NIFK_CLOPA
ID NIFK_CLOPA Reviewed; 458 AA.
AC P11347;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 109.
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 Clostridium pasteurianum.
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1501;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 6013 / DSM 525 / NCIB 9486 / VKM B-1774 / W5;
RX PubMed=2840948; DOI=10.1021/bi00408a021;
RA Wang S.-Z., Chen J.-S., Johnson J.L.;
RT "Distinct structural features of the alpha and beta subunits of nitrogenase
RT molybdenum-iron protein of Clostridium pasteurianum: an analysis of amino
RT acid sequences.";
RL Biochemistry 27:2800-2810(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-11.
RX PubMed=3473447; DOI=10.1093/nar/15.9.3935;
RA Wang S.-Z., Chen J.-S., Johnson J.L.;
RT "Nucleotide and deduced amino acid sequences of nifD encoding the alpha-
RT subunit of nitrogenase MoFe protein of Clostridium pasteurianum.";
RL Nucleic Acids Res. 15:3935-3935(1987).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=8393705; DOI=10.1021/bi00079a006;
RA Kim J., Woo D., Rees D.C.;
RT "X-ray crystal structure of the nitrogenase molybdenum-iron protein from
RT Clostridium pasteurianum at 3.0-A resolution.";
RL Biochemistry 32:7104-7115(1993).
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;
CC Note=Binds 1 [8Fe-7S] cluster per heterodimer.;
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; AY603957; AAA23266.2; -; Genomic_DNA.
DR PIR; A29992; NICLMB.
DR RefSeq; WP_003447875.1; NZ_LFYL01000003.1.
DR PDB; 1MIO; X-ray; 3.00 A; B/D=1-458.
DR PDB; 4WES; X-ray; 1.08 A; B/D=1-458.
DR PDB; 4WN9; X-ray; 1.90 A; B/D=1-458.
DR PDB; 5VPW; X-ray; 1.85 A; B/D=1-458.
DR PDB; 5VQ3; X-ray; 1.72 A; B/D=1-458.
DR PDBsum; 1MIO; -.
DR PDBsum; 4WES; -.
DR PDBsum; 4WN9; -.
DR PDBsum; 5VPW; -.
DR PDBsum; 5VQ3; -.
DR AlphaFoldDB; P11347; -.
DR SMR; P11347; -.
DR PRIDE; P11347; -.
DR BioCyc; MetaCyc:NIFKCP-MON; -.
DR BRENDA; 1.18.6.1; 1502.
DR EvolutionaryTrace; P11347; -.
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 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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Iron; Iron-sulfur; Metal-binding;
KW Nitrogen fixation; Nucleotide-binding; Oxidoreductase.
FT CHAIN 1..458
FT /note="Nitrogenase molybdenum-iron protein beta chain"
FT /id="PRO_0000153097"
FT BINDING 23
FT /ligand="[8Fe-7S] cluster"
FT /ligand_id="ChEBI:CHEBI:21143"
FT /ligand_note="ligand shared with alpha chain"
FT BINDING 48
FT /ligand="[8Fe-7S] cluster"
FT /ligand_id="ChEBI:CHEBI:21143"
FT /ligand_note="ligand shared with alpha chain"
FT BINDING 106
FT /ligand="[8Fe-7S] cluster"
FT /ligand_id="ChEBI:CHEBI:21143"
FT /ligand_note="ligand shared with alpha chain"
FT BINDING 141
