VNFK_AZOVI
ID VNFK_AZOVI Reviewed; 475 AA.
AC P16856;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 94.
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;
GN Name=vnfK;
OS Azotobacter vinelandii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=354;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2345152; DOI=10.1128/jb.172.6.3400-3408.1990;
RA Joerger R.D., Loveless T.M., Pau R.N., Mitchenall L.A., Simon B.H.,
RA Bishop P.E.;
RT "Nucleotide sequences and mutational analysis of the structural genes for
RT nitrogenase 2 of Azotobacter vinelandii.";
RL J. Bacteriol. 172:3400-3408(1990).
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 -!- SIMILARITY: Belongs to the NifD/NifK/NifE/NifN family. {ECO:0000305}.
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DR EMBL; M32371; AAA22174.1; -; Genomic_DNA.
DR PIR; E35405; E35405.
DR RefSeq; WP_012698948.1; NZ_FPKM01000002.1.
DR PDB; 5N6Y; X-ray; 1.35 A; B/E=1-475.
DR PDB; 7ADR; X-ray; 1.00 A; B/E=1-475.
DR PDB; 7ADY; X-ray; 1.05 A; B/E=1-475.
DR PDB; 7AIZ; X-ray; 1.05 A; B/E=1-475.
DR PDBsum; 5N6Y; -.
DR PDBsum; 7ADR; -.
DR PDBsum; 7ADY; -.
DR PDBsum; 7AIZ; -.
DR AlphaFoldDB; P16856; -.
DR SMR; P16856; -.
DR DIP; DIP-48894N; -.
DR IntAct; P16856; 2.
DR PRIDE; P16856; -.
DR OMA; LAHMFFA; -.
DR GO; GO:0016613; C:vanadium-iron nitrogenase complex; IEA:InterPro.
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 InterPro; IPR014281; Nase_VnfK.
DR Pfam; PF00148; Oxidored_nitro; 1.
DR TIGRFAMs; TIGR02932; vnfK_nitrog; 1.
DR PROSITE; PS00699; NITROGENASE_1_1; 1.
DR PROSITE; PS00090; NITROGENASE_1_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP-binding; Iron; Iron-sulfur; Metal-binding;
KW Nitrogen fixation; Nucleotide-binding; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT CHAIN 2..475
FT /note="Nitrogenase vanadium-iron protein beta chain"
FT /id="PRO_0000153093"
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 STRAND 14..18
FT /evidence="ECO:0007829|PDB:7ADR"
FT STRAND 22..26
FT /evidence="ECO:0007829|PDB:7ADR"
FT HELIX 32..41
FT /evidence="ECO:0007829|PDB:7ADR"
FT STRAND 49..52
FT /evidence="ECO:0007829|PDB:7ADR"
FT HELIX 55..68
FT /evidence="ECO:0007829|PDB:7ADR"
FT HELIX 81..86
FT /evidence="ECO:0007829|PDB:7ADR"
FT HELIX 89..102
FT /evidence="ECO:0007829|PDB:7ADR"
FT STRAND 108..113
FT /evidence="ECO:0007829|PDB:7ADR"
FT HELIX 115..120
FT /evidence="ECO:0007829|PDB:7ADR"
FT HELIX 124..138
FT /evidence="ECO:0007829|PDB:7ADR"
FT STRAND 145..149
FT /evidence="ECO:0007829|PDB:7ADR"
FT HELIX 158..177
FT /evidence="ECO:0007829|PDB:7ADR"
FT STRAND 186..189
FT /evidence="ECO:0007829|PDB:7ADR"
FT HELIX 195..207
FT /evidence="ECO:0007829|PDB:7ADR"
FT STRAND 212..216
FT /evidence="ECO:0007829|PDB:7ADR"
FT HELIX 219..221
FT /evidence="ECO:0007829|PDB:7ADR"
FT HELIX 239..243
FT /evidence="ECO:0007829|PDB:7ADR"
FT HELIX 244..247
FT /evidence="ECO:0007829|PDB:7ADR"
FT STRAND 249..253
FT /evidence="ECO:0007829|PDB:7ADR"
FT TURN 256..259
FT /evidence="ECO:0007829|PDB:7ADR"
FT HELIX 260..270
FT /evidence="ECO:0007829|PDB:7ADR"
FT STRAND 274..276
FT /evidence="ECO:0007829|PDB:7ADR"
FT HELIX 283..297
FT /evidence="ECO:0007829|PDB:7ADR"
FT HELIX 303..317
FT /evidence="ECO:0007829|PDB:7ADR"
FT HELIX 320..323
FT /evidence="ECO:0007829|PDB:7ADR"
FT TURN 324..326
FT /evidence="ECO:0007829|PDB:7ADR"
FT STRAND 328..334
FT /evidence="ECO:0007829|PDB:7ADR"
FT HELIX 335..347
FT /evidence="ECO:0007829|PDB:7ADR"
FT STRAND 351..356
FT /evidence="ECO:0007829|PDB:7ADR"
FT HELIX 362..365
FT /evidence="ECO:0007829|PDB:7ADR"
FT HELIX 369..377
FT /evidence="ECO:0007829|PDB:7ADR"
FT STRAND 382..387
FT /evidence="ECO:0007829|PDB:7ADR"
FT HELIX 391..398
FT /evidence="ECO:0007829|PDB:7ADR"
FT STRAND 404..408
FT /evidence="ECO:0007829|PDB:7ADR"
FT HELIX 410..412
FT /evidence="ECO:0007829|PDB:7ADR"
FT HELIX 413..419
FT /evidence="ECO:0007829|PDB:7ADR"
FT STRAND 423..425
FT /evidence="ECO:0007829|PDB:7ADR"
FT STRAND 433..435
FT /evidence="ECO:0007829|PDB:7ADR"
FT HELIX 436..438
FT /evidence="ECO:0007829|PDB:7ADR"
FT HELIX 443..465
FT /evidence="ECO:0007829|PDB:7ADR"
FT HELIX 469..471
FT /evidence="ECO:0007829|PDB:7ADR"
SQ SEQUENCE 475 AA; 52776 MW; 540D5EA83B75A88C CRC64;
MSNCELTVLK PAEVKLSPRD REGIINPMYD CQPAGAQYAG IGIKDCIPLV HGGQGCTMFV
RLLFAQHFKE NFDVASTSLH EESAVFGGAK RVEEGVLVLA RRYPNLRVIP IITTCSTEVI
GDDIEGSIRV CNRALEAEFP DRKIYLAPVH TPSFKGSHVT GYAECVKSVF KTITDAHGKG
QPSGKLNVFP GWVNPGDVVL LKRYFKEMDV EANIYMDTED FDSPMLPNKS IETHGRTTVE
DIADSANALA TLSLARYEGN TTGELLQKTF AVPNALVNTP YGIKNTDDML RKIAEVTGKE
IPESLVRERG IALDALADLA HMFFANKKVA IFGHPDLVLG LAQFCMEVEL EPVLLLIGDD
QGNKYKKDPR IEELKNTAHF DIEIVHNADL WELEKRINAG LQLDLIMGHS KGRYVAIEAN
IPMVRVGFPT FDRAGLYRKP SIGYQGAMEL GEMIANAMFA HMEYTRNKEW ILNTW
