NIFK_AZOVI
ID NIFK_AZOVI Reviewed; 523 AA.
AC P07329;
DT 01-APR-1988, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 131.
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 Azotobacter vinelandii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=354;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIMB 11614 / LMG 3878 / UW;
RX PubMed=2644218; DOI=10.1128/jb.171.2.1017-1027.1989;
RA Jacobson M.R., Brigle K.E., Bennett L.T., Setterquist R.A., Wilson M.S.,
RA Cash V.L., Beynon J., Newton W.E., Dean D.R.;
RT "Physical and genetic map of the major nif gene cluster from Azotobacter
RT vinelandii.";
RL J. Bacteriol. 171:1017-1027(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIMB 11614 / LMG 3878 / UW;
RX PubMed=3863780; DOI=10.1016/0378-1119(85)90255-0;
RA Brigle K.E., Newton W.E., Dean D.R.;
RT "Complete nucleotide sequence of the Azotobacter vinelandii nitrogenase
RT structural gene cluster.";
RL Gene 37:37-44(1985).
RN [3]
RP PROTEIN SEQUENCE OF 2-20 AND 521-523.
RX PubMed=649581; DOI=10.1016/s0021-9258(17)34817-2;
RA Lundell D.J., Howard J.B.;
RT "Isolation and partial characterization of two different subunits from the
RT molybdenum-iron protein of Azotobacter vinelandii nitrogenase.";
RL J. Biol. Chem. 253:3422-3426(1978).
RN [4]
RP ACTIVITY REGULATION, AND INDUCTION.
RC STRAIN=CA;
RX PubMed=7830548; DOI=10.1111/j.1365-2958.1994.tb01270.x;
RA Moshiri F., Kim J.W., Fu C., Maier R.J.;
RT "The FeSII protein of Azotobacter vinelandii is not essential for aerobic
RT nitrogen fixation, but confers significant protection to oxygen-mediated
RT inactivation of nitrogenase in vitro and in vivo.";
RL Mol. Microbiol. 14:101-114(1994).
RN [5]
RP X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
RA Kim J., Rees D.C.;
RT "Crystallographic structure and functional implications of the nitrogenase
RT molybdenum-iron protein from Azotobacter vinelandii.";
RL Nature 360:553-560(1992).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
RX PubMed=9163420; DOI=10.1038/387370a0;
RA Schindelin H., Kisker C., Schlessman J.L., Howard J.B., Rees D.C.;
RT "Structure of ADP x [AlF(4)](-)-stabilized nitrogenase complex and its
RT implications for signal transduction.";
RL Nature 387:370-376(1997).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX PubMed=9063865; DOI=10.1021/bi9626665;
RA Peters J.W., Stowell M.H.B., Soltis S.M., Finnegan M.G., Johnson M.K.,
RA Rees D.C.;
RT "Redox-dependent structural changes in the nitrogenase P-cluster.";
RL Biochemistry 36:1181-1187(1997).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
RX PubMed=11170380; DOI=10.1021/bi001645e;
RA Chiu H.-J., Peters J.W., Lanzilotta W.N., Ryle M.J., Seefeldt L.C.,
RA Howard J.B., Rees D.C.;
RT "MgATP-bound and nucleotide-free structures of a nitrogenase protein
RT complex between the Leu 127Delta-Fe-protein and the MoFe-protein.";
RL Biochemistry 40:641-650(2001).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF MUTANT GLN-195.
RX PubMed=11327812; DOI=10.1021/bi0013997;
RA Soerlie M., Christiansen J., Lemon B.J., Peters J.W., Dean D.R.,
RA Hales B.J.;
RT "Mechanistic features and structure of the nitrogenase alpha-Gln195 MoFe
RT protein.";
RL Biochemistry 40:1540-1549(2001).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF CROSS-LINKED HETERODIMER WITH
RP FE-PROTEIN.
