ID   VNFG_AZOCH              Reviewed;         113 AA.
AC   P15333;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 2.
DT   25-MAY-2022, entry version 69.
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 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 2-16.
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: 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; X51756; CAA36059.1; -; Genomic_DNA.
DR   EMBL; X15077; CAA33174.1; -; Genomic_DNA.
DR   PIR; S04114; S04114.
DR   AlphaFoldDB; P15333; -.
DR   SMR; P15333; -.
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: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   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..113
FT                   /note="Nitrogenase vanadium-iron protein delta chain"
FT                   /id="PRO_0000213560"
SQ   SEQUENCE   113 AA;  13364 MW;  2B741CA78A4ACECD CRC64;
     MSQSHLDDLF DYTEERCLWQ FFSRTWDREE NIEGVLGQVA RLLTGQEPLR GTPQERLFYA
     DALAMANDVR ERFPWASQIN HEEIHFLIDG LKSRLVDTVI QSSTNRELNH HLY