ID Q9AJ61_9BACT Unreviewed; 479 AA.
AC Q9AJ61;
DT 01-JUN-2001, integrated into UniProtKB/TrEMBL.
DT 01-JUN-2001, sequence version 1.
DT 27-MAR-2024, entry version 63.
DE RecName: Full=Nitrogenase protein alpha chain {ECO:0000256|RuleBase:RU004022};
DE EC=1.18.6.1 {ECO:0000256|RuleBase:RU004022};
GN Name=nifD {ECO:0000313|EMBL:AAK26106.1};
OS uncultured bacterium.
OC Bacteria; environmental samples.
OX NCBI_TaxID=77133 {ECO:0000313|EMBL:AAK26106.1};
RN [1] {ECO:0000313|EMBL:AAK26106.1}
RP NUCLEOTIDE SEQUENCE.
RX PubMed=11157237; DOI=10.1128/AEM.67.2.725-732.2001;
RA Minerdi D., Fani R., Gallo R., Boarino A., Bonfante P.;
RT "Nitrogen fixation genes in an endosymbiotic Burkholderia strain.";
RL Appl. Environ. Microbiol. 67:725-732(2001).
CC -!- FUNCTION: This molybdenum-iron protein is part of the nitrogenase
CC complex that catalyzes the key enzymatic reactions in nitrogen
CC fixation. {ECO:0000256|ARBA:ARBA00002621}.
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 ECO:0000256|RuleBase:RU004022};
CC -!- COFACTOR:
CC Name=[7Fe-Mo-9S-C-homocitryl] cluster; Xref=ChEBI:CHEBI:30409;
CC Evidence={ECO:0000256|ARBA:ARBA00001969};
CC -!- COFACTOR:
CC Name=[8Fe-7S] cluster; Xref=ChEBI:CHEBI:21143;
CC Evidence={ECO:0000256|ARBA:ARBA00001919};
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains. Forms complex with
CC the iron protein (nitrogenase component 2).
CC {ECO:0000256|ARBA:ARBA00011462}.
CC -!- SIMILARITY: Belongs to the NifD/NifK/NifE/NifN family.
CC {ECO:0000256|RuleBase:RU004021}.
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DR EMBL; AF194084; AAK26106.1; -; Genomic_DNA.
DR AlphaFoldDB; Q9AJ61; -.
DR GO; GO:0016612; C:molybdenum-iron nitrogenase complex; IEA:InterPro.
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:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
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; cd01976; Nitrogenase_MoFe_alpha; 1.
DR Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 3.
DR InterPro; IPR000510; Nase/OxRdtase_comp1.
DR InterPro; IPR010143; Nase_comp1_asu.
DR InterPro; IPR000318; Nase_comp1_CS.
DR InterPro; IPR005972; Nase_Mo-Fe_asu.
DR NCBIfam; TIGR01862; N2-ase-Ialpha; 1.
DR NCBIfam; TIGR01282; nifD; 1.
DR PANTHER; PTHR43457; NITROGENASE MOLYBDENUM-IRON PROTEIN ALPHA CHAIN; 1.
DR PANTHER; PTHR43457:SF1; NITROGENASE MOLYBDENUM-IRON PROTEIN ALPHA CHAIN; 1.
DR Pfam; PF00148; Oxidored_nitro; 1.
DR SUPFAM; SSF53807; Helical backbone' metal receptor; 1.
DR PROSITE; PS00699; NITROGENASE_1_1; 1.
DR PROSITE; PS00090; NITROGENASE_1_2; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU004022};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723,
KW ECO:0000256|RuleBase:RU004022}; Molybdenum {ECO:0000256|ARBA:ARBA00022505};
KW Nitrogen fixation {ECO:0000256|ARBA:ARBA00023231,
KW ECO:0000256|RuleBase:RU004021};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Oxidoreductase {ECO:0000256|ARBA:ARBA00023002,
KW ECO:0000256|RuleBase:RU004022}.
FT DOMAIN 62..466
FT /note="Nitrogenase/oxidoreductase component 1"
FT /evidence="ECO:0000259|Pfam:PF00148"
SQ SEQUENCE 479 AA; 53939 MW; E6ACFAAECA82F915 CRC64;
MSLSENTTVD VKALVNDVLE AYPEKTRKRR AKHINVLEAE AKDCGVKSNV KSIPGVMTIR
GCAYAGSKGV VWGPIKDMIH ISHGPVGCGY YSWSGRRNYY IGDTGIDSWG TMHFTSDFQE
KDIVFGGDKK LHKVIEEIND LFPLVNGISI QSECPIGLIG DDIEAVARVK SAEIGKPVIP
VRCEGFRGVS QSLGHHIAND TIRDWVFEKT TPKADFVSTP YDVTIIGDYN IGGDAWSSRI
LLEEMGLRVI SQWSGDGTLA ELENTPKAKV NLIHCYRSMN YIARHMEEKY NIPWMEYNFF
GPSQIAESLR KIAALFDDSI KEKAEAVIAR YQPMVDAVIA KYRTRLEGKK VMLYVGGLRP
RHVVDAYHDL GMEVVGTGYE FAHNDDYQRT QHYVKEGTLI YDDVTAFELE KFVEALRPDL
VASGIKEKYV FQKMGLPFRQ MHSWDYSGPY HGYDGFAIFA RDMDLAINNP VWGVMKAPF
//