RX PubMed=12501184; DOI=10.1021/bi026642b;
RA Schmid B., Einsle O., Chiu H.J., Willing A., Yoshida M., Howard J.B.,
RA Rees D.C.;
RT "Biochemical and structural characterization of the cross-linked complex of
RT nitrogenase: comparison to the ADP-AlF4(-)-stabilized structure.";
RL Biochemistry 41:15557-15565(2002).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
RX PubMed=11951047; DOI=10.1126/science.1070010;
RA Schmid B., Ribbe M.W., Einsle O., Yoshida M., Thomas L.M., Dean D.R.,
RA Rees D.C., Burgess B.K.;
RT "Structure of a cofactor-deficient nitrogenase MoFe protein.";
RL Science 296:352-356(2002).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.16 ANGSTROMS).
RX PubMed=12215645; DOI=10.1126/science.1073877;
RA Einsle O., Tezcan F.A., Andrade S.L.A., Schmid B., Yoshida M., Howard J.B.,
RA Rees D.C.;
RT "Nitrogenase MoFe-protein at 1.16 A resolution: a central ligand in the
RT FeMo-cofactor.";
RL Science 297:1696-1700(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 -!- ACTIVITY REGULATION: Nitrogenase holoenzyme is subject to
CC 'conformational protection' by FeSII; under oxidizing conditions FeSII
CC binds to the holoenzyme and reversibly protects it from oxidation
CC (PubMed:7830548). {ECO:0000269|PubMed:7830548}.
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains. Forms complex with
CC the iron protein (nitrogenase component 2).
CC -!- INDUCTION: Constitutively expressed during log and stationary phase in
CC sucrose-limited cultures, its levels decrease during stationary phase
CC (at protein level). {ECO:0000269|PubMed:7830548}.
CC -!- SIMILARITY: Belongs to the NifD/NifK/NifE/NifN family. {ECO:0000305}.
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DR EMBL; M20568; AAA64711.1; -; Genomic_DNA.
DR EMBL; M11579; AAA22144.1; -; Genomic_DNA.
DR PIR; B43049; NIAVMB.
DR RefSeq; WP_012698833.1; NZ_FPKM01000020.1.
DR PDB; 1FP4; X-ray; 2.50 A; B/D=1-523.
DR PDB; 1G20; X-ray; 2.20 A; B/D=1-523.
DR PDB; 1G21; X-ray; 3.00 A; B/D=1-523.
DR PDB; 1L5H; X-ray; 2.30 A; B=2-523.
DR PDB; 1M1N; X-ray; 1.16 A; B/D/F/H=2-523.
DR PDB; 1M1Y; X-ray; 3.20 A; B/D/J/L=2-523.
DR PDB; 1M34; X-ray; 2.30 A; B/D/J/L=2-523.
DR PDB; 1N2C; X-ray; 3.00 A; B/D=2-523.
DR PDB; 2AFH; X-ray; 2.10 A; B/D=2-523.
DR PDB; 2AFI; X-ray; 3.10 A; B/D/J/L=2-523.
DR PDB; 2MIN; X-ray; 2.03 A; B/D=2-523.
DR PDB; 3K1A; X-ray; 2.23 A; B/D=2-523.
DR PDB; 3MIN; X-ray; 2.03 A; B/D=2-523.
DR PDB; 3U7Q; X-ray; 1.00 A; B/D=1-523.
DR PDB; 4ND8; X-ray; 2.00 A; B/D=1-523.
DR PDB; 4TKU; X-ray; 1.43 A; B/D=1-523.
DR PDB; 4TKV; X-ray; 1.50 A; B/D=1-523.
DR PDB; 4WNA; X-ray; 2.00 A; B/D=1-523.
DR PDB; 4WZA; X-ray; 1.90 A; B/D=2-523.
DR PDB; 4WZB; X-ray; 2.30 A; B/D=2-523.
DR PDB; 4XPI; X-ray; 1.97 A; B/D=2-523.
DR PDB; 5BVG; X-ray; 1.60 A; B/D=1-523.
DR PDB; 5BVH; X-ray; 1.53 A; B/D=1-523.
DR PDB; 5CX1; X-ray; 1.75 A; B/D/F/H/J/L/N/P=1-523.
DR PDB; 5VQ4; X-ray; 2.30 A; B/D=1-523.
DR PDB; 6BBL; X-ray; 1.68 A; B/D=1-523.
DR PDB; 6CDK; X-ray; 2.10 A; B/D=1-523.
DR PDB; 6O7L; X-ray; 2.26 A; B/D=1-523.
DR PDB; 6O7M; X-ray; 1.40 A; B/D=1-523.
