ID A6VFE2_METM7 Unreviewed; 275 AA.
AC A6VFE2;
DT 21-AUG-2007, integrated into UniProtKB/TrEMBL.
DT 21-AUG-2007, sequence version 1.
DT 27-MAR-2024, entry version 99.
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=MmarC7_0098 {ECO:0000313|EMBL:ABR65168.1};
OS Methanococcus maripaludis (strain C7 / ATCC BAA-1331).
OC Archaea; Euryarchaeota; Methanomada group; Methanococci; Methanococcales;
OC Methanococcaceae; Methanococcus.
OX NCBI_TaxID=426368 {ECO:0000313|EMBL:ABR65168.1};
RN [1] {ECO:0000313|EMBL:ABR65168.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C7 {ECO:0000313|EMBL:ABR65168.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Glavina del Rio T., Dalin E.,
RA Tice H., Pitluck S., Clum A., Schmutz J., Larimer F., Land M., Hauser L.,
RA Kyrpides N., Anderson I., Sieprawska-Lupa M., Whitman W.B., Richardson P.;
RT "Complete sequence of Methanococcus maripaludis C7.";
RL Submitted (JUN-2007) 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.
CC {ECO:0000256|ARBA:ARBA00002234, ECO:0000256|HAMAP-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-100 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; CP000745; ABR65168.1; -; Genomic_DNA.
DR AlphaFoldDB; A6VFE2; -.
DR STRING; 426368.MmarC7_0098; -.
DR KEGG; mmz:MmarC7_0098; -.
DR eggNOG; arCOG00590; Archaea.
DR HOGENOM; CLU_059373_0_0_2; -.
DR OrthoDB; 145464at2157; -.
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}.
FT BINDING 9..16
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00533"
FT BINDING 97
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 132
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 100
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 275 AA; 30123 MW; 3FCE4661166E6F03 CRC64;
MVRKIAIYGK GGIGKSTTTQ NTVAAMAYFH DKKVMIHGCD PKADSTRLIL HGKQQTTMMD
TLREKGEEEC TPEKVIDVGF CGVKCVESGG PEPGVGCAGR GVITAITLME QQGVYEDNLD
YVFFDVLGDV VCGGFAMPVR DGKADEIYVV ASGEMMALYA ANNICKGMVK YAEQSGVRLG
GIICNSRNVD GELELLQEFC DKIGTQLIHF VPRDNIVQKA EFQKMAVVDF DDSCNQALEY
KALAQKIIDN KNLVIPNPMT MDELEELTSK YGFLD
//
