NIFD_BRADU
ID NIFD_BRADU Reviewed; 500 AA.
AC P06121; Q52767; Q9ANN5;
DT 01-JAN-1988, integrated into UniProtKB/Swiss-Prot.
DT 28-FEB-2003, sequence version 2.
DT 03-AUG-2022, entry version 137.
DE RecName: Full=Nitrogenase molybdenum-iron protein alpha chain;
DE EC=1.18.6.1;
DE AltName: Full=Dinitrogenase;
DE AltName: Full=Nitrogenase component I;
GN Name=nifD; OrderedLocusNames=blr1743;
OS Bradyrhizobium diazoefficiens (strain JCM 10833 / BCRC 13528 / IAM 13628 /
OS NBRC 14792 / USDA 110).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Bradyrhizobiaceae; Bradyrhizobium.
OX NCBI_TaxID=224911;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RA Kaluza K., Hennecke H.;
RT "Fine structure analysis of the nifDK operon encoding the alpha and beta
RT subunits of dinitrogenase from Rhizobium japonicum.";
RL Mol. Gen. Genet. 196:35-42(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=USDA 110spc4;
RX PubMed=11157954; DOI=10.1128/jb.183.4.1405-1412.2001;
RA Goettfert M., Roethlisberger S., Kuendig C., Beck C., Marty R.,
RA Hennecke H.;
RT "Potential symbiosis-specific genes uncovered by sequencing a 410-kb DNA
RT region of the Bradyrhizobium japonicum chromosome.";
RL J. Bacteriol. 183:1405-1412(2001).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=12597275; DOI=10.1093/dnares/9.6.189;
RA Kaneko T., Nakamura Y., Sato S., Minamisawa K., Uchiumi T., Sasamoto S.,
RA Watanabe A., Idesawa K., Iriguchi M., Kawashima K., Kohara M.,
RA Matsumoto M., Shimpo S., Tsuruoka H., Wada T., Yamada M., Tabata S.;
RT "Complete genomic sequence of nitrogen-fixing symbiotic bacterium
RT Bradyrhizobium japonicum USDA110.";
RL DNA Res. 9:189-197(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-116.
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RX PubMed=6588133;
RA Adams T.H., Chelm B.K.;
RT "The nifH and nifDK promoter regions from Rhizobium japonicum share
RT structural homologies with each other and with nitrogen-regulated promoters
RT from other organisms.";
RL J. Mol. Appl. Genet. 2:392-405(1984).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 496-500.
RC STRAIN=JCM 10833 / BCRC 13528 / IAM 13628 / NBRC 14792 / USDA 110;
RA Thoeny B., Kaluza K., Hennecke H.;
RT "Structural and functional homology between the alpha and beta subunits of
RT the nitrogenase MoFe protein as revealed by sequencing the Rhizobium
RT japonicum nifK gene.";
RL Mol. Gen. Genet. 198:441-448(1985).
CC -!- FUNCTION: This molybdenum-iron protein is part of the nitrogenase
CC complex that catalyzes the key enzymatic reactions in nitrogen
CC fixation.
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 -!- COFACTOR:
CC Name=[8Fe-7S] cluster; Xref=ChEBI:CHEBI:21143; Evidence={ECO:0000250};
CC Note=Binds 1 [8Fe-7S] cluster per heterodimer. {ECO:0000250};
CC -!- COFACTOR:
CC Name=[7Fe-Mo-9S-C-homocitryl] cluster; Xref=ChEBI:CHEBI:30409;
CC Evidence={ECO:0000250};
CC Note=Binds 1 [7Fe-Mo-9S-C-homocitryl] cluster per subunit.
CC {ECO:0000250};
CC -!- SUBUNIT: Tetramer of two alpha and two beta chains. Forms complex with
CC the iron protein (nitrogenase component 2).
CC -!- SIMILARITY: Belongs to the NifD/NifK/NifE/NifN family. {ECO:0000305}.
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DR EMBL; X01045; CAA25523.1; -; Genomic_DNA.
DR EMBL; AF322012; AAG60729.1; -; Genomic_DNA.
DR EMBL; BA000040; BAC47008.1; -; Genomic_DNA.
DR EMBL; K01621; AAA26310.1; -; Genomic_DNA.
DR EMBL; M64591; AAA26325.1; -; Genomic_DNA.
DR PIR; S07301; NIZJAM.
DR RefSeq; NP_768383.1; NC_004463.1.
DR RefSeq; WP_011084552.1; NZ_CP011360.1.
DR AlphaFoldDB; P06121; -.
DR SMR; P06121; -.
DR STRING; 224911.27349996; -.
DR EnsemblBacteria; BAC47008; BAC47008; BAC47008.