DR PDB; 6O7N; X-ray; 1.75 A; B/D=1-523.
DR PDB; 6O7O; X-ray; 1.89 A; B/D=1-523.
DR PDB; 6O7P; X-ray; 1.70 A; B/D=1-523.
DR PDB; 6O7Q; X-ray; 2.00 A; B/D=1-523.
DR PDB; 6O7R; X-ray; 2.27 A; B/D=1-523.
DR PDB; 6O7S; X-ray; 2.27 A; B/D=1-523.
DR PDB; 6OP1; X-ray; 1.70 A; B/D=2-523.
DR PDB; 6OP2; X-ray; 1.90 A; B/D=2-523.
DR PDB; 6OP3; X-ray; 1.60 A; B/D=2-523.
DR PDB; 6OP4; X-ray; 2.30 A; B/D=2-523.
DR PDB; 6UG0; X-ray; 1.83 A; B/D=1-523.
DR PDB; 6VXT; X-ray; 1.74 A; B/D=1-523.
DR PDB; 7JRF; X-ray; 1.33 A; B/D=1-523.
DR PDBsum; 1FP4; -.
DR PDBsum; 1G20; -.
DR PDBsum; 1G21; -.
DR PDBsum; 1L5H; -.
DR PDBsum; 1M1N; -.
DR PDBsum; 1M1Y; -.
DR PDBsum; 1M34; -.
DR PDBsum; 1N2C; -.
DR PDBsum; 2AFH; -.
DR PDBsum; 2AFI; -.
DR PDBsum; 2MIN; -.
DR PDBsum; 3K1A; -.
DR PDBsum; 3MIN; -.
DR PDBsum; 3U7Q; -.
DR PDBsum; 4ND8; -.
DR PDBsum; 4TKU; -.
DR PDBsum; 4TKV; -.
DR PDBsum; 4WNA; -.
DR PDBsum; 4WZA; -.
DR PDBsum; 4WZB; -.
DR PDBsum; 4XPI; -.
DR PDBsum; 5BVG; -.
DR PDBsum; 5BVH; -.
DR PDBsum; 5CX1; -.
DR PDBsum; 5VQ4; -.
DR PDBsum; 6BBL; -.
DR PDBsum; 6CDK; -.
DR PDBsum; 6O7L; -.
DR PDBsum; 6O7M; -.
DR PDBsum; 6O7N; -.
DR PDBsum; 6O7O; -.
DR PDBsum; 6O7P; -.
DR PDBsum; 6O7Q; -.
DR PDBsum; 6O7R; -.
DR PDBsum; 6O7S; -.
DR PDBsum; 6OP1; -.
DR PDBsum; 6OP2; -.
DR PDBsum; 6OP3; -.
DR PDBsum; 6OP4; -.
DR PDBsum; 6UG0; -.
DR PDBsum; 6VXT; -.
DR PDBsum; 7JRF; -.
DR AlphaFoldDB; P07329; -.
DR SMR; P07329; -.
DR OMA; GLNNMID; -.
DR BioCyc; MetaCyc:MON-19494; -.
DR BRENDA; 1.18.6.1; 49.
DR EvolutionaryTrace; P07329; -.
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; IMP:CACAO.
