NIFH_KLEPN
ID NIFH_KLEPN Reviewed; 293 AA.
AC P00458;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 118.
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 Klebsiella pneumoniae.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=573;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3062178; DOI=10.1016/0022-2836(88)90205-7;
RA Arnold W., Rump A., Klipp W., Priefer U.B., Puehler A.;
RT "Nucleotide sequence of a 24,206-base-pair DNA fragment carrying the entire
RT nitrogen fixation gene cluster of Klebsiella pneumoniae.";
RL J. Mol. Biol. 203:715-738(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=UNF 841;
RX PubMed=6809876;
RA Scott K.F., Rolfe B.G., Shine J.;
RT "Biological nitrogen fixation: primary structure of the Klebsiella
RT pneumoniae nifH and nifD genes.";
RL J. Mol. Appl. Genet. 1:71-81(1981).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6259144; DOI=10.1016/s0021-9258(19)69686-9;
RA Sundaresan V., Ausubel F.M.;
RT "Nucleotide sequence of the gene coding for the nitrogenase iron protein
RT from Klebsiella pneumoniae.";
RL J. Biol. Chem. 256:2808-2812(1981).
RN [4]
RP PROTEIN SEQUENCE OF 2-26.
RX PubMed=7001444; DOI=10.1073/pnas.77.7.3826;
RA Hausinger R.P., Howard J.B.;
RT "Comparison of the iron proteins from the nitrogen fixation complexes of
RT Azotobacter vinelandii, Clostridium pasteurianum, and Klebsiella
RT pneumoniae.";
RL Proc. Natl. Acad. Sci. U.S.A. 77:3826-3830(1980).
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; V00631; CAA23903.1; -; Genomic_DNA.
DR EMBL; X13303; CAA31666.1; -; Genomic_DNA.
DR PIR; A92834; NIKBFP.
DR AlphaFoldDB; P00458; -.
DR SMR; P00458; -.
DR BioCyc; MetaCyc:NIFHKLEB-MON; -.
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 1: Evidence at protein level;
KW 4Fe-4S; ADP-ribosylation; ATP-binding; Direct protein sequencing; Iron;
KW Iron-sulfur; Metal-binding; Nitrogen fixation; Nucleotide-binding;
KW Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:7001444"
FT CHAIN 2..293
FT /note="Nitrogenase iron protein"
FT /id="PRO_0000139511"
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 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 101
FT /note="ADP-ribosylarginine; by dinitrogenase reductase ADP-
FT ribosyltransferase"
FT /evidence="ECO:0000250"
SQ SEQUENCE 293 AA; 31903 MW; B51BCB17E8C94FB1 CRC64;
MTMRQCAIYG KGGIGKSTTT QNLVAALAEM GKKVMIVGCD PKADSTRLIL HAKAQNTIME
MAAEVGSVED LELEDVLQIG YGDVRCAESG GPEPGVGCAG RGVITAINFL EEEGAYEDDL
DFVFYDVLGD VVCGGFAMPI RENKAQEIYI VCSGEMMAMY AANNISKGIV KYAKSGKVRL
GGLICNSRQT DREDELIIAL AEKLGTQMIH FVPRDNIVQR AEIRRMTVIE YDPACKQANE
YRTLAQKIVN NTMKVVPTPC TMDELESLLM EFGIMEEEDT SIIGKTAAEE NAA