DR GeneID; 64067050; -.
DR KEGG; bja:blr1743; -.
DR PATRIC; fig|224911.44.peg.1208; -.
DR eggNOG; COG2710; Bacteria.
DR HOGENOM; CLU_025876_1_1_5; -.
DR InParanoid; P06121; -.
DR OMA; CGQYSWA; -.
DR PhylomeDB; P06121; -.
DR Proteomes; UP000002526; Chromosome.
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 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 PANTHER; PTHR43457; PTHR43457; 1.
DR Pfam; PF00148; Oxidored_nitro; 1.
DR TIGRFAMs; TIGR01862; N2-ase-Ialpha; 1.
DR TIGRFAMs; TIGR01282; nifD; 1.
DR PROSITE; PS00699; NITROGENASE_1_1; 1.
DR PROSITE; PS00090; NITROGENASE_1_2; 1.
PE 3: Inferred from homology;
KW ATP-binding; Iron; Iron-sulfur; Metal-binding; Molybdenum;
KW Nitrogen fixation; Nucleotide-binding; Oxidoreductase; Reference proteome.
FT CHAIN 1..500
FT /note="Nitrogenase molybdenum-iron protein alpha chain"
FT /id="PRO_0000153061"
FT BINDING 67
FT /ligand="[8Fe-7S] cluster"
FT /ligand_id="ChEBI:CHEBI:21143"
FT /ligand_note="ligand shared with beta chain"
FT /evidence="ECO:0000250"
FT BINDING 93
FT /ligand="[8Fe-7S] cluster"
FT /ligand_id="ChEBI:CHEBI:21143"
FT /ligand_note="ligand shared with beta chain"
FT /evidence="ECO:0000250"
FT BINDING 159
FT /ligand="[8Fe-7S] cluster"
FT /ligand_id="ChEBI:CHEBI:21143"
FT /ligand_note="ligand shared with beta chain"
FT /evidence="ECO:0000250"
FT BINDING 283
FT /ligand="[7Fe-Mo-9S-C-homocitryl] cluster"
FT /ligand_id="ChEBI:CHEBI:30409"
FT /evidence="ECO:0000250"
FT BINDING 451
FT /ligand="[7Fe-Mo-9S-C-homocitryl] cluster"
FT /ligand_id="ChEBI:CHEBI:30409"
FT /evidence="ECO:0000250"
FT CONFLICT 24
FT /note="L -> P (in Ref. 4; AAA26310)"
FT /evidence="ECO:0000305"
FT CONFLICT 36
FT /note="A -> R (in Ref. 4; AAA26310)"
FT /evidence="ECO:0000305"
FT CONFLICT 58
FT /note="I -> R (in Ref. 4; AAA26310)"
FT /evidence="ECO:0000305"
FT CONFLICT 101
FT /note="R -> G (in Ref. 4; AAA26310)"
FT /evidence="ECO:0000305"
FT CONFLICT 424
FT /note="K -> R (in Ref. 1; CAA25523)"
FT /evidence="ECO:0000305"
FT CONFLICT 490..500
FT /note="EAPSAKLQAAE -> DAERQDSRLQNNATRLALRESPGIPI (in Ref.
FT 1; AAA26325)"
FT /evidence="ECO:0000305"
FT CONFLICT 498..500
FT /note="AAE -> NNATRLALRESPGIPI (in Ref. 5)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 500 AA; 56157 MW; BEAB61673A651107 CRC64;
MSLATTNSVA EIRARNKELI EEVLKVYPEK TAKRRAKHLN VHQAGKSDCG VKSNIKSIPG
VMTIRGCAYA GSKGVVWGPI KDMVHISHGP VGCGQYSWGS RRNYYVGTTG IDSFVTLQFT
SDFQEKDIVF GGDKKLDKIL DEIQELFPLN NGITIQSECP VGLIGDDIEA VSRAKSKEYG
GKTIVPVRCE GFRGVSQSLG HHIANDAVRD WIFGHIEAEG KPKFEPTPYD VAIIGDYNIG
GDAWSSRILL EEMGLRVIAQ WSGDGSLAEL EATPKAKLNI LHCYRSMNYI SRHMEEKFGI
PWCEYNFFGP SKIADSLRRI AGYFDDKIKE GAERVIEKYQ PLVDAVIAKY RPRLEGKTVM
LYVGGLRPRH VIGAYEDLGM DVIGTGYEFG HNDDYQRTAQ HYVKDSTLIY DDVNGYEFER
FVEKLQPDLV GSGIKEKYVF QKMSVPFRQM HSWDYSGPYH GYDGFAIFAR DMDMAVNSPI
WKRTKAPWKE APSAKLQAAE
