ANFD_RUMHU
ID ANFD_RUMHU Reviewed; 518 AA.
AC Q46082;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 20-DEC-2005, sequence version 2.
DT 03-AUG-2022, entry version 90.
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 Ruminiclostridium hungatei (Clostridium hungatei).
OC Bacteria; Firmicutes; Clostridia; Eubacteriales; Oscillospiraceae;
OC Ruminiclostridium.
OX NCBI_TaxID=48256;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=B3B;
RA Chen T., Leschine S.B.;
RL Submitted (MAY-1996) to the EMBL/GenBank/DDBJ databases.
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 {ECO:0000250}.
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 -!- SEQUENCE CAUTION:
CC Sequence=AAB02935.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; U59415; AAB02935.1; ALT_FRAME; Genomic_DNA.
DR AlphaFoldDB; Q46082; -.
DR SMR; Q46082; -.
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.
PE 3: Inferred from homology;
KW ATP-binding; Iron; Iron-sulfur; Metal-binding; Nitrogen fixation;
KW Nucleotide-binding; Oxidoreductase.
FT CHAIN 1..518
FT /note="Nitrogenase iron-iron protein alpha chain"
FT /id="PRO_0000153063"
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 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 518 AA; 58647 MW; 95B10456D69D02AA CRC64;
MPHHEFECSK VIPERKKHAV IKGKGETLAD ALPQGYLNTI PGSISERGCA YCVAKHVIGT
PMKDVIHISH GPVGCTYDTW QTKRYISDND NFQLKYTYAT DVKEKHIVFG AEKLLKQNII
EAFKRFPQIK RMTIYQTPCT ALIGDDINAI AEEVMEEMPE VDIFVCNSPG FAGPSQSGGH
HKINIAWINQ KVGTVEPEIT GDHVINYVGE YNIQGDQEVM VDYFKRMGIQ VLSTFTGNLS
YDGLRAMHRA HLNVLECARS AEYICNELRV RYGIPRLDID GFGFKPLADS LRKYGMFFGI
EDRRKAIIDE EVARWKPELD WYKERLMGKK VSVWPGGSKL WHWAHVIEEE MGLKVVSVYT
KFGHQGDMEK GMPRCGEGTL AIDDPNELEG LEALEMLKPD IILTGKRPGE VAKKVRVPYL
NAHAYHNGPY KGFEGWVRFA RDIYNAIYSP IHQLSGIDIT KDNAPEWGNG FRTRQMLSDG
NLSDAVRNSE TLAQYTGGYD SVSNVREREY PAFERKVG