ID F2NEQ1_DESAR Unreviewed; 274 AA.
AC F2NEQ1;
DT 31-MAY-2011, integrated into UniProtKB/TrEMBL.
DT 31-MAY-2011, sequence version 1.
DT 24-JAN-2024, entry version 71.
DE RecName: Full=Nitrogenase iron protein {ECO:0000256|HAMAP-Rule:MF_00533};
DE EC=1.18.6.1 {ECO:0000256|HAMAP-Rule:MF_00533};
DE AltName: Full=Nitrogenase Fe protein {ECO:0000256|HAMAP-Rule:MF_00533};
DE AltName: Full=Nitrogenase component II {ECO:0000256|HAMAP-Rule:MF_00533};
DE AltName: Full=Nitrogenase reductase {ECO:0000256|HAMAP-Rule:MF_00533};
GN Name=nifH {ECO:0000256|HAMAP-Rule:MF_00533};
GN OrderedLocusNames=Desac_0350 {ECO:0000313|EMBL:AEB08241.1};
OS Desulfobacca acetoxidans (strain ATCC 700848 / DSM 11109 / ASRB2).
OC Bacteria; Thermodesulfobacteriota; Desulfobaccia; Desulfobaccales;
OC Desulfobaccaceae; Desulfobacca.
OX NCBI_TaxID=880072 {ECO:0000313|EMBL:AEB08241.1, ECO:0000313|Proteomes:UP000000483};
RN [1] {ECO:0000313|EMBL:AEB08241.1, ECO:0000313|Proteomes:UP000000483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700848 / DSM 11109 / ASRB2
RC {ECO:0000313|Proteomes:UP000000483};
RX PubMed=21886866;
RA Goker M., Teshima H., Lapidus A., Nolan M., Lucas S., Hammon N.,
RA Deshpande S., Cheng J.F., Tapia R., Han C., Goodwin L., Pitluck S.,
RA Huntemann M., Liolios K., Ivanova N., Pagani I., Mavromatis K.,
RA Ovchinikova G., Pati A., Chen A., Palaniappan K., Land M., Hauser L.,
RA Brambilla E.M., Rohde M., Spring S., Detter J.C., Woyke T., Bristow J.,
RA Eisen J.A., Markowitz V., Hugenholtz P., Kyrpides N.C., Klenk H.P.;
RT "Complete genome sequence of the acetate-degrading sulfate reducer
RT Desulfobacca acetoxidans type strain (ASRB2).";
RL Stand. Genomic Sci. 4:393-401(2011).
RN [2] {ECO:0000313|Proteomes:UP000000483}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700848 / DSM 11109 / ASRB2
RC {ECO:0000313|Proteomes:UP000000483};
RG US DOE Joint Genome Institute (JGI-PGF);
RA Lucas S., Copeland A., Lapidus A., Bruce D., Goodwin L., Pitluck S.,
RA Peters L., Kyrpides N., Mavromatis K., Ivanova N., Ovchinnikova G.,
RA Teshima H., Detter J.C., Han C., Land M., Hauser L., Markowitz V.,
RA Cheng J.-F., Hugenholtz P., Woyke T., Wu D., Spring S., Schueler E.,
RA Brambilla E., Klenk H.-P., Eisen J.A.;
RT "The complete genome of Desulfobacca acetoxidans DSM 11109.";
RL Submitted (MAR-2011) 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:0000256|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;
CC Evidence={ECO:0000256|ARBA:ARBA00000805, ECO:0000256|HAMAP-
CC Rule:MF_00533};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|HAMAP-Rule:MF_00533};
CC Note=Binds 1 [4Fe-4S] cluster per dimer. {ECO:0000256|HAMAP-
CC Rule:MF_00533};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738, ECO:0000256|HAMAP-
CC Rule:MF_00533}.
CC -!- PTM: The reversible ADP-ribosylation of Arg inactivates the nitrogenase
CC reductase and regulates nitrogenase activity.
CC {ECO:0000256|PIRSR:PIRSR605977-50}.
CC -!- PTM: The reversible ADP-ribosylation of Arg-97 inactivates the
CC nitrogenase reductase and regulates nitrogenase activity.
CC {ECO:0000256|HAMAP-Rule:MF_00533}.
CC -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family.
CC {ECO:0000256|ARBA:ARBA00005504, ECO:0000256|HAMAP-Rule:MF_00533,
CC ECO:0000256|RuleBase:RU003688}.
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DR EMBL; CP002629; AEB08241.1; -; Genomic_DNA.
DR RefSeq; WP_013705354.1; NC_015388.1.
DR AlphaFoldDB; F2NEQ1; -.
DR STRING; 880072.Desac_0350; -.
DR KEGG; dao:Desac_0350; -.
DR eggNOG; COG1348; Bacteria.
DR HOGENOM; CLU_059373_0_0_7; -.
DR OMA; YVCDYYL; -.
DR OrthoDB; 9778641at2; -.
DR Proteomes; UP000000483; 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 CDD; cd02040; NifH; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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 NCBIfam; TIGR01287; nifH; 1.
DR PANTHER; PTHR42864; LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE IRON-SULFUR ATP-BINDING PROTEIN; 1.
DR PANTHER; PTHR42864:SF2; LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE IRON-SULFUR ATP-BINDING PROTEIN; 1.
DR Pfam; PF00142; Fer4_NifH; 1.
DR PIRSF; PIRSF000363; Nitrogenase_iron; 1.
DR PRINTS; PR00091; NITROGNASEII.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 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 {ECO:0000256|HAMAP-Rule:MF_00533, ECO:0000256|RuleBase:RU003688};
KW ADP-ribosylation {ECO:0000256|ARBA:ARBA00022765, ECO:0000256|HAMAP-
KW Rule:MF_00533};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|HAMAP-
KW Rule:MF_00533};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|HAMAP-Rule:MF_00533};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|HAMAP-
KW Rule:MF_00533};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723, ECO:0000256|HAMAP-
KW Rule:MF_00533};
KW Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231, ECO:0000256|HAMAP-
KW Rule:MF_00533};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|HAMAP-
KW Rule:MF_00533};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002, ECO:0000256|HAMAP-
KW Rule:MF_00533}; Reference proteome {ECO:0000313|Proteomes:UP000000483}.
FT BINDING 8..15
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00533"
FT BINDING 94
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00533"
FT BINDING 131
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /ligand_note="ligand shared between dimeric partners"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00533"
FT MOD_RES 97
FT /note="ADP-ribosylarginine; by dinitrogenase reductase ADP-
FT ribosyltransferase"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00533,
FT ECO:0000256|PIRSR:PIRSR605977-50"
SQ SEQUENCE 274 AA; 29586 MW; 9401FD80CDF5BBD9 CRC64;
MRKIAIYGKG GIGKSTTTQN TVAGLAEMGR KVMVVGCDPK ADSTRLLLGG LAQRSVLDTL
REEGEDVDLE DIRRLGFSGI ICVESGGPEP GVGCAGRGII TSINLLEQLG AYADSEKLDY
AFYDVLGDVV CGGFAMPIRE GKAKEIYIVV SGEMMAMYAA NNICKGIVKF AEAGGVRLGG
LICNSRKVEN EEEMIQALAV KLGTQMIHFI PRDNIVQRAE IHRKTVIDYD SGHPQADEYR
TLAKKIEANT MHVIPKPMST DELESLLIEY GLAG
//