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ANFD_RHOCA
ID   ANFD_RHOCA              Reviewed;         526 AA.
AC   Q07933;
DT   01-FEB-1995, integrated into UniProtKB/Swiss-Prot.
DT   01-FEB-1995, sequence version 1.
DT   03-AUG-2022, entry version 83.
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   Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC   STRAIN=B10S;
RX   PubMed=8332060; DOI=10.1111/j.1365-2958.1993.tb01611.x;
RA   Schueddekopf K., Hennecke S., Liese U., Kutsche M., Klipp W.;
RT   "Characterization of anf genes specific for the alternative nitrogenase and
RT   identification of nif genes required for both nitrogenases in Rhodobacter
RT   capsulatus.";
RL   Mol. Microbiol. 8:673-684(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; X70033; CAA49625.1; -; Genomic_DNA.
DR   PIR; S34945; S34945.
DR   AlphaFoldDB; Q07933; -.
DR   SMR; Q07933; -.
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   3: Inferred from homology;
KW   ATP-binding; Iron; Iron-sulfur; Metal-binding; Nitrogen fixation;
KW   Nucleotide-binding; Oxidoreductase.
FT   CHAIN           1..526
FT                   /note="Nitrogenase iron-iron protein alpha chain"
FT                   /id="PRO_0000153082"
FT   REGION          507..526
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
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"
SQ   SEQUENCE   526 AA;  59061 MW;  D6AD51EA40421074 CRC64;
     MPYHEFEVSK CIPERREHAV MKAAGEDLTS CLPKGYLNTI PGTISERGCA YCGAKHVIGT
     PMKDVIHISH GPNGCTYDTW QTKRYISDND NFQLKYTFAT DVKEKHVVFG AEGLLKKSMH
     EAFDAFPNIK RMTVYQTCTT ALIGDDVDAI AKEVMEERGD VDVFVCNSPG FAGPSQSGGH
     HKINIAWLNQ KVGTVEPDYL GEHVINYVGE YNIQGDQEVM IDYFNRMGIQ VLSTFTGNGS
     YDSLRMMHRA HLNVLECARS AEYICDELRA RYGIPRLDID GFGFEPLANS LRKVALFFGI
     EDKAEAIIAE EYAKWKPQLD WYKERLKGKK VCLWPGGSKL WHWAHAIEEE MGLKVVSVYT
     KFGHQGDMEK GVSRCGEGAL AIDDPNELES VEAIEMLKPD IIFTGKRPGE FVKKHGVPYL
     NAHAYHNGPY KGFEGWVRFA RDIYNAIYSP MRQLAALDIS APDAAITSGF RTAKMNADLT
     VSDEVKFSEV LHEYTGKYDS IAEIRARNQP MPPSRKLRDA VQPAAE
 
 
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