NIFK_KLEPN
ID NIFK_KLEPN Reviewed; 520 AA.
AC P09772; P09771;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 03-AUG-2022, entry version 111.
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 Klebsiella pneumoniae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3062178; DOI=10.1016/0022-2836(88)90205-7;
RA Arnold W., Rump A., Klipp W., Priefer U.B., Puehler A.;
RT "Nucleotide sequence of a 24,206-base-pair DNA fragment carrying the entire
RT nitrogen fixation gene cluster of Klebsiella pneumoniae.";
RL J. Mol. Biol. 203:715-738(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3043382; DOI=10.1093/nar/16.14.7199;
RA Steinbauer J., Wenzel W., Hess D.;
RT "Nucleotide and deduced amino acid sequences of the Klebsiella pneumoniae
RT nifK gene coding for the beta-subunit of nitrogenase MoFe protein.";
RL Nucleic Acids Res. 16:7199-7199(1988).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3322261; DOI=10.1042/bj2470277;
RA Holland D., Zilberstein A., Zamir A., Sussman J.L.;
RT "A quantitative approach to sequence comparisons of nitrogenase MoFe
RT protein alpha- and beta-subunits including the newly sequenced nifK gene
RT from Klebsiella pneumoniae.";
RL Biochem. J. 247:277-285(1987).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3211766; DOI=10.1093/nar/16.24.11843;
RA Lignon J.M., Nakas J.P.;
RT "Nucleotide sequence of nifK and partial sequence of nifD from Frankia
RT species strain FaC1.";
RL Nucleic Acids Res. 16:11843-11843(1988).
RN [5]
RP ERRATUM OF PUBMED:3211766, AND CORRECTION OF ORGANISM GIVEN IN
RP PUBMED:3211766.
RA Lignon J.M., Nakas J.P.;
RL Nucleic Acids Res. 18:1097-1097(1990).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) OF 3-480.
RX PubMed=10525412; DOI=10.1006/jmbi.1999.3107;
RA Mayer S.M., Lawson D.M., Gormal C.A., Roe S.M., Smith B.E.;
RT "New insights into structure-function relationships in nitrogenase: a 1.6 A
RT resolution X-ray crystallographic study of Klebsiella pneumoniae MoFe-
RT protein.";
RL J. Mol. Biol. 292:871-891(1999).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 3-483.
RX PubMed=12133839; DOI=10.1074/jbc.m205888200;
RA Mayer S.M., Gormal C.A., Smith B.E., Lawson D.M.;
RT "Crystallographic analysis of the MoFe protein of nitrogenase from a nifV
RT mutant of Klebsiella pneumoniae identifies citrate as a ligand to the
RT molybdenum of iron molybdenum cofactor (FeMoco).";
RL J. Biol. Chem. 277:35263-35266(2002).
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}.
CC -!- CAUTION: The authors of PubMed:3211766 originally stated that their
CC sequence was from Frankia sp. {ECO:0000305}.
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DR EMBL; X13303; CAA31668.1; -; Genomic_DNA.
DR EMBL; X07749; CAA30573.1; -; Genomic_DNA.
DR EMBL; X06243; CAA29588.1; -; Genomic_DNA.
DR EMBL; X12649; CAA31180.1; -; Genomic_DNA.
DR PIR; S02505; S02505.
DR PDB; 1H1L; X-ray; 1.90 A; B/D=2-520.
DR PDB; 1QGU; X-ray; 1.60 A; B/D=2-520.
DR PDB; 1QH1; X-ray; 1.60 A; B/D=2-520.
DR PDB; 1QH8; X-ray; 1.60 A; B/D=2-520.
DR PDBsum; 1H1L; -.
DR PDBsum; 1QGU; -.
DR PDBsum; 1QH1; -.
DR PDBsum; 1QH8; -.
DR AlphaFoldDB; P09772; -.
DR SMR; P09772; -.
DR DIP; DIP-6207N; -.
DR BioCyc; MetaCyc:NIFKKLEB-MON; -.
DR BRENDA; 1.18.6.1; 2814.
DR EvolutionaryTrace; P09772; -.
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 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Iron; Iron-sulfur; Metal-binding;
KW Nitrogen fixation; Nucleotide-binding; Oxidoreductase.
