ID   NIFH_GLOC7              Reviewed;         299 AA.
AC   B7KG76;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 1.
DT   03-AUG-2022, entry version 71.
DE   RecName: Full=Nitrogenase iron protein {ECO:0000255|HAMAP-Rule:MF_00533};
DE            EC=1.18.6.1 {ECO:0000255|HAMAP-Rule:MF_00533};
DE   AltName: Full=Nitrogenase Fe protein {ECO:0000255|HAMAP-Rule:MF_00533};
DE   AltName: Full=Nitrogenase component II {ECO:0000255|HAMAP-Rule:MF_00533};
DE   AltName: Full=Nitrogenase reductase {ECO:0000255|HAMAP-Rule:MF_00533};
GN   Name=nifH {ECO:0000255|HAMAP-Rule:MF_00533};
GN   OrderedLocusNames=PCC7424_2120;
OS   Gloeothece citriformis (strain PCC 7424) (Cyanothece sp. (strain PCC
OS   7424)).
OC   Bacteria; Cyanobacteria; Oscillatoriophycideae; Chroococcales;
OC   Aphanothecaceae; Gloeothece; Gloeothece citriformis.
OX   NCBI_TaxID=65393;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=PCC 7424;
RX   PubMed=21972240; DOI=10.1128/mbio.00214-11;
RA   Bandyopadhyay A., Elvitigala T., Welsh E., Stockel J., Liberton M., Min H.,
RA   Sherman L.A., Pakrasi H.B.;
RT   "Novel metabolic attributes of the genus Cyanothece, comprising a group of
RT   unicellular nitrogen-fixing Cyanobacteria.";
RL   MBio 2:E214-E214(2011).
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:0000255|HAMAP-
CC       Rule:MF_00533}.
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; Evidence={ECO:0000255|HAMAP-
CC         Rule:MF_00533};
CC   -!- COFACTOR:
CC       Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_00533};
CC       Note=Binds 1 [4Fe-4S] cluster per dimer. {ECO:0000255|HAMAP-
CC       Rule:MF_00533};
CC   -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_00533}.
CC   -!- PTM: The reversible ADP-ribosylation of Arg-99 inactivates the
CC       nitrogenase reductase and regulates nitrogenase activity.
CC       {ECO:0000255|HAMAP-Rule:MF_00533}.
CC   -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family. {ECO:0000255|HAMAP-
CC       Rule:MF_00533}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; CP001291; ACK70547.1; -; Genomic_DNA.
DR   RefSeq; WP_015954153.1; NC_011729.1.
DR   AlphaFoldDB; B7KG76; -.
DR   SMR; B7KG76; -.
DR   STRING; 65393.PCC7424_2120; -.
DR   EnsemblBacteria; ACK70547; ACK70547; PCC7424_2120.
DR   KEGG; cyc:PCC7424_2120; -.
DR   eggNOG; COG1348; Bacteria.
DR   HOGENOM; CLU_059373_0_0_3; -.
DR   OMA; TTMMDTL; -.
DR   OrthoDB; 729012at2; -.
DR   Proteomes; UP000002384; 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..299
FT                   /note="Nitrogenase iron protein"
FT                   /id="PRO_1000211860"
FT   BINDING         8..15
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00533"
FT   BINDING         96
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00533"
FT   BINDING         130
FT                   /ligand="[4Fe-4S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:49883"
FT                   /ligand_note="ligand shared between dimeric partners"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00533"
FT   MOD_RES         99
FT                   /note="ADP-ribosylarginine; by dinitrogenase reductase ADP-
FT                   ribosyltransferase"
FT                   /evidence="ECO:0000255|HAMAP-Rule:MF_00533"
SQ   SEQUENCE   299 AA;  32723 MW;  759EEE314A4AE701 CRC64;
     MRQIAFYGKG GIGKSTTSQN TLAGMAQNGN RIMIVGCDPK ADSTRLILNT KAQVTVLHLA
     AERGAVEDLE LEDVLLQGFA DIKCVESGGP EPGVGCAGRG IITAINFLEE EGAYEDLDFV
     SYDVLGDVVC GGFAMPIREG KAQEIYIVTS GEMMAMYAAN NIARGILKYA HTGGVRLGGL
     ICNSRNVNRE TDLIEELADR LNTQMIHFVP RSKQVQEAEL RRMTVIQYSP DHPQADEYRT
     LAKKIEENTK LTIPTPIDND TLEELLINYG LLGSEEEYKK VMEADMATQA LTRATSINK