NIFH2_NOSS1
ID NIFH2_NOSS1 Reviewed; 297 AA.
AC O30577;
DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2002, sequence version 2.
DT 03-AUG-2022, entry version 140.
DE RecName: Full=Nitrogenase iron protein 2;
DE EC=1.18.6.1;
DE AltName: Full=Nitrogenase Fe protein 2;
DE AltName: Full=Nitrogenase component II;
DE AltName: Full=Nitrogenase reductase;
GN Name=nifH2; OrderedLocusNames=alr0874;
OS Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576).
OC Bacteria; Cyanobacteria; Nostocales; Nostocaceae; Nostoc.
OX NCBI_TaxID=103690;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RA Robinson S.J., Haselkorn R.;
RT "Second copy of nifH in Anabaena sp. strain PCC 7120.";
RL Submitted (JUL-1997) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PCC 7120 / SAG 25.82 / UTEX 2576;
RX PubMed=11759840; DOI=10.1093/dnares/8.5.205;
RA Kaneko T., Nakamura Y., Wolk C.P., Kuritz T., Sasamoto S., Watanabe A.,
RA Iriguchi M., Ishikawa A., Kawashima K., Kimura T., Kishida Y., Kohara M.,
RA Matsumoto M., Matsuno A., Muraki A., Nakazaki N., Shimpo S., Sugimoto M.,
RA Takazawa M., Yamada M., Yasuda M., Tabata S.;
RT "Complete genomic sequence of the filamentous nitrogen-fixing
RT cyanobacterium Anabaena sp. strain PCC 7120.";
RL DNA Res. 8:205-213(2001).
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-105 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; AF012326; AAB65801.1; -; Genomic_DNA.
DR EMBL; BA000019; BAB72831.1; -; Genomic_DNA.
DR PIR; AG1915; AG1915.
DR RefSeq; WP_010995048.1; NZ_RSCN01000006.1.
DR AlphaFoldDB; O30577; -.
DR SMR; O30577; -.
DR STRING; 103690.17130219; -.
DR EnsemblBacteria; BAB72831; BAB72831; BAB72831.
DR KEGG; ana:alr0874; -.
DR eggNOG; COG1348; Bacteria.
DR OMA; NTHMIHY; -.
DR OrthoDB; 729012at2; -.
DR Proteomes; UP000002483; Chromosome.
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; Reference proteome.
FT CHAIN 1..297
FT /note="Nitrogenase iron protein 2"
FT /id="PRO_0000139482"
FT BINDING 14..21
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 102
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 136
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 105
FT /note="ADP-ribosylarginine; by dinitrogenase reductase ADP-
FT ribosyltransferase"
FT /evidence="ECO:0000250"
FT CONFLICT 297
FT /note="K -> SK (in Ref. 1; AAB65801)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 297 AA; 32602 MW; 9F37E5284E9B6D17 CRC64;
MSIDKKIRQI AFYGKGGIGK STTSQNTLAA MAEMGQRILI VGCDPKADST RLMLHSKAQT
TVLHLAAERG AVEDLELEEV MLTGFRGVKC VESGGPEPGV GCAGRGIITA INFLEENGAY
QDVDFVSYDV LGDVVCGGFA MPIRENKAQE IYIVTSGEMM AMYAANNIAR GILKYAHTGG
VRLGGLICNS RNVDREIELI ETLAKRLNTQ MIHYVPRDNI VQHAELRRMT VNEYAPDSNQ
GNEYRILANK IINNENLKIP TPIEMEELEE LLIEFGILES EENAAKMIAT TSESKSK