FT CHAIN 1..520
FT /note="Nitrogenase molybdenum-iron protein beta chain"
FT /id="PRO_0000153101"
FT BINDING 69
FT /ligand="[8Fe-7S] cluster"
FT /ligand_id="ChEBI:CHEBI:21143"
FT /ligand_note="ligand shared with alpha chain"
FT BINDING 94
FT /ligand="[8Fe-7S] cluster"
FT /ligand_id="ChEBI:CHEBI:21143"
FT /ligand_note="ligand shared with alpha chain"
FT BINDING 152
FT /ligand="[8Fe-7S] cluster"
FT /ligand_id="ChEBI:CHEBI:21143"
FT /ligand_note="ligand shared with alpha chain"
FT BINDING 187
FT /ligand="[8Fe-7S] cluster"
FT /ligand_id="ChEBI:CHEBI:21143"
FT /ligand_note="ligand shared with alpha chain"
FT CONFLICT 24
FT /note="F -> V (in Ref. 4; CAA31180)"
FT /evidence="ECO:0000305"
FT CONFLICT 33
FT /note="A -> R (in Ref. 4; CAA31180)"
FT /evidence="ECO:0000305"
FT CONFLICT 57..58
FT /note="RR -> H (in Ref. 4; CAA31180)"
FT /evidence="ECO:0000305"
FT CONFLICT 57
FT /note="R -> Q (in Ref. 2 and 3)"
FT /evidence="ECO:0000305"
FT CONFLICT 70..71
FT /note="QP -> HA (in Ref. 4; CAA31180)"
FT /evidence="ECO:0000305"
FT CONFLICT 99
FT /note="R -> G (in Ref. 4; CAA31180)"
FT /evidence="ECO:0000305"
FT CONFLICT 163
FT /note="A -> R (in Ref. 4; CAA31180)"
FT /evidence="ECO:0000305"
FT CONFLICT 180
FT /note="V -> W (in Ref. 4; CAA31180)"
FT /evidence="ECO:0000305"
FT CONFLICT 221
FT /note="L -> LKL (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 225
FT /note="T -> P (in Ref. 4; CAA31180)"
FT /evidence="ECO:0000305"
FT CONFLICT 232
FT /note="G -> GTG (in Ref. 4)"
FT /evidence="ECO:0000305"
FT CONFLICT 265
FT /note="H -> Q (in Ref. 4; CAA31180)"
FT /evidence="ECO:0000305"
FT CONFLICT 287..290
FT /note="TLLL -> AAP (in Ref. 3; CAA29588)"
FT /evidence="ECO:0000305"
FT CONFLICT 351..352
FT /note="MM -> IV (in Ref. 3; CAA29588)"
FT /evidence="ECO:0000305"
FT CONFLICT 357
FT /note="Missing (in Ref. 3; CAA29588)"
FT /evidence="ECO:0000305"
FT CONFLICT 395..400
FT /note="ANKRWQ -> GQQTLD (in Ref. 3; CAA29588)"
FT /evidence="ECO:0000305"
FT CONFLICT 411
FT /note="P -> R (in Ref. 3; CAA29588)"
FT /evidence="ECO:0000305"
FT CONFLICT 412..417
FT /note="YGRDSE -> NRARYS (in Ref. 4; CAA31180)"
FT /evidence="ECO:0000305"
FT CONFLICT 422
FT /note="C -> R (in Ref. 3; CAA29588)"
FT /evidence="ECO:0000305"
FT CONFLICT 435..438
FT /note="QPDF -> SAGL (in Ref. 3; CAA29588)"
FT /evidence="ECO:0000305"
FT CONFLICT 451
FT /note="D -> V (in Ref. 4; CAA31180)"
FT /evidence="ECO:0000305"
FT CONFLICT 482
FT /note="W -> S (in Ref. 3; CAA29588)"
FT /evidence="ECO:0000305"
FT CONFLICT 497
FT /note="A -> V (in Ref. 3; CAA29588)"
FT /evidence="ECO:0000305"
FT CONFLICT 508..509
FT /note="QL -> PA (in Ref. 3; CAA29588)"
FT /evidence="ECO:0000305"
FT CONFLICT 510
FT /note="G -> A (in Ref. 4; CAA31180)"
FT /evidence="ECO:0000305"
FT HELIX 11..14
FT /evidence="ECO:0007829|PDB:1QGU"
FT HELIX 18..28
