NIFH_SINFN
ID NIFH_SINFN Reviewed; 296 AA.
AC P19068; P55672;
DT 01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1997, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Nitrogenase iron protein;
DE EC=1.18.6.1;
DE AltName: Full=Nitrogenase Fe protein;
DE AltName: Full=Nitrogenase component II;
DE AltName: Full=Nitrogenase reductase;
GN Name=nifH1; OrderedLocusNames=NGR_a01130; ORFNames=y4vK;
GN and
GN Name=nifH2; OrderedLocusNames=NGR_a00890; ORFNames=y4xA;
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 [GENOMIC DNA].
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).
RN [2]
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 [3]
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).
CC -!- FUNCTION: The key enzymatic reactions in nitrogen fixation are
CC catalyzed by the nitrogenase complex, which has 2 components: the iron
CC protein and the molybdenum-iron protein. {ECO:0000250}.
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=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883; Evidence={ECO:0000250};
CC Note=Binds 1 [4Fe-4S] cluster per dimer. {ECO:0000250};
CC -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC -!- PTM: The reversible ADP-ribosylation of Arg-102 inactivates the
CC nitrogenase reductase and regulates nitrogenase activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family. {ECO:0000305}.
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DR EMBL; M26961; AAA26329.1; -; Genomic_DNA.
DR EMBL; U00090; AAB91899.1; -; Genomic_DNA.
DR EMBL; U00090; AAB91923.1; -; Genomic_DNA.
DR PIR; JS0238; JS0238.
DR RefSeq; NP_444112.1; NC_000914.2.
DR RefSeq; NP_444136.1; NC_000914.2.
DR RefSeq; WP_010875130.1; NC_000914.2.
DR AlphaFoldDB; P19068; -.
DR SMR; P19068; -.
DR STRING; 394.NGR_a00890; -.
DR EnsemblBacteria; AAB91899; AAB91899; NGR_a01130.
DR EnsemblBacteria; AAB91923; AAB91923; NGR_a00890.
DR GeneID; 48977766; -.
DR KEGG; rhi:NGR_a00890; -.
DR KEGG; rhi:NGR_a01130; -.
DR PATRIC; fig|394.7.peg.78; -.
DR eggNOG; COG1348; Bacteria.
DR HOGENOM; CLU_059373_0_0_5; -.
DR OMA; YVCDYYL; -.
DR OrthoDB; 729012at2; -.
DR Proteomes; UP000001054; Plasmid sym pNGR234a.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0018697; F:carbonyl sulfide nitrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016163; F:nitrogenase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-UniRule.
DR Gene3D; 3.40.50.300; -; 1.
DR HAMAP; MF_00533; NifH; 1.
DR InterPro; IPR030655; NifH/chlL_CS.
DR InterPro; IPR000392; NifH/frxC.
DR InterPro; IPR005977; Nitrogenase_Fe_NifH.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR42864; PTHR42864; 1.
DR Pfam; PF00142; Fer4_NifH; 1.
DR PIRSF; PIRSF000363; Nitrogenase_iron; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
DR TIGRFAMs; TIGR01287; nifH; 1.
DR PROSITE; PS00746; NIFH_FRXC_1; 1.
DR PROSITE; PS00692; NIFH_FRXC_2; 1.
DR PROSITE; PS51026; NIFH_FRXC_3; 1.
PE 3: Inferred from homology;
KW 4Fe-4S; ADP-ribosylation; ATP-binding; Iron; Iron-sulfur; Metal-binding;
KW Nitrogen fixation; Nucleotide-binding; Oxidoreductase; Plasmid;
KW Reference proteome.
FT CHAIN 1..296
FT /note="Nitrogenase iron protein"
FT /id="PRO_0000139525"
FT BINDING 11..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 99
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT BINDING 133
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000250"
FT MOD_RES 102
FT /note="ADP-ribosylarginine; by dinitrogenase reductase ADP-
FT ribosyltransferase"
FT /evidence="ECO:0000250"
FT CONFLICT 262
FT /note="T -> N (in Ref. 1; AAA26329)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 296 AA; 31747 MW; 58ADF69DB677BA7A CRC64;
MAGLRQIAFY GKGGIGKSTT SQNTLAALVD LGQKILIVGC DPKADSTRLI LNAKAQDTVL
HLAAKEGSVE DLEVEDVLKV GYKGIKCVES GGPEPGVGCA GRGVITSINF LEENGAYDDV
DYVSYDVLGD VVCGGFAMPI RENKAQEIYI VMSGEMMALY AANNIAKGIL KYAHSGGVRL
GGLICNERQT DRELDLAEAL AAKLNSRLIH FVPRDNIVQH AELRKMTVIQ YAPESQQAAE
YRALADKIHA NSGQGTVPTP ITMEELEDML LDFGVMKTDE QMLAELQAKE AAAAAQ
