VNFD_AZOCH
ID VNFD_AZOCH Reviewed; 473 AA.
AC P15332;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Nitrogenase vanadium-iron protein alpha chain;
DE EC=1.18.6.1;
DE AltName: Full=Dinitrogenase 2 subunit alpha;
DE AltName: Full=Nitrogenase component I;
GN Name=vnfD;
OS Azotobacter chroococcum mcd 1.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=355;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2388847; DOI=10.1093/nar/18.15.4616;
RA Fallik E., Robson R.L.;
RT "Completed sequence of the region encoding the structural genes for the
RT vanadium nitrogenase of Azotobacter chroococcum.";
RL Nucleic Acids Res. 18:4616-4616(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-11.
RX PubMed=2743980; DOI=10.1002/j.1460-2075.1989.tb03495.x;
RA Robson R.L., Woodley P.R., Pau R.N., Eady R.R.;
RT "Structural genes for the vanadium nitrogenase from Azotobacter
RT chroococcum.";
RL EMBO J. 8:1217-1224(1989).
CC -!- FUNCTION: This vanadium-iron protein is part of the nitrogenase complex
CC that catalyzes the key enzymatic reactions in nitrogen 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-V-9S-C-homocitryl] cluster; Xref=ChEBI:CHEBI:60357;
CC Evidence={ECO:0000250};
CC Note=Binds 1 [7Fe-V-9S-C-homocitryl] cluster per subunit.
CC {ECO:0000250};
CC -!- SUBUNIT: Hexamer of two alpha, two beta, and two delta chains.
CC -!- MISCELLANEOUS: The structure of the 7Fe-V-9S-C-homocitryl cluster is
CC assumed to be analogous to the 7Fe-Mo-9S-C-homocitryl cluster.
CC -!- SIMILARITY: Belongs to the NifD/NifK/NifE/NifN family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; X51756; CAA36058.1; -; Genomic_DNA.
DR EMBL; X15077; CAA33173.1; -; Genomic_DNA.
DR PIR; S04113; S04113.
DR AlphaFoldDB; P15332; -.
DR SMR; P15332; -.
DR BRENDA; 1.18.6.2; 617.
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:0016163; F:nitrogenase activity; IEA:UniProtKB-EC.
DR GO; GO:0051212; F:vanadium ion binding; IEA:InterPro.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR InterPro; IPR000510; Nase/OxRdtase_comp1.
DR InterPro; IPR005974; Nase_asu.
DR InterPro; IPR010143; Nase_comp1_asu.
DR InterPro; IPR000318; Nase_comp1_CS.
DR InterPro; IPR010142; Nase_V-Fe_asu.
DR PANTHER; PTHR43457; PTHR43457; 1.
DR Pfam; PF00148; Oxidored_nitro; 1.
DR TIGRFAMs; TIGR01284; alt_nitrog_alph; 1.
DR TIGRFAMs; TIGR01862; N2-ase-Ialpha; 1.
DR TIGRFAMs; TIGR01860; VNFD; 1.
DR PROSITE; PS00699; NITROGENASE_1_1; 1.
DR PROSITE; PS00090; NITROGENASE_1_2; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Direct protein sequencing; Iron; Iron-sulfur; Metal-binding;
KW Nitrogen fixation; Nucleotide-binding; Oxidoreductase; Vanadium.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2743980"
FT CHAIN 2..473
FT /note="Nitrogenase vanadium-iron protein alpha chain"
FT /id="PRO_0000153055"
FT BINDING 49
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 74
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 137
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 256
FT /ligand="[7Fe-V-9S-C-homocitryl] cluster"
FT /ligand_id="ChEBI:CHEBI:60357"
FT /evidence="ECO:0000250"
FT BINDING 422
FT /ligand="[7Fe-V-9S-C-homocitryl] cluster"
FT /ligand_id="ChEBI:CHEBI:60357"
FT /evidence="ECO:0000250"
FT CONFLICT 50..53
FT /note="LLRR -> AFCGA (in Ref. 1; CAA36058)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 473 AA; 53993 MW; 2C1CE3FB8C6AEAED CRC64;
MPMVLLECDK DIPERQKHIY LKAPNEDTRE FLPIANAATI PGTLSERGCL LRRKLVIGGV
LKDTIQMIHG PLGCAYDTWH TKRYPTDNGH FNMKYVWSTD MKESHVVFGG EKRLEQRMHE
AFDEMPDIKR MIVYTTCPTA LIGDDIKAVA KKVMKERPDV DVFTVECPGF SGVSQSKGHH
VLNIGWINEK VETMEKEITS EYTMNFIGDF NIQGDTQLLQ TYWDRLGIQV VAHFTGNGTY
DDLRCMHQAQ LNVVNCARSS GYIANELKKR YGIPRLDIDS WGFSYMAEGI RKICAFFGIE
EKGERLIAEE YAKWKPKLDW YKERLQGKKM AIWTGGPRLW HWTKSVEDDL GIQVVAMSSK
FGHEEDFEKV IARGKEGTYY IDDGNELEFF EIIDLVKPDV IFTGPRVGEL VKKLHIPYVN
GHGYHNGPYM GFEGFVNLAR DTYNAVHNPL RHLAAVDIRD SSQTTPVIVR GAA