NIFE_AZOVI
ID NIFE_AZOVI Reviewed; 474 AA.
AC P08293;
DT 01-AUG-1988, integrated into UniProtKB/Swiss-Prot.
DT 01-AUG-1988, sequence version 1.
DT 03-AUG-2022, entry version 88.
DE RecName: Full=Nitrogenase iron-molybdenum cofactor biosynthesis protein NifE;
GN Name=nifE;
OS Azotobacter vinelandii.
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Azotobacter.
OX NCBI_TaxID=354;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=ATCC 13705 / OP1 / DSM 366 / NCIMB 11614 / LMG 3878 / UW;
RX PubMed=2644218; DOI=10.1128/jb.171.2.1017-1027.1989;
RA Jacobson M.R., Brigle K.E., Bennett L.T., Setterquist R.A., Wilson M.S.,
RA Cash V.L., Beynon J., Newton W.E., Dean D.R.;
RT "Physical and genetic map of the major nif gene cluster from Azotobacter
RT vinelandii.";
RL J. Bacteriol. 171:1017-1027(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=16593596; DOI=10.1073/pnas.82.17.5720;
RA Dean D.R., Brigle K.E.;
RT "Azotobacter vinelandii nifD- and nifE-encoded polypeptides share
RT structural homology.";
RL Proc. Natl. Acad. Sci. U.S.A. 82:5720-5723(1985).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND SEQUENCE REVISION.
RX PubMed=3387235; DOI=10.1093/nar/16.11.5214;
RA Brigle K.E., Dean D.R.;
RT "Revised nucleotide sequence of the Azotobacter vinelandii nifE gene.";
RL Nucleic Acids Res. 16:5214-5214(1988).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 422-473.
RX PubMed=3470285; DOI=10.1128/jb.169.4.1547-1553.1987;
RA Brigle K.E., Weiss M.C., Newton W.E., Dean D.R.;
RT "Products of the iron-molybdenum cofactor-specific biosynthetic genes, nifE
RT and nifN, are structurally homologous to the products of the nitrogenase
RT molybdenum-iron protein genes, nifD and nifK.";
RL J. Bacteriol. 169:1547-1553(1987).
CC -!- FUNCTION: This protein may play a role in the biosynthesis of the
CC prosthetic group of nitrogenase (FeMo cofactor).
CC -!- PATHWAY: Cofactor biosynthesis; Fe-Mo cofactor biosynthesis.
CC -!- SIMILARITY: Belongs to the NifD/NifK/NifE/NifN family. {ECO:0000305}.
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DR EMBL; M20568; AAA64716.1; -; Genomic_DNA.
DR EMBL; X07293; CAA30271.1; -; Genomic_DNA.
DR EMBL; M11745; AAA22153.1; -; Genomic_DNA.
DR EMBL; M15815; AAA22157.1; -; Genomic_DNA.
DR PIR; S00880; S00880.
DR AlphaFoldDB; P08293; -.
DR SMR; P08293; -.
DR DIP; DIP-59675N; -.
DR IntAct; P08293; 1.
DR BioCyc; MetaCyc:MON-19486; -.
DR UniPathway; UPA00782; -.
DR GO; GO:0016163; F:nitrogenase activity; IEA:InterPro.
DR GO; GO:0032324; P:molybdopterin cofactor biosynthetic process; IMP:CACAO.
DR GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR GO; GO:0065003; P:protein-containing complex assembly; IEA:InterPro.
DR InterPro; IPR000510; Nase/OxRdtase_comp1.
DR InterPro; IPR000318; Nase_comp1_CS.
DR InterPro; IPR005973; NifE.
DR Pfam; PF00148; Oxidored_nitro; 1.
DR TIGRFAMs; TIGR01283; nifE; 1.
DR PROSITE; PS00699; NITROGENASE_1_1; 1.
DR PROSITE; PS00090; NITROGENASE_1_2; 1.
PE 3: Inferred from homology;
KW Nitrogen fixation.
FT CHAIN 1..474
FT /note="Nitrogenase iron-molybdenum cofactor biosynthesis
FT protein NifE"
FT /id="PRO_0000153112"
FT CONFLICT 133..150
FT /note="Missing (in Ref. 2; AAA22153)"
FT /evidence="ECO:0000305"
FT CONFLICT 233
FT /note="R -> G (in Ref. 2; AAA22153)"
FT /evidence="ECO:0000305"
FT CONFLICT 256..257
FT /note="NV -> KR (in Ref. 2; AAA22153)"
FT /evidence="ECO:0000305"
FT CONFLICT 465
FT /note="R -> A (in Ref. 1; AAA64716)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 474 AA; 52163 MW; 638F015BF5D11E65 CRC64;
MKAKDIAELL DEPACSHNKK EKSGCAKPKP GATDGRCSFD GAQIALLPVA DVAHIVHGPI
ACAGSSWDNR GTRSSGPDLY RIGMTTDLTE NDVIMGRAEK RLFHAIRQAV ESYLPPAVFV
YNTCVPALIG DDVDAVCKAA AERFGTPVIP VDSAGFYGTK NLGNRIAGEA MLKYVIGTRE
PDPLPVGSER PGIRVHDVNL IGEYNIAGEF WHVLPLLDEL GLRVLCTLAG DARYREVQTM
HRAEVNMMVC SKAMLNVARK LQETYGTPWF EGSFYGITDT SQALRDFARL LDDPDLTART
EALIAREEAK VRAALEPWRA RLEGKRVLLY TGGVKSWSVV SPLQDLGMKV VATGTKKSTE
EDKARIRELM GDDVKMLDEG NARVLLKTVD EYQADILIAG GRNMYTALKG RVPFLDINQE
REFGYGGYDR MLELVRHVCI TLECPVWEAV RRPAPWDIPA SQDARPSGGP FGER