NIFH_AZOBR
ID NIFH_AZOBR Reviewed; 293 AA.
AC P17303;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1990, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=Nitrogenase iron protein;
DE EC=1.18.6.1;
DE AltName: Full=Nitrogenase Fe protein;
DE AltName: Full=Nitrogenase component II;
DE AltName: Full=Nitrogenase reductase;
GN Name=nifH;
OS Azospirillum brasilense.
OC Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC Azospirillaceae; Azospirillum.
OX NCBI_TaxID=192;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 29145 / DSM 1690 / IMET 11303 / Sp7;
RX PubMed=2608030; DOI=10.1007/bf00260861;
RA de Zamaroczy M., Delorme F., Elmerich C.;
RT "Regulation of transcription and promoter mapping of the structural genes
RT for nitrogenase (nifHDK) of Azospirillum brasilense Sp7.";
RL Mol. Gen. Genet. 220:88-94(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2608029; DOI=10.1007/bf00260860;
RA Fani R., Allotta G., Bazzicalupo M., Ricci F., Schipani C., Polsinelli M.;
RT "Nucleotide sequence of the gene encoding the nitrogenase iron protein
RT (nifH) of Azospirillum brasilense and identification of a region
RT controlling nifH transcription.";
RL Mol. Gen. Genet. 220:81-87(1989).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=1823284;
RA Passaglia L.M.P., Nunes C.P., Zaha A., Schrank I.S.;
RT "The nifHDK operon in the free-living nitrogen-fixing bacteria Azospirillum
RT brasilense sequentially comprises genes H, D, K, an 353 bp orf and gene
RT Y.";
RL Braz. J. Med. Biol. Res. 24:649-675(1991).
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.
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;
CC Note=Binds 1 [4Fe-4S] cluster per dimer.;
CC -!- SUBUNIT: Homodimer.
CC -!- PTM: The reversible ADP-ribosylation of Arg-101 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; X51500; CAA35868.1; -; Genomic_DNA.
DR EMBL; M64344; AAB02342.1; ALT_SEQ; Genomic_DNA.
DR PIR; S15747; S15747.
DR RefSeq; WP_014239786.1; NZ_WFKD01000124.1.
DR AlphaFoldDB; P17303; -.
DR SMR; P17303; -.
DR GeneID; 56451760; -.
DR OrthoDB; 729012at2; -.
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..293
FT /note="Nitrogenase iron protein"
FT /id="PRO_0000139485"
FT BINDING 10..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 98
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 132
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 101
FT /note="ADP-ribosylarginine; by dinitrogenase reductase ADP-
FT ribosyltransferase"
FT /evidence="ECO:0000250"
FT CONFLICT 160
FT /note="A -> E (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 209
FT /note="H -> T (in Ref. 2)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="E -> Q (in Ref. 2)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 293 AA; 31729 MW; 1CEC281B3030802F CRC64;
MSLRQIAFYG KGGIGKSTTS QNTLAALVEL DQKILIVGCD PKADSTRLIL HAKAQDTVLH
LAAEAGSVED LELEDVLKIG YKGIKCVESG GPEPGVGCAG RGVITSINFL EENGAYDDVD
YVSYDVLGDV VCGGFAMPIR ENKAQEIYIV MSGEMMALYA ANNIAKGILK YAHSGGVRLG
GLICNERQTD KEIDLASALA ARLGTQLIHF VPRDNIVQHA ELRRMTVIEY APDSQQAQEY
RQLANKVHAN KGKGTIPTPI TMEELEEMLM DFGIMKSEEQ QLAELQAKEA AKA
