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