ID G3IZ25_METTV Unreviewed; 293 AA.
AC G3IZ25;
DT 16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT 16-NOV-2011, sequence version 1.
DT 27-MAR-2024, entry version 62.
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 ORFNames=Mettu_3327 {ECO:0000313|EMBL:EGW20197.1};
OS Methylobacter tundripaludum (strain ATCC BAA-1195 / DSM 17260 / SV96).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Methylococcales;
OC Methylococcaceae; Methylobacter.
OX NCBI_TaxID=697282 {ECO:0000313|EMBL:EGW20197.1, ECO:0000313|Proteomes:UP000004664};
RN [1] {ECO:0000313|EMBL:EGW20197.1, ECO:0000313|Proteomes:UP000004664}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-1195 / DSM 17260 / SV96
RC {ECO:0000313|Proteomes:UP000004664};
RG US DOE Joint Genome Institute;
RA Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S., Held B.,
RA Detter J.C., Han C., Tapia R., Land M., Hauser L., Kyrpides N., Ivanova N.,
RA Ovchinnikova G., Pagani I., Klotz M.G., Dispirito A.A., Murrell J.C.,
RA Dunfield P., Kalyuzhnaya M.G., Svenning M., Trotsenko Y.A., Stein L.Y.,
RA Woyke T.;
RT "Genomic sequence of Methylobacter tundripaludum SV96.";
RL Submitted (JUN-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-101 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; JH109153; EGW20197.1; -; Genomic_DNA.
DR RefSeq; WP_006892491.1; NZ_JH109153.1.
DR AlphaFoldDB; G3IZ25; -.
DR STRING; 697282.Mettu_3327; -.
DR eggNOG; COG1348; Bacteria.
DR HOGENOM; CLU_059373_0_0_6; -.
DR OrthoDB; 9815116at2; -.
DR Proteomes; UP000004664; Unassembled WGS sequence.
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:UP000004664}.
FT BINDING 10..17
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00533"
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:0000256|HAMAP-Rule:MF_00533"
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:0000256|HAMAP-Rule:MF_00533"
FT MOD_RES 101
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 293 AA; 31597 MW; 88475F862E16652D CRC64;
MALRQCAIYG KGGIGKSTTT QNLVSALAEL GNSVMIVGCD PKADSTRLIL HAKAQTTIMS
LAAEAGSVED LELEDVLKAG YRGIKCVESG GPEPGVGCAG RGVITAINFL EEEGAYDDEL
DFVFYDVLGD VVCGGFAMPI RENKAQEIYI VCSGEMMAMY AANNIAKGIV KYANSGSVRL
AGLICNSRET AREDELISAL AAKIGTTMIH FVPRDNVVQR AEIRRMTVIE YEPGHKQAQE
YRDLAIKIRD NKNFVIPTPI TMDELEELMM EFGIIDQEDE SIIGVTAAAE ATA
//
