NIFH2_METBA
ID NIFH2_METBA Reviewed; 273 AA.
AC P54800;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 109.
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;
OS Methanosarcina barkeri.
OC Archaea; Euryarchaeota; Stenosarchaea group; Methanomicrobia;
OC Methanosarcinales; Methanosarcinaceae; Methanosarcina.
OX NCBI_TaxID=2208;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 43241 / DSM 1538 / 227;
RX PubMed=2068380; DOI=10.1016/0923-2508(91)90091-n;
RA Sibold L., Henriquet M., Possot O., Aubert J.-P.;
RT "Nucleotide sequence of nifH regions from Methanobacterium ivanovii and
RT Methanosarcina barkeri 227 and characterization of glnB-like genes.";
RL Res. Microbiol. 142:5-12(1991).
RN [2]
RP SEQUENCE REVISION TO 11-13.
RC STRAIN=ATCC 43241 / DSM 1538 / 227;
RX PubMed=7961410; DOI=10.1128/jb.176.21.6590-6598.1994;
RA Chien Y.-T., Zinder S.H.;
RT "Cloning, DNA sequencing, and characterization of a nifD-homologous gene
RT from the archaeon Methanosarcina barkeri 227 which resembles nifD1 from the
RT eubacterium Clostridium pasteurianum.";
RL J. Bacteriol. 176:6590-6598(1994).
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-98 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; X56073; CAA39556.1; -; Genomic_DNA.
DR AlphaFoldDB; P54800; -.
DR SMR; P54800; -.
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.
FT CHAIN 1..273
FT /note="Nitrogenase iron protein 2"
FT /id="PRO_0000139536"
FT BINDING 8..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 95
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 130
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 98
FT /note="ADP-ribosylarginine; by dinitrogenase reductase ADP-
FT ribosyltransferase"
FT /evidence="ECO:0000250"
FT CONFLICT 11..13
FT /note="GIG -> WELE (in Ref. 1)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 273 AA; 29346 MW; 147F73F02DD6B7AA CRC64;
MRQIAIYGKG GIGKSTTTQN LTASLSTMGN KIMLVGCDPK ADSTRMLLGG LNQKTVLDTL
RSEGDEGVDL DVVMQRGFGD IKCVESGGPE PGVGCAGRGI ITSIGLLENL GAYTDDLDYV
FYDVLGDVVC GGFAMPIREG KAKEIYIVAS GELMAIYAAN NICKGLAKFA KGGARLGGII
CNSRNVDGER ELLDAFAKKL GSHLIHFIPR DNIVQRAEIN RKTVIDFDPE SNQAKEYLTL
AHNVQNNDKL VVPTPLPMEE LEAMMVEFGI VDL
