NIFK_SINFN
ID NIFK_SINFN Reviewed; 513 AA.
AC P19067;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 145.
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=nifK1; OrderedLocusNames=NGR_a01110; ORFNames=y4vM;
GN and
GN Name=nifK2; OrderedLocusNames=NGR_a00870; ORFNames=y4xC;
OS Sinorhizobium fredii (strain NBRC 101917 / NGR234).
OG Plasmid sym pNGR234a.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Sinorhizobium/Ensifer group; Sinorhizobium.
OX NCBI_TaxID=394;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234;
RX PubMed=9163424; DOI=10.1038/387394a0;
RA Freiberg C.A., Fellay R., Bairoch A., Broughton W.J., Rosenthal A.,
RA Perret X.;
RT "Molecular basis of symbiosis between Rhizobium and legumes.";
RL Nature 387:394-401(1997).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=NBRC 101917 / NGR234;
RX PubMed=19376903; DOI=10.1128/aem.00515-09;
RA Schmeisser C., Liesegang H., Krysciak D., Bakkou N., Le Quere A.,
RA Wollherr A., Heinemeyer I., Morgenstern B., Pommerening-Roeser A.,
RA Flores M., Palacios R., Brenner S., Gottschalk G., Schmitz R.A.,
RA Broughton W.J., Perret X., Strittmatter A.W., Streit W.R.;
RT "Rhizobium sp. strain NGR234 possesses a remarkable number of secretion
RT systems.";
RL Appl. Environ. Microbiol. 75:4035-4045(2009).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 132-195.
RC STRAIN=ANU 240;
RX PubMed=2744485; DOI=10.1016/0378-1119(89)90368-5;
RA Badenoch-Jones J., Holton T.A., Morrison C.M., Scott K.F., Shine J.;
RT "Structural and functional analysis of nitrogenase genes from the broad-
RT host-range Rhizobium strain ANU240.";
RL Gene 77:141-153(1989).
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 -!- MISCELLANEOUS: Ala-188 is present instead of the usual Ser that would
CC serve as a ligand for the 8Fe-7S cluster in the oxidized state.
CC -!- SIMILARITY: Belongs to the NifD/NifK/NifE/NifN family. {ECO:0000305}.
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DR EMBL; U00090; AAB91901.1; -; Genomic_DNA.
DR EMBL; U00090; AAB91925.1; -; Genomic_DNA.
DR EMBL; M26963; AAA26327.1; -; Genomic_DNA.
DR PIR; PS0046; PS0046.
DR PIR; T10830; T10830.
DR RefSeq; NP_444114.1; NC_000914.2.
DR RefSeq; NP_444138.1; NC_000914.2.
DR RefSeq; WP_010875128.1; NC_000914.2.
DR AlphaFoldDB; P19067; -.
DR SMR; P19067; -.
DR STRING; 394.NGR_a00870; -.
DR EnsemblBacteria; AAB91901; AAB91901; NGR_a00870.
DR EnsemblBacteria; AAB91925; AAB91925; NGR_a01110.
DR KEGG; rhi:NGR_a00870; -.
DR KEGG; rhi:NGR_a01110; -.
DR PATRIC; fig|394.7.peg.76; -.
DR eggNOG; COG2710; Bacteria.
DR HOGENOM; CLU_025876_2_0_5; -.
DR OMA; GLNNMID; -.
DR OrthoDB; 397330at2; -.
DR Proteomes; UP000001054; Plasmid sym pNGR234a.
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 3: Inferred from homology;
KW ATP-binding; Iron; Iron-sulfur; Metal-binding; Nitrogen fixation;
KW Nucleotide-binding; Oxidoreductase; Plasmid; Reference proteome.
FT CHAIN 1..513
FT /note="Nitrogenase molybdenum-iron protein beta chain"
FT /id="PRO_0000153107"
FT BINDING 70
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 95
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 153
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 513 AA; 57302 MW; 41631040335541AE CRC64;
MPQSAEKILD HAPLFREPEY RQMLAEKKLN FECPHPERLV TDQREYSKGW EYREKNLARE
ALVVNPAKAC QPLGAVFAAA GFERTMSFVH GSQGCVAYYR SHLSRHFKEP ASAVSSSMTE
DAAVFGGLKN MVDGLANTYA LYDPKMIAVS TTCMAEVIGD DLHGFIENAK SEGAVPPEFD
VPFAHTPAFV GSHVDGYDSM VKGILEHFWK GQARTQAAGT INIIPGFDGF CVGNNRELQR
LLTLMGVSYT FIQDASDQFD TPSDGEYRMY DGGTTIKALR AALNAEATLS LQHYNSRKTL
EYCREVGQAT AAFHYPLGIN ATDAFLMKVS AISGREIPET IRLERGRLVD AMADSQSWLH
GKTYAIYGDP DFVYAMARFV METGGEPRHC LATNGTAAWQ AEMTELLASS PFGKQAKVWP
GKDLWALRSL LFTEPVDLLI GNSYGKYLER DTGTPLIRLM FPIFDRHHHH RFPLMGYQGG
LRLLTTILDT IFDRLDRETM QTAVTDYSYD LTR
