NIFH_DESAP
ID NIFH_DESAP Reviewed; 280 AA.
AC B1I0Y8;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 29-APR-2008, sequence version 1.
DT 03-AUG-2022, entry version 80.
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}; OrderedLocusNames=Daud_0143;
OS Desulforudis audaxviator (strain MP104C).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Peptococcaceae;
OC Candidatus Desulforudis.
OX NCBI_TaxID=477974;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP104C;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Bruce D., Pitluck S., Lowry S.R., Larimer F., Land M.L.,
RA Hauser L., Kyrpides N., Ivanova N.N., Richardson P.;
RT "Complete sequence of chromosome of Desulforudis audaxviator MP104C.";
RL Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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-100 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}.
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DR EMBL; CP000860; ACA58711.1; -; Genomic_DNA.
DR RefSeq; WP_012301305.1; NC_010424.1.
DR AlphaFoldDB; B1I0Y8; -.
DR SMR; B1I0Y8; -.
DR STRING; 477974.Daud_0143; -.
DR EnsemblBacteria; ACA58711; ACA58711; Daud_0143.
DR KEGG; dau:Daud_0143; -.
DR eggNOG; COG1348; Bacteria.
DR HOGENOM; CLU_059373_0_0_9; -.
DR OMA; CNQAREY; -.
DR OrthoDB; 729012at2; -.
DR Proteomes; UP000008544; 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..280
FT /note="Nitrogenase iron protein"
FT /id="PRO_1000211866"
FT BINDING 9..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00533"
FT BINDING 97
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 132
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 100
FT /note="ADP-ribosylarginine; by dinitrogenase reductase ADP-
FT ribosyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00533"
SQ SEQUENCE 280 AA; 30788 MW; C4F765CC011CB65D CRC64;
MTRKIAIYGK GGIGKSTTTQ NTAAAMAYFF GKRIMIHGCD PKADSTRLIL GGMMQTTVMD
TLREEGEEGV TLDRVRLQGF GEIDCVESGG PEPGVGCAGR GVITAINLME DLNAYGDELD
FVFFDVLGDV VCGGFAMPVR EGKAQEIYIV ASGEMMALYA ANNICRGMVK YAEQSGVRLG
GIICNSRRVE GERELIEEFC ARLGTRMIMF VPRDNIVQKA EFNRKTVTEF APDSEQAQVY
RELARRIIEN DHFVIPTPMT MDEMESLVLK YGLLDLGEAS