FT /ligand="[8Fe-7S] cluster"
FT /ligand_id="ChEBI:CHEBI:21143"
FT /ligand_note="ligand shared with alpha chain"
FT STRAND 16..20
FT /evidence="ECO:0007829|PDB:4WES"
FT HELIX 24..33
FT /evidence="ECO:0007829|PDB:4WES"
FT STRAND 38..44
FT /evidence="ECO:0007829|PDB:4WES"
FT HELIX 46..60
FT /evidence="ECO:0007829|PDB:4WES"
FT HELIX 73..78
FT /evidence="ECO:0007829|PDB:4WES"
FT HELIX 81..95
FT /evidence="ECO:0007829|PDB:4WES"
FT STRAND 98..104
FT /evidence="ECO:0007829|PDB:4WES"
FT HELIX 106..111
FT /evidence="ECO:0007829|PDB:4WES"
FT HELIX 115..125
FT /evidence="ECO:0007829|PDB:4WES"
FT STRAND 133..136
FT /evidence="ECO:0007829|PDB:4WES"
FT HELIX 146..161
FT /evidence="ECO:0007829|PDB:4WES"
FT STRAND 172..175
FT /evidence="ECO:0007829|PDB:4WES"
FT HELIX 181..193
FT /evidence="ECO:0007829|PDB:4WES"
FT STRAND 198..202
FT /evidence="ECO:0007829|PDB:4WES"
FT TURN 205..207
FT /evidence="ECO:0007829|PDB:4WES"
FT HELIX 226..231
FT /evidence="ECO:0007829|PDB:4WES"
FT HELIX 232..234
FT /evidence="ECO:0007829|PDB:4WES"
FT STRAND 236..242
FT /evidence="ECO:0007829|PDB:4WES"
FT HELIX 243..257
FT /evidence="ECO:0007829|PDB:4WES"
FT STRAND 261..264
FT /evidence="ECO:0007829|PDB:4WES"
FT HELIX 270..284
FT /evidence="ECO:0007829|PDB:4WES"
FT HELIX 290..305
FT /evidence="ECO:0007829|PDB:4WES"
FT HELIX 307..309
FT /evidence="ECO:0007829|PDB:4WES"
FT TURN 310..312
FT /evidence="ECO:0007829|PDB:4WES"
FT STRAND 314..319
FT /evidence="ECO:0007829|PDB:4WES"
FT HELIX 321..333
FT /evidence="ECO:0007829|PDB:4WES"
FT STRAND 337..345
FT /evidence="ECO:0007829|PDB:4WES"
FT HELIX 348..360
FT /evidence="ECO:0007829|PDB:4WES"
FT STRAND 367..370
FT /evidence="ECO:0007829|PDB:4WES"
FT HELIX 374..383
FT /evidence="ECO:0007829|PDB:4WES"
FT STRAND 387..392
FT /evidence="ECO:0007829|PDB:4WES"
FT HELIX 393..395
FT /evidence="ECO:0007829|PDB:4WES"
FT HELIX 396..402
FT /evidence="ECO:0007829|PDB:4WES"
FT STRAND 406..408
FT /evidence="ECO:0007829|PDB:4WES"
FT STRAND 415..418
FT /evidence="ECO:0007829|PDB:5VQ3"
FT HELIX 419..421
FT /evidence="ECO:0007829|PDB:4WES"
FT HELIX 426..448
FT /evidence="ECO:0007829|PDB:4WES"
FT HELIX 451..453
FT /evidence="ECO:0007829|PDB:4WES"
SQ SEQUENCE 458 AA; 50119 MW; FECFB097C7CC9068 CRC64;
MLDATPKEIV ERKALRINPA KTCQPVGAMY AALGIHNCLP HSHGSQGCCS YHRTVLSRHF
KEPAMASTSS FTEGASVFGG GSNIKTAVKN IFSLYNPDII AVHTTCLSET LGDDLPTYIS
QMEDAGSIPE GKLVIHTNTP SYVGSHVTGF ANMVQGIVNY LSENTGAKNG KINVIPGFVG
PADMREIKRL FEAMDIPYIM FPDTSGVLDG PTTGEYKMYP EGGTKIEDLK DTGNSDLTLS
LGSYASDLGA KTLEKKCKVP FKTLRTPIGV SATDEFIMAL SEATGKEVPA SIEEERGQLI
DLMIDAQQYL QGKKVALLGD PDEIIALSKF IIELGAIPKY VVTGTPGMKF QKEIDAMLAE
AGIEGSKVKV EGDFFDVHQW IKNEGVDLLI SNTYGKFIAR EENIPFVRFG FPIMDRYGHY
YNPKVGYKGA IRLVEEITNV ILDKIERECT EEDFEVVR