FT /evidence="ECO:0007829|PDB:1QGU"
FT TURN 29..32
FT /evidence="ECO:0007829|PDB:1QGU"
FT HELIX 36..46
FT /evidence="ECO:0007829|PDB:1QGU"
FT HELIX 49..55
FT /evidence="ECO:0007829|PDB:1QGU"
FT STRAND 62..64
FT /evidence="ECO:0007829|PDB:1QGU"
FT HELIX 70..79
FT /evidence="ECO:0007829|PDB:1QGU"
FT STRAND 84..90
FT /evidence="ECO:0007829|PDB:1QGU"
FT HELIX 92..106
FT /evidence="ECO:0007829|PDB:1QGU"
FT HELIX 121..124
FT /evidence="ECO:0007829|PDB:1QGU"
FT HELIX 127..141
FT /evidence="ECO:0007829|PDB:1QGU"
FT STRAND 144..150
FT /evidence="ECO:0007829|PDB:1QGU"
FT HELIX 152..157
FT /evidence="ECO:0007829|PDB:1QGU"
FT HELIX 161..170
FT /evidence="ECO:0007829|PDB:1QGU"
FT HELIX 192..208
FT /evidence="ECO:0007829|PDB:1QGU"
FT STRAND 217..224
FT /evidence="ECO:0007829|PDB:1QGU"
FT HELIX 231..244
FT /evidence="ECO:0007829|PDB:1QGU"
FT STRAND 248..252
FT /evidence="ECO:0007829|PDB:1QGU"
FT TURN 254..258
FT /evidence="ECO:0007829|PDB:1QGU"
FT HELIX 275..280
FT /evidence="ECO:0007829|PDB:1QGU"
FT HELIX 281..283
FT /evidence="ECO:0007829|PDB:1QGU"
FT STRAND 284..291
FT /evidence="ECO:0007829|PDB:1QGU"
FT TURN 292..294
FT /evidence="ECO:0007829|PDB:1QGU"
FT HELIX 296..304
FT /evidence="ECO:0007829|PDB:1QGU"
FT HELIX 319..333
FT /evidence="ECO:0007829|PDB:1QGU"
FT HELIX 339..359
FT /evidence="ECO:0007829|PDB:1QGU"
FT STRAND 363..368
FT /evidence="ECO:0007829|PDB:1QGU"
FT HELIX 370..382
FT /evidence="ECO:0007829|PDB:1QGU"
FT STRAND 386..392
FT /evidence="ECO:0007829|PDB:1QGU"
FT HELIX 397..409
FT /evidence="ECO:0007829|PDB:1QGU"
FT STRAND 417..421
FT /evidence="ECO:0007829|PDB:1QGU"
FT HELIX 424..434
FT /evidence="ECO:0007829|PDB:1QGU"
FT STRAND 437..441
FT /evidence="ECO:0007829|PDB:1QGU"
FT HELIX 443..445
FT /evidence="ECO:0007829|PDB:1QGU"
FT HELIX 446..455
FT /evidence="ECO:0007829|PDB:1QGU"
FT HELIX 457..459
FT /evidence="ECO:0007829|PDB:1QGU"
FT STRAND 463..465
FT /evidence="ECO:0007829|PDB:1QGU"
FT STRAND 472..475
FT /evidence="ECO:0007829|PDB:1QGU"
FT HELIX 476..478
FT /evidence="ECO:0007829|PDB:1QGU"
FT HELIX 483..505
FT /evidence="ECO:0007829|PDB:1QGU"
FT TURN 509..511
FT /evidence="ECO:0007829|PDB:1QGU"
FT HELIX 513..515
FT /evidence="ECO:0007829|PDB:1QGU"
SQ SEQUENCE 520 AA; 58408 MW; F51C455ECD0DF5C9 CRC64;
MSQTIDKINS CYPLFEQDEY QELFRNKRQL EEAHDAQRVQ EVFAWTTTAE YEALNFRREA
LTVDPAKACQ PLGAVLCSLG FANTLPYVHG SQGCVAYFRT YFNRHFKEPI ACVSDSMTED
AAVFGGNNNM NLGLQNASAL YKPEIIAVST TCMAEVIGDD LQAFIANAKK DGFVDSSIAV
PHAHTPSFIG SHVTGWDNMF EGFAKTFTAD YQGQPGKLPK LNLVTGFETY LGNFRVLKRM
MEQMAVPCSL LSDPSEVLDT PADGHYRMYS GGTTQQEMKE APDAIDTLLL QPWQLLKSKK
VVQEMWNQPA TEVAIPLGLA ATDELLMTVS QLSGKPIADA LTLERGRLVD MMLDSHTWLH
GKKFGLYGDP DFVMGLTRFL LELGCEPTVI LSHNANKRWQ KAMNKMLDAS PYGRDSEVFI
NCDLWHFRSL MFTRQPDFMI GNSYGKFIQR DTLAKGKAFE VPLIRLGFPL FDRHHLHRQT
TWGYEGAMNI VTTLVNAVLE KLDSDTSQLG KTDYSFDLVR
