ID C6G471_9BRAD Unreviewed; 240 AA.
AC C6G471;
DT 01-SEP-2009, integrated into UniProtKB/TrEMBL.
DT 01-SEP-2009, sequence version 1.
DT 24-JAN-2024, entry version 61.
DE RecName: Full=nitrogenase {ECO:0000256|ARBA:ARBA00012773};
DE EC=1.18.6.1 {ECO:0000256|ARBA:ARBA00012773};
DE AltName: Full=Nitrogenase component II {ECO:0000256|ARBA:ARBA00029951};
DE AltName: Full=Nitrogenase reductase {ECO:0000256|ARBA:ARBA00033027};
DE Flags: Fragment;
GN Name=nifH {ECO:0000313|EMBL:ACS89059.1};
OS Bradyrhizobium yuanmingense.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Bradyrhizobium.
OX NCBI_TaxID=108015 {ECO:0000313|EMBL:ACS89059.1};
RN [1] {ECO:0000313|EMBL:ACS89059.1}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=SR50 {ECO:0000313|EMBL:ACS89059.1};
RX PubMed=19541444; DOI=10.1016/j.syapm.2009.05.005;
RA Appunu C., N'Zoue A., Moulin L., Depret G., Laguerre G.;
RT "Vigna mungo, V. radiata and V. unguiculata plants sampled in different
RT agronomical-ecological-climatic regions of India are nodulated by
RT Bradyrhizobium yuanmingense.";
RL Syst. Appl. Microbiol. 32:460-470(2009).
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};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SUBUNIT: Homodimer. {ECO:0000256|ARBA:ARBA00011738}.
CC -!- PTM: The reversible ADP-ribosylation of Arg inactivates the nitrogenase
CC reductase and regulates nitrogenase activity.
CC {ECO:0000256|PIRSR:PIRSR605977-50}.
CC -!- SIMILARITY: Belongs to the NifH/BchL/ChlL family.
CC {ECO:0000256|ARBA:ARBA00005504, ECO:0000256|RuleBase:RU003688}.
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DR EMBL; FJ514068; ACS89059.1; -; Genomic_DNA.
DR AlphaFoldDB; C6G471; -.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
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-EC.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR CDD; cd02040; NifH; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 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|RuleBase:RU003688};
KW ADP-ribosylation {ECO:0000256|ARBA:ARBA00022765,
KW ECO:0000256|PIRSR:PIRSR605977-50};
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|RuleBase:RU003688};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU003688};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU003688};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU003688};
KW Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741,
KW ECO:0000256|RuleBase:RU003688};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU003688}.
FT MOD_RES 88
FT /note="ADP-ribosylarginine; by dinitrogenase reductase ADP-
FT ribosyltransferase"
FT /evidence="ECO:0000256|PIRSR:PIRSR605977-50"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:ACS89059.1"
FT NON_TER 240
FT /evidence="ECO:0000313|EMBL:ACS89059.1"
SQ SEQUENCE 240 AA; 25904 MW; 1D5176806CBBD1D1 CRC64;
IGKSTTSQNT LAALAEMGQK ILIVGCDPKA DSTRLILHAK AQDTILSLAA SAGSVEDLEL
EDVMKVGYKD IRCVESGGPE PGVGCAGRGV ITSINFLEEN GAYENIDYVS YDVLGDVVCG
GFAMPIRENK AQEIYIVMSG EMMAMYAANN ISKGILKYAN SGGVRLGGLI CNERQTDKEL
ELAEALAKKL GTQLIYFVPR DNVVQHAELR RMTVLEYAPD SKQADHYRNL ATKVHNNGGK
//
