ID VNFK_AZOCH Reviewed; 475 AA.
AC P15334;
DT 01-APR-1990, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 2.
DT 13-SEP-2023, entry version 92.
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 chroococcum mcd 1.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=355;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2388847; DOI=10.1093/nar/18.15.4616;
RA Fallik E., Robson R.L.;
RT "Completed sequence of the region encoding the structural genes for the
RT vanadium nitrogenase of Azotobacter chroococcum.";
RL Nucleic Acids Res. 18:4616-4616(1990).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 2-11.
RX PubMed=2743980; DOI=10.1002/j.1460-2075.1989.tb03495.x;
RA Robson R.L., Woodley P.R., Pau R.N., Eady R.R.;
RT "Structural genes for the vanadium nitrogenase from Azotobacter
RT chroococcum.";
RL EMBO J. 8:1217-1224(1989).
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; X51756; CAA36060.1; -; Genomic_DNA.
DR EMBL; X15077; CAA33175.1; -; Genomic_DNA.
DR PIR; S04115; S04115.
DR AlphaFoldDB; P15334; -.
DR SMR; P15334; -.
DR BRENDA; 1.18.6.2; 617.
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 Gene3D; 3.40.50.1980; Nitrogenase molybdenum iron protein domain; 3.
DR InterPro; IPR000510; Nase/OxRdtase_comp1.
DR InterPro; IPR000318; Nase_comp1_CS.
DR InterPro; IPR014281; Nase_VnfK.
DR NCBIfam; TIGR02932; vnfK_nitrog; 1.
DR PANTHER; PTHR33712; LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT B; 1.
DR PANTHER; PTHR33712:SF7; LIGHT-INDEPENDENT PROTOCHLOROPHYLLIDE REDUCTASE SUBUNIT B; 1.
DR Pfam; PF00148; Oxidored_nitro; 1.
DR SUPFAM; SSF53807; Helical backbone' metal receptor; 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:2743980"
FT CHAIN 2..475
FT /note="Nitrogenase vanadium-iron protein beta chain"
FT /id="PRO_0000153088"
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"
SQ SEQUENCE 475 AA; 52855 MW; 4F73D43FC656DB42 CRC64;
MSNCELTVLK PAEVKLVKRE REGIINPMYD CQPAGAQYAG IGVKDCIPLV HGGQGCTMFV
RLLFAQHFKE NFDVASTSLH EESAVFGGAK RVEEGVLVLA RRYPELRLIP IITTCSTEVI
GDDIEGTINV CNRALAAEFP ERKIYLAPVH TPSFKGSHVT GYAECVKSMF KTITEVHGKG
QPSGKLNVFP GWVNPGDVVL LKRYFKEMGV DATVFMDTED FDSPMLPNKS IETHGRTTVE
DIADSANALA TLALARYEGA TTGEYLEKTF AVPNSLVNTP YGIKNTDDML RKIAEITGKE
IPESLVREPR IAWIALADLA HMFFANKKVA IFGHPDLVLG LAQFCLEVEL EPVLLLIGDD
QGSKYKKDPR LQELKDAAHF DMEIVHNADL WELEKRINDG LQLDLIMGHS KGRYVAIEAN
IPMVRVGFPT FDRAGLYRKP SIGYQGAMEL GEMIANAMFA HMEYTRNKEW ILNTW
//
