ANFD_AZOVI
ID ANFD_AZOVI Reviewed; 518 AA.
AC P16266;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 3.
DT 03-AUG-2022, entry version 98.
DE RecName: Full=Nitrogenase iron-iron protein alpha chain;
DE EC=1.18.6.1;
DE AltName: Full=Dinitrogenase 3 subunit alpha;
DE AltName: Full=Nitrogenase component I;
GN Name=anfD;
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 2-7.
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: This iron-iron protein is part of the nitrogenase complex
CC that catalyzes the key enzymatic reactions in nitrogen fixation. Other
CC nitrogenase complexes utilize a molybdenum-iron protein or a vanadium-
CC 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=[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=[8Fe-9S-C-homocitryl] cluster; Xref=ChEBI:CHEBI:60504;
CC Evidence={ECO:0000250};
CC Note=Binds 1 [8Fe-9S-C-homocitryl] cluster per subunit. {ECO:0000250};
CC -!- SUBUNIT: Hexamer of two alpha, two beta, and two delta chains.
CC -!- MISCELLANEOUS: The structure of the 8Fe-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}.
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DR EMBL; M23528; AAA82509.1; -; Genomic_DNA.
DR PIR; B32057; B32057.
DR AlphaFoldDB; P16266; -.
DR SMR; P16266; -.
DR BioCyc; MetaCyc:MON-16520; -.
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; IPR000510; Nase/OxRdtase_comp1.
DR InterPro; IPR005974; Nase_asu.
DR InterPro; IPR010143; Nase_comp1_asu.
DR InterPro; IPR000318; Nase_comp1_CS.
DR InterPro; IPR011290; Nase_Fe-Fe_asu.
DR PANTHER; PTHR43457; PTHR43457; 1.
DR Pfam; PF00148; Oxidored_nitro; 1.
DR TIGRFAMs; TIGR01284; alt_nitrog_alph; 1.
DR TIGRFAMs; TIGR01861; ANFD; 1.
DR TIGRFAMs; TIGR01862; N2-ase-Ialpha; 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.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:8392330"
FT CHAIN 2..518
FT /note="Nitrogenase iron-iron protein alpha chain"
FT /id="PRO_0000153059"
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 75
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 138
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 257
FT /ligand="[8Fe-9S-C-homocitryl] cluster"
FT /ligand_id="ChEBI:CHEBI:60504"
FT /evidence="ECO:0000250"
FT BINDING 423
FT /ligand="[8Fe-9S-C-homocitryl] cluster"
FT /ligand_id="ChEBI:CHEBI:60504"
FT /evidence="ECO:0000250"
FT CONFLICT 4
FT /note="H -> E (in Ref. 2; AA sequence)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 518 AA; 58414 MW; 414B513BD2F6EB1F CRC64;
MPHHEFECSK VIPERKKHAV IKGKGETLAD ALPQGYLNTI PGSISERGCA YCGAKHVIGT
PMKDVIHISH GPVGCTYDTW QTKRYISDND NFQLKYTYAT DVKEKHIVFG AEKLLKQNII
EAFKAFPQIK RMTIYQTCAT ALIGDDINAI AEEVMEEMPE VDIFVCNSPG FAGPSQSGGH
HKINIAWINQ KVGTVEPEIT GDHVINYVGE YNIQGDQEVM VDYFKRMGIQ VLSTFTGNGS
YDGLRAMHRA HLNVLECARS AEYICNELRV RYGIPRLDID GFGFKPLADS LRKIGMFFGI
EDRAKAIIDE EVARWKPELD WYKERLMGKK VCLWPGGSKL WHWAHVIEEE MGLKVVSVYI
KFGHQGDMEK GIARCGEGTL AIDDPNELEG LEALEMLKPD IILTGKRPGE VAKKVRVPYL
NAHAYHNGPY KGFEGWVRFA RDIYNAIYSP IHQLSGIDIT KDNAPEWGNG FRTRQMLSDG
NLSDAVRNSE TLRQYTGGYD SVSKLREREY PAFERKVG
