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VNFK_AZOPA
ID   VNFK_AZOPA              Reviewed;         348 AA.
AC   O68949;
DT   15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT   01-AUG-1998, sequence version 1.
DT   03-AUG-2022, entry version 69.
DE   RecName: Full=Nitrogenase vanadium-iron protein beta chain;
DE            EC=1.18.6.1;
DE   AltName: Full=Dinitrogenase 2 subunit beta;
DE   AltName: Full=Nitrogenase component I;
DE   Flags: Fragment;
GN   Name=vnfK;
OS   Azorhizophilus paspali (Azotobacter paspali).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azorhizophilus.
OX   NCBI_TaxID=69963;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=10420583; DOI=10.1139/w99-007;
RA   Loveless T.M., Bishop P.E.;
RT   "Identification of genes unique to Mo-independent nitrogenase systems in
RT   diverse diazotrophs.";
RL   Can. J. Microbiol. 45:312-317(1999).
CC   -!- FUNCTION: This vanadium-iron protein is part of the nitrogenase complex
CC       that catalyzes the key enzymatic reactions in nitrogen fixation.
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   -!- SUBUNIT: Hexamer of two alpha, two beta, and two delta chains.
CC       {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the NifD/NifK/NifE/NifN family. {ECO:0000305}.
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DR   EMBL; AF058781; AAC14336.1; -; Genomic_DNA.
DR   AlphaFoldDB; O68949; -.
DR   SMR; O68949; -.
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; IPR000318; Nase_comp1_CS.
DR   Pfam; PF00148; Oxidored_nitro; 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..>348
FT                   /note="Nitrogenase vanadium-iron protein beta chain"
FT                   /id="PRO_0000153089"
FT   BINDING         31
FT                   /ligand="[8Fe-7S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21143"
FT                   /ligand_note="ligand shared with alpha chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         56
FT                   /ligand="[8Fe-7S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21143"
FT                   /ligand_note="ligand shared with alpha chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         115
FT                   /ligand="[8Fe-7S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21143"
FT                   /ligand_note="ligand shared with alpha chain"
FT                   /evidence="ECO:0000250"
FT   BINDING         153
FT                   /ligand="[8Fe-7S] cluster"
FT                   /ligand_id="ChEBI:CHEBI:21143"
FT                   /ligand_note="ligand shared with alpha chain"
FT                   /evidence="ECO:0000250"
FT   NON_TER         348
SQ   SEQUENCE   348 AA;  38112 MW;  2B1F223B50D08577 CRC64;
     MSNCELTVLK PAEVKLSPRD REGIINPMYD CQPAGAQYAG IGIKDCIPLV HGGQGCTMFV
     RLLFAQHFKE NFDVASTSLH EESAVFGGAK RVEEGVLVLA RRYPNLRVIP IITTCSTEVI
     GDDIEGSIRV CNRALEAEFP DRKIYLAPVH TPSFKGSHVT GYAECVKSVF KTITDAHGKG
     QPSGKLNVFP GWVNPGDVVL LKHYFKEMDV EANIYMDTED FDSPMLPNKS IETHGRTTVE
     DIADSANALA TLSLARYEGN TTGELLQKTF AVPNALVNTP YGIKNTDDML RKIAEVTGKE
     IPESLVRERG IALDALADLA HMFFANKKVA IFGHPDLVLG LAQFCIEV
 
 
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