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; Direct protein sequencing; Iron; Iron-sulfur;
KW Metal-binding; Nitrogen fixation; Nucleotide-binding; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:649581"
FT CHAIN 2..523
FT /note="Nitrogenase molybdenum-iron protein beta chain"
FT /id="PRO_0000153091"
FT BINDING 70
FT /ligand="[8Fe-7S] cluster"
FT /ligand_id="ChEBI:CHEBI:21143"
FT /ligand_note="ligand shared with alpha chain"
FT BINDING 95
FT /ligand="[8Fe-7S] cluster"
FT /ligand_id="ChEBI:CHEBI:21143"
FT /ligand_note="ligand shared with alpha chain"
FT BINDING 153
FT /ligand="[8Fe-7S] cluster"
FT /ligand_id="ChEBI:CHEBI:21143"
FT /ligand_note="ligand shared with alpha chain"
FT BINDING 188
FT /ligand="[8Fe-7S] cluster"
FT /ligand_id="ChEBI:CHEBI:21143"
FT /ligand_note="ligand shared with alpha chain"
FT CONFLICT 103
FT /note="F -> L (in Ref. 2; AAA22144)"
FT /evidence="ECO:0000305"
FT HELIX 5..7
FT /evidence="ECO:0007829|PDB:1G21"
FT HELIX 11..14
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 18..31
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 37..46
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 50..57
FT /evidence="ECO:0007829|PDB:3U7Q"
FT STRAND 63..65
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 71..80
FT /evidence="ECO:0007829|PDB:3U7Q"
FT STRAND 85..91
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 93..107
FT /evidence="ECO:0007829|PDB:3U7Q"
FT STRAND 114..117
FT /evidence="ECO:0007829|PDB:1G21"
FT HELIX 120..123
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 128..142
FT /evidence="ECO:0007829|PDB:3U7Q"
FT STRAND 145..151
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 153..158
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 162..171
FT /evidence="ECO:0007829|PDB:3U7Q"
FT STRAND 177..179
FT /evidence="ECO:0007829|PDB:1L5H"
FT STRAND 188..191
FT /evidence="ECO:0007829|PDB:2AFI"
FT HELIX 193..209
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 210..215
FT /evidence="ECO:0007829|PDB:3U7Q"
FT TURN 218..221
FT /evidence="ECO:0007829|PDB:3U7Q"
FT STRAND 224..227
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 234..246
FT /evidence="ECO:0007829|PDB:3U7Q"
FT STRAND 251..255
FT /evidence="ECO:0007829|PDB:3U7Q"
FT TURN 258..261
FT /evidence="ECO:0007829|PDB:3U7Q"
FT STRAND 266..268
FT /evidence="ECO:0007829|PDB:6O7M"
FT HELIX 278..283
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 284..286
FT /evidence="ECO:0007829|PDB:3U7Q"
FT STRAND 287..294
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 295..297
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 299..307
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 321..336
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 342..362
FT /evidence="ECO:0007829|PDB:3U7Q"
FT STRAND 366..370
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 373..385
FT /evidence="ECO:0007829|PDB:3U7Q"
FT STRAND 389..395
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 400..411
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 414..416
FT /evidence="ECO:0007829|PDB:3U7Q"
FT STRAND 420..424
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 427..436
FT /evidence="ECO:0007829|PDB:3U7Q"
FT STRAND 440..444
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 448..458
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 460..462
FT /evidence="ECO:0007829|PDB:3U7Q"
FT STRAND 466..468
FT /evidence="ECO:0007829|PDB:3U7Q"
FT STRAND 475..478
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 479..481
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 486..508
FT /evidence="ECO:0007829|PDB:3U7Q"
FT TURN 512..515
FT /evidence="ECO:0007829|PDB:3U7Q"
FT HELIX 516..518
FT /evidence="ECO:0007829|PDB:3U7Q"
SQ SEQUENCE 523 AA; 59460 MW; B6ECD633A24998F2 CRC64;
MSQQVDKIKA SYPLFLDQDY KDMLAKKRDG FEEKYPQDKI DEVFQWTTTK EYQELNFQRE
ALTVNPAKAC QPLGAVLCAL GFEKTMPYVH GSQGCVAYFR SYFNRHFREP VSCVSDSMTE
DAAVFGGQQN MKDGLQNCKA TYKPDMIAVS TTCMAEVIGD DLNAFINNSK KEGFIPDEFP
VPFAHTPSFV GSHVTGWDNM FEGIARYFTL KSMDDKVVGS NKKINIVPGF ETYLGNFRVI
KRMLSEMGVG YSLLSDPEEV LDTPADGQFR MYAGGTTQEE MKDAPNALNT VLLQPWHLEK
TKKFVEGTWK HEVPKLNIPM GLDWTDEFLM KVSEISGQPI PASLTKERGR LVDMMTDSHT
WLHGKRFALW GDPDFVMGLV KFLLELGCEP VHILCHNGNK RWKKAVDAIL AASPYGKNAT
VYIGKDLWHL RSLVFTDKPD FMIGNSYGKF IQRDTLHKGK EFEVPLIRIG FPIFDRHHLH
RSTTLGYEGA MQILTTLVNS ILERLDEETR GMQATDYNHD LVR
