VNFG_AZOVI
ID VNFG_AZOVI Reviewed; 113 AA.
AC P16857;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Nitrogenase vanadium-iron protein delta chain;
DE EC=1.18.6.1;
DE AltName: Full=Dinitrogenase 2 subunit delta;
DE AltName: Full=Nitrogenase component I;
GN Name=vnfG;
OS Azotobacter vinelandii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=354;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2345152; DOI=10.1128/jb.172.6.3400-3408.1990;
RA Joerger R.D., Loveless T.M., Pau R.N., Mitchenall L.A., Simon B.H.,
RA Bishop P.E.;
RT "Nucleotide sequences and mutational analysis of the structural genes for
RT nitrogenase 2 of Azotobacter vinelandii.";
RL J. Bacteriol. 172:3400-3408(1990).
CC -!- FUNCTION: The key enzymatic reactions in nitrogen fixation are
CC catalyzed by the nitrogenase complex, which has 2 components: the iron
CC protein (component 2) and a component 1 which is either a molybdenum-
CC iron protein, a vanadium-iron, or an iron-iron protein.
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=iron-sulfur cluster; Xref=ChEBI:CHEBI:30408;
CC -!- COFACTOR:
CC Name=vanadium cation; Xref=ChEBI:CHEBI:35172;
CC -!- SUBUNIT: Hexamer of two alpha, two beta, and two delta chains.
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DR EMBL; M32371; AAA22173.1; -; Genomic_DNA.
DR PIR; D35405; D35405.
DR RefSeq; WP_012698949.1; NZ_FPKM01000002.1.
DR PDB; 5N6Y; X-ray; 1.35 A; C/F=1-113.
DR PDB; 7ADR; X-ray; 1.00 A; C/F=1-113.
DR PDB; 7ADY; X-ray; 1.05 A; C/F=1-113.
DR PDB; 7AIZ; X-ray; 1.05 A; C/F=1-113.
DR PDBsum; 5N6Y; -.
DR PDBsum; 7ADR; -.
DR PDBsum; 7ADY; -.
DR PDBsum; 7AIZ; -.
DR AlphaFoldDB; P16857; -.
DR SMR; P16857; -.
DR DIP; DIP-48895N; -.
DR IntAct; P16857; 2.
DR OMA; SWDREEN; -.
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 InterPro; IPR014279; Nase_V-Fe_dsu.
DR InterPro; IPR004349; V/Nase_d_su.
DR Pfam; PF03139; AnfG_VnfG; 1.
DR TIGRFAMs; TIGR02930; vnfG_nitrog; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Iron; Iron-sulfur; Metal-binding;
KW Nitrogen fixation; Nucleotide-binding; Oxidoreductase; Vanadium.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..113
FT /note="Nitrogenase vanadium-iron protein delta chain"
FT /id="PRO_0000213564"
FT HELIX 2..16
FT /evidence="ECO:0007829|PDB:7ADR"
FT HELIX 19..21
FT /evidence="ECO:0007829|PDB:7ADR"
FT HELIX 25..43
FT /evidence="ECO:0007829|PDB:7ADR"
FT HELIX 53..72
FT /evidence="ECO:0007829|PDB:7ADR"
FT HELIX 74..77
FT /evidence="ECO:0007829|PDB:7ADR"
FT HELIX 81..99
FT /evidence="ECO:0007829|PDB:7ADR"
FT TURN 100..102
FT /evidence="ECO:0007829|PDB:7ADR"
FT TURN 106..109
FT /evidence="ECO:0007829|PDB:7ADR"
SQ SEQUENCE 113 AA; 13372 MW; CFA7E86AE2B08618 CRC64;
MSQSHLDDLF AYVEERCLWQ FFSRTWDREE NIEGVLNQVG RLLTGQEPLR GTPQERLFYA
DALAMANDVR ERFPWASQVN KEEIEFLLDG LKSRLVDVTI TRSTNRELNH HLY
