NIFH1_CLOPA
ID NIFH1_CLOPA Reviewed; 273 AA.
AC P00456;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=Nitrogenase iron protein 1;
DE EC=1.18.6.1;
DE AltName: Full=Nitrogenase Fe protein 1;
DE AltName: Full=Nitrogenase component II;
DE AltName: Full=Nitrogenase reductase;
GN Name=nifH1;
OS Clostridium pasteurianum.
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Clostridiaceae;
OC Clostridium.
OX NCBI_TaxID=1501;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2829127; DOI=10.1093/nar/16.2.439;
RA Wang S.-Z., Chen J.-S., Johnson J.L.;
RT "The presence of five nifH-like sequences in Clostridium pasteurianum:
RT sequence divergence and transcription properties.";
RL Nucleic Acids Res. 16:439-454(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=3457003; DOI=10.1128/jb.166.1.162-172.1986;
RA Chen K.C.K., Chen J.-S., Johnson J.L.;
RT "Structural features of multiple nifH-like sequences and very biased codon
RT usage in nitrogenase genes of Clostridium pasteurianum.";
RL J. Bacteriol. 166:162-172(1986).
RN [3]
RP PROTEIN SEQUENCE.
RX PubMed=561783; DOI=10.1016/s0021-9258(19)66939-5;
RA Tanaka M., Haniu M., Yasunobu K.T., Mortenson L.E.;
RT "The amino acid sequence of Clostridium pasteurianum iron protein, a
RT component of nitrogenase. III. The NH2-terminal and COOH-terminal
RT sequences, tryptic peptides of large cyanogen bromide peptides, and the
RT complete sequence.";
RL J. Biol. Chem. 252:7093-7100(1977).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.93 ANGSTROMS).
RC STRAIN=ATCC 6013 / DSM 525 / NCIB 9486 / VKM B-1774 / W5;
RX PubMed=9677296; DOI=10.1006/jmbi.1998.1898;
RA Schlessman J.L., Woo D., Joshua-Tor L., Howard J.B., Rees D.C.;
RT "Conformational variability in structures of the nitrogenase iron proteins
RT from Azotobacter vinelandii and Clostridium pasteurianum.";
RL J. Mol. Biol. 280:669-685(1998).
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-97 inactivates the
CC nitrogenase reductase and regulates nitrogenase activity.
CC {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X07472; CAA30359.1; -; Genomic_DNA.
DR EMBL; AY603957; AAT37644.1; -; Genomic_DNA.
DR PIR; A00533; NICLFP.
DR RefSeq; WP_003447877.1; NZ_CP013019.1.
DR PDB; 1CP2; X-ray; 1.93 A; A/B=1-269.
DR PDBsum; 1CP2; -.
DR AlphaFoldDB; P00456; -.
DR SMR; P00456; -.
DR BioCyc; MetaCyc:NIFH1CP-MON; -.
DR EvolutionaryTrace; P00456; -.
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 3D-structure; 4Fe-4S; ADP-ribosylation; ATP-binding;
KW Direct protein sequencing; Iron; Iron-sulfur; Metal-binding;
KW Nitrogen fixation; Nucleotide-binding; Oxidoreductase.
FT CHAIN 1..273
FT /note="Nitrogenase iron protein 1"
FT /id="PRO_0000139498"
FT BINDING 8..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 94
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT BINDING 129
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT MOD_RES 97
FT /note="ADP-ribosylarginine; by dinitrogenase reductase ADP-
FT ribosyltransferase"
FT /evidence="ECO:0000250"
FT STRAND 2..8
FT /evidence="ECO:0007829|PDB:1CP2"
FT HELIX 14..26
FT /evidence="ECO:0007829|PDB:1CP2"
FT TURN 27..29
FT /evidence="ECO:0007829|PDB:1CP2"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:1CP2"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:1CP2"
FT HELIX 56..63
FT /evidence="ECO:0007829|PDB:1CP2"
FT HELIX 64..66
FT /evidence="ECO:0007829|PDB:1CP2"
FT HELIX 69..72
FT /evidence="ECO:0007829|PDB:1CP2"
FT HELIX 77..79
FT /evidence="ECO:0007829|PDB:1CP2"
FT STRAND 81..84
FT /evidence="ECO:0007829|PDB:1CP2"
FT HELIX 95..108
FT /evidence="ECO:0007829|PDB:1CP2"
FT STRAND 117..124
FT /evidence="ECO:0007829|PDB:1CP2"
FT TURN 130..133
FT /evidence="ECO:0007829|PDB:1CP2"
FT HELIX 134..137
FT /evidence="ECO:0007829|PDB:1CP2"
FT STRAND 143..148
FT /evidence="ECO:0007829|PDB:1CP2"
FT HELIX 152..168
FT /evidence="ECO:0007829|PDB:1CP2"
FT STRAND 175..182
FT /evidence="ECO:0007829|PDB:1CP2"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:1CP2"
FT HELIX 190..200
FT /evidence="ECO:0007829|PDB:1CP2"
FT STRAND 204..208
FT /evidence="ECO:0007829|PDB:1CP2"
FT HELIX 212..219
FT /evidence="ECO:0007829|PDB:1CP2"
FT HELIX 224..227
FT /evidence="ECO:0007829|PDB:1CP2"
FT HELIX 232..246
FT /evidence="ECO:0007829|PDB:1CP2"
FT HELIX 258..268
FT /evidence="ECO:0007829|PDB:1CP2"
SQ SEQUENCE 273 AA; 29662 MW; A4EC06C5F58F08EC CRC64;
MRQVAIYGKG GIGKSTTTQN LTSGLHAMGK TIMVVGCDPK ADSTRLLLGG LAQKSVLDTL
REEGEDVELD SILKEGYGGI RCVESGGPEP GVGCAGRGII TSINMLEQLG AYTDDLDYVF
YDVLGDVVCG GFAMPIREGK AQEIYIVASG EMMALYAANN ISKGIQKYAK SGGVRLGGII
CNSRKVANEY ELLDAFAKEL GSQLIHFVPR SPMVTKAEIN KQTVIEYDPT CEQAEEYREL
ARKVDANELF VIPKPMTQER LEEILMQYGL MDL
