NIFH_METNO
ID NIFH_METNO Reviewed; 299 AA.
AC B8ITG7;
DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT 03-MAR-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}; OrderedLocusNames=Mnod_3996;
OS Methylobacterium nodulans (strain LMG 21967 / CNCM I-2342 / ORS 2060).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Methylobacteriaceae; Methylobacterium.
OX NCBI_TaxID=460265;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21967 / CNCM I-2342 / ORS 2060;
RG US DOE Joint Genome Institute;
RA Lucas S., Copeland A., Lapidus A., Glavina del Rio T., Dalin E., Tice H.,
RA Bruce D., Goodwin L., Pitluck S., Sims D., Brettin T., Detter J.C., Han C.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Ivanova N., Marx C.J.,
RA Richardson P.;
RT "Complete sequence of chromosome of Methylobacterium nodulans ORS 2060.";
RL Submitted (JAN-2009) 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-102 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; CP001349; ACL58883.1; -; Genomic_DNA.
DR RefSeq; WP_015930533.1; NC_011894.1.
DR AlphaFoldDB; B8ITG7; -.
DR SMR; B8ITG7; -.
DR STRING; 460265.Mnod_3996; -.
DR PRIDE; B8ITG7; -.
DR EnsemblBacteria; ACL58883; ACL58883; Mnod_3996.
DR KEGG; mno:Mnod_3996; -.
DR eggNOG; COG1348; Bacteria.
DR HOGENOM; CLU_059373_0_0_5; -.
DR OMA; YVCDYYL; -.
DR OrthoDB; 729012at2; -.
DR Proteomes; UP000008207; 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_1000211876"
FT BINDING 11..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00533"
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:0000255|HAMAP-Rule:MF_00533"
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:0000255|HAMAP-Rule:MF_00533"
FT MOD_RES 102
FT /note="ADP-ribosylarginine; by dinitrogenase reductase ADP-
FT ribosyltransferase"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_00533"
SQ SEQUENCE 299 AA; 32115 MW; 01E20DD678CD1318 CRC64;
MTGLRQIAFY GKGGIGKSTT SQNTLAALVE KGQKILIVGC DPKADSTRLI LNAKAQDTVL
SLAAEAGSVE DLELEEVLKI GYKGIKCVES GGPEPGVGCA GRGVITSINF LEENGAYDDV
DYVSYDVLGD VVCGGFAMPI RENKAQEIYI VMSGEMMALY AANNIAKGIL KYAHSGGVRL
GGLICNERQT DRELDLAEAL AKRLNSQLIH FVPRDNIVQH AELRRQTVIQ YAPDSAQAGE
YRKLAEKVHA NAGKGTIPTP ITMEELEQML LDFGIMKTEE QQLAELAAKE AAKAAAALR
