ID   NIFH1_RHOCB             Reviewed;         295 AA.
AC   D5ANI3; P08718;
DT   28-JUN-2011, integrated into UniProtKB/Swiss-Prot.
DT   15-JUN-2010, sequence version 1.
DT   03-AUG-2022, entry version 58.
DE   RecName: Full=Nitrogenase iron protein 1;
DE            EC=1.18.6.1;
DE   AltName: Full=Nitrogenase Fe protein 1;
DE   AltName: Full=Nitrogenase component II;
DE   AltName: Full=Nitrogenase reductase;
GN   Name=nifH; OrderedLocusNames=RCAP_rcc00572;
OS   Rhodobacter capsulatus (strain ATCC BAA-309 / NBRC 16581 / SB1003).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=272942;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX   PubMed=3419937; DOI=10.1093/nar/16.17.8735;
RA   Jones R., Haselkorn R.;
RT   "The DNA sequence of the Rhodobacter capsulatus nifH gene.";
RL   Nucleic Acids Res. 16:8735-8735(1988).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-309 / NBRC 16581 / SB1003;
RX   PubMed=20418398; DOI=10.1128/jb.00366-10;
RA   Strnad H., Lapidus A., Paces J., Ulbrich P., Vlcek C., Paces V.,
RA   Haselkorn R.;
RT   "Complete genome sequence of the photosynthetic purple nonsulfur bacterium
RT   Rhodobacter capsulatus SB 1003.";
RL   J. Bacteriol. 192:3545-3546(2010).
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; X07866; CAA30716.1; -; Genomic_DNA.
DR   EMBL; CP001312; ADE84337.1; -; Genomic_DNA.
DR   PIR; JN0888; JN0888.
DR   RefSeq; WP_013066316.1; NC_014034.1.
DR   AlphaFoldDB; D5ANI3; -.
DR   SMR; D5ANI3; -.
DR   STRING; 272942.RCAP_rcc00572; -.
DR   EnsemblBacteria; ADE84337; ADE84337; RCAP_rcc00572.
DR   GeneID; 31489522; -.
DR   KEGG; rcp:RCAP_rcc00572; -.
DR   eggNOG; COG1348; Bacteria.
DR   HOGENOM; CLU_059373_0_0_5; -.
DR   OMA; YVCDYYL; -.
DR   OrthoDB; 729012at2; -.
DR   Proteomes; UP000002361; 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..295
FT                   /note="Nitrogenase iron protein 1"
FT                   /id="PRO_0000410440"
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        66
FT                   /note="A -> V (in Ref. 1; CAA30716)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   295 AA;  32113 MW;  43D40C239CDDE307 CRC64;
     MGKLRQIAFY GKGGIGKSTT SQNTLAALVE MGQKILIVGC DPKADSTRLI LNTKLQDTVL
     HLAAEAGSVE DLEVEDVVKI GYKGIKCTEA GGPEPGVGCA GRGVITAINF LEENGAYDDV
     DYVSYDVLGD VVCGGFAMPI RENKAQEIYI VMSGEMMALY AANNIAKGIL KYANSGGVRL
     GGLICNERKT DRELELAEAL AAKLGCKMIH FVPRNNVVQH AELRRETVIQ YDPTCSQAQE
     YRELARKIHE NSGKGVIPTP ITMEELEEML MDFGIMQSEE DREKQIAEME AAMKA