ID Q79BE9_RHIEC Unreviewed; 297 AA.
AC Q79BE9;
DT 10-MAY-2005, integrated into UniProtKB/TrEMBL.
DT 10-MAY-2005, sequence version 1.
DT 27-MAR-2024, entry version 144.
DE RecName: Full=Nitrogenase iron protein {ECO:0000256|ARBA:ARBA00017783, ECO:0000256|HAMAP-Rule:MF_00533};
DE EC=1.18.6.1 {ECO:0000256|ARBA:ARBA00012773, ECO:0000256|HAMAP-Rule:MF_00533};
DE AltName: Full=Nitrogenase Fe protein {ECO:0000256|ARBA:ARBA00029858, ECO:0000256|HAMAP-Rule:MF_00533};
DE AltName: Full=Nitrogenase component II {ECO:0000256|ARBA:ARBA00029951, ECO:0000256|HAMAP-Rule:MF_00533};
DE AltName: Full=Nitrogenase reductase {ECO:0000256|ARBA:ARBA00033027, ECO:0000256|HAMAP-Rule:MF_00533};
GN Name=nifH {ECO:0000256|HAMAP-Rule:MF_00533};
GN OrderedLocusNames=RHE_PD00202 {ECO:0000313|EMBL:AAM54849.1},
GN RHE_PD00260 {ECO:0000313|EMBL:AAM54793.1}, RHE_PD00308
GN {ECO:0000313|EMBL:AAM54750.1};
OS Rhizobium etli (strain CFN 42 / ATCC 51251).
OG Plasmid p42d {ECO:0000313|EMBL:AAM54793.1}, and
OG Plasmid sym p42d {ECO:0000313|Proteomes:UP000001936}.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Rhizobium/Agrobacterium group; Rhizobium.
OX NCBI_TaxID=347834 {ECO:0000313|EMBL:AAM54793.1, ECO:0000313|Proteomes:UP000001936};
RN [1] {ECO:0000313|EMBL:AAM54793.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CFN 42 {ECO:0000313|EMBL:AAM54793.1};
RC PLASMID=p42d {ECO:0000313|EMBL:AAM54793.1};
RX PubMed=2013564;
RA Girard M.L., Flores M., Brom S., Romero D., Palacios R., Davila G.;
RT "Structural complexity of the symbiotic plasmid of Rhizobium leguminosarum
RT bv. phaseoli.";
RL J. Bacteriol. 173:2411-2419(1991).
RN [2] {ECO:0000313|EMBL:AAM54793.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CFN 42 {ECO:0000313|EMBL:AAM54793.1};
RC PLASMID=p42d {ECO:0000313|EMBL:AAM54793.1};
RX PubMed=9274036;
RA Ramirez-Romero M.A., Bustos P., Girard L., Rodriguez O., Cevallos M.A.,
RA Davila G.;
RT "Sequence, localization and characteristics of the replicator region of the
RT symbiotic plasmid of Rhizobium etli.";
RL Microbiology 143:2825-2831(1997).
RN [3] {ECO:0000313|EMBL:AAM54793.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CFN 42 {ECO:0000313|EMBL:AAM54793.1};
RC PLASMID=p42d {ECO:0000313|EMBL:AAM54793.1};
RA Ramirez M.A., Bustos P., Girard L., Rodriguez O., Cevallos M.A., Davila G.;
RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases.
RN [4] {ECO:0000313|EMBL:AAM54793.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CFN 42 {ECO:0000313|EMBL:AAM54793.1};
RC PLASMID=p42d {ECO:0000313|EMBL:AAM54793.1};
RX PubMed=12421308; DOI=10.1046/j.1365-2958.2002.03205.x;
RA Quintero V., Cevallos M.A., Davila G.;
RT "A site-specific recombinase (RinQ) is required to exert incompatibility
RT towards the symbiotic plasmid of Rhizobium etli.";
RL Mol. Microbiol. 46:1023-1032(2002).
RN [5] {ECO:0000313|Proteomes:UP000001936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFN 42 / ATCC 51251 {ECO:0000313|Proteomes:UP000001936};
RX PubMed=12801410; DOI=10.1186/gb-2003-4-6-r36;
RA Gonzalez V., Bustos P., Ramirez-Romero M.A., Medrano-Soto A., Salgado H.,
RA Hernandez-Gonzalez I., Hernandez-Celis J.C., Quintero V.,
RA Moreno-Hagelsieb G., Girard L., Rodriguez O., Flores M., Cevallos M.A.,
RA Collado-Vides J., Romero D., Davila G.;
RT "The mosaic structure of the symbiotic plasmid of Rhizobium etli CFN42 and
RT its relation to other symbiotic genome compartments.";
RL Genome Biol. 4:R36.1-R36.13(2003).
RN [6] {ECO:0000313|Proteomes:UP000001936}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CFN 42 / ATCC 51251 {ECO:0000313|Proteomes:UP000001936};
RX PubMed=16505379; DOI=10.1073/pnas.0508502103;
RA Gonzalez V., Santamaria R.I., Bustos P., Hernandez-Gonzalez I.,
RA Medrano-Soto A., Moreno-Hagelsieb G., Janga S.C., Ramirez M.A.,
RA Jimenez-Jacinto V., Collado-Vides J., Davila G.;
RT "The partitioned Rhizobium etli genome: genetic and metabolic redundancy in
RT seven interacting replicons.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:3834-3839(2006).
RN [7] {ECO:0000313|EMBL:AAM54793.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=CFN 42 {ECO:0000313|EMBL:AAM54793.1};
RC PLASMID=p42d {ECO:0000313|EMBL:AAM54793.1};
RA Gonzalez V.V.;
RT "The mosaic structure of the symbiotic plasmid of Rhizobium etli CFN42 and
RT its relation to other symbiotic genome compartments.";
RL Submitted (MAR-2006) 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-102 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; U80928; AAM54750.1; -; Genomic_DNA.
DR EMBL; U80928; AAM54793.1; -; Genomic_DNA.
DR EMBL; U80928; AAM54849.1; -; Genomic_DNA.
DR RefSeq; WP_004675840.1; NC_004041.2.
DR AlphaFoldDB; Q79BE9; -.
DR SMR; Q79BE9; -.
DR GeneID; 45960649; -.
DR KEGG; ret:RHE_PD00202; -.
DR KEGG; ret:RHE_PD00260; -.
DR KEGG; ret:RHE_PD00308; -.
DR HOGENOM; CLU_059373_0_0_5; -.
DR OrthoDB; 9778641at2; -.
DR Proteomes; UP000001936; Plasmid sym p42d.
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}; Plasmid {ECO:0000313|EMBL:AAM54793.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001936}.
FT BINDING 11..18
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_00533"
FT BINDING 99
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 102
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 297 AA; 31966 MW; 1AEEB5F5AB080879 CRC64;
MSDLRQIAFY GKGGIGKSTT SQNTLAALVD LGQKILIVGC DPKADSTRLI LNAKAQDTVL
HLAAQEGSVE DLELEDVLKA GYKGIKCVES GGPEPGVGCA GRGVITSINF LEENGAYDDV
DYVSYDVLGD VVCGGFAMPI RENKAQEIYI VMSGEMMALY AANNIAKGIL KYAHSGGVRL
GGLICNERQT DRELDLSEAL AARLNSKLIH FVPRDNIVQH AELRKMTVIQ YAPDSKQAGE
YRALAEKIHA NSGQGTIPTP ITMEELEDML LDFGIMKSDE QMLAELQAKE SAVVAAQ
//
