ID   ANFG_AZOVI              Reviewed;         132 AA.
AC   P16268;
DT   01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT   23-JAN-2007, sequence version 3.
DT   03-AUG-2022, entry version 79.
DE   RecName: Full=Nitrogenase iron-iron protein delta chain;
DE            EC=1.18.6.1;
DE   AltName: Full=Dinitrogenase 3 subunit delta;
DE   AltName: Full=Nitrogenase component I;
GN   Name=anfG;
OS   Azotobacter vinelandii.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=354;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2644222; DOI=10.1128/jb.171.2.1075-1086.1989;
RA   Joerger R.D., Jacobson M.R., Premakumar R., Wolfinger E.D., Bishop P.E.;
RT   "Nucleotide sequence and mutational analysis of the structural genes
RT   (anfHDGK) for the second alternative nitrogenase from Azotobacter
RT   vinelandii.";
RL   J. Bacteriol. 171:1075-1086(1989).
RN   [2]
RP   PROTEIN SEQUENCE OF 2-8.
RC   STRAIN=RP306;
RX   PubMed=8392330; DOI=10.1042/bj2930101;
RA   Pau R.N., Eldridge M.E., Lowe D.J., Mitchenall L.A., Eady R.R.;
RT   "Molybdenum-independent nitrogenases of Azotobacter vinelandii: a
RT   functional species of alternative nitrogenase-3 isolated from a molybdenum-
RT   tolerant strain contains an iron-molybdenum cofactor.";
RL   Biochem. J. 293:101-107(1993).
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   -!- SUBUNIT: Hexamer of two alpha, two beta, and two delta chains.
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DR   EMBL; M23528; AAA82510.1; -; Genomic_DNA.
DR   PIR; C32057; C32057.
DR   AlphaFoldDB; P16268; -.
DR   SMR; P16268; -.
DR   PRIDE; P16268; -.
DR   OMA; CYWVDAV; -.
DR   BioCyc; MetaCyc:MON-16522; -.
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:0005506; F:iron ion binding; IEA:InterPro.
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:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR   InterPro; IPR014278; Nase_Fe-Fe_dsu.
DR   InterPro; IPR004349; V/Nase_d_su.
DR   Pfam; PF03139; AnfG_VnfG; 1.
DR   TIGRFAMs; TIGR02929; anfG_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.
FT   INIT_MET        1
FT                   /note="Removed"
FT                   /evidence="ECO:0000269|PubMed:8392330"
FT   CHAIN           2..132
FT                   /note="Nitrogenase iron-iron protein delta chain"
FT                   /id="PRO_0000213563"
SQ   SEQUENCE   132 AA;  15343 MW;  A1C28194C835EA35 CRC64;
     MSTASAAAVV KQKVEAPVHP MDARIDELTD YIMKNCLWQF HSRSWDRERQ NAEILKKTKE
     LLCGEPVDLS TSHDRCYWVD AVCLADDYRE HYPWINSMSK EEIGSLMQGL KDRMDYLTIT
     GSLNEELSDK HY