ID   NIFX_RHOCA              Reviewed;         159 AA.
AC   P19078;
DT   01-NOV-1990, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1990, sequence version 1.
DT   25-MAY-2022, entry version 68.
DE   RecName: Full=Protein NifX;
GN   Name=nifX;
OS   Rhodobacter capsulatus (Rhodopseudomonas capsulata).
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodobacterales;
OC   Rhodobacteraceae; Rhodobacter.
OX   NCBI_TaxID=1061;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=2747620; DOI=10.1007/bf00334376;
RA   Moreno-Vivian C., Schmehl M., Masepohl B., Arnold W., Klipp W.;
RT   "DNA sequence and genetic analysis of the Rhodobacter capsulatus nifENX
RT   gene region: homology between NifX and NifB suggests involvement of NifX in
RT   processing of the iron-molybdenum cofactor.";
RL   Mol. Gen. Genet. 216:353-363(1989).
CC   -!- FUNCTION: May play a role in the processing of the iron-molybdenum
CC       cofactor.
CC   -!- SIMILARITY: Belongs to the NifX/NifY family. {ECO:0000305}.
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DR   EMBL; X17433; CAA35474.1; -; Genomic_DNA.
DR   PIR; JE0031; JE0031.
DR   AlphaFoldDB; P19078; -.
DR   SMR; P19078; -.
DR   OMA; MQIGGPA; -.
DR   GO; GO:0051540; F:metal cluster binding; IEA:InterPro.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR   CDD; cd00853; NifX; 1.
DR   Gene3D; 3.30.420.130; -; 1.
DR   InterPro; IPR003731; Di-Nase_FeMo-co_biosynth.
DR   InterPro; IPR036105; DiNase_FeMo-co_biosyn_sf.
DR   InterPro; IPR013480; NifX.
DR   InterPro; IPR034169; NifX-like.
DR   Pfam; PF02579; Nitro_FeMo-Co; 1.
DR   SUPFAM; SSF53146; SSF53146; 1.
DR   TIGRFAMs; TIGR02663; nifX; 1.
PE   3: Inferred from homology;
KW   Nitrogen fixation.
FT   CHAIN           1..159
FT                   /note="Protein NifX"
FT                   /id="PRO_0000096832"
SQ   SEQUENCE   159 AA;  17456 MW;  8470D344B6C71005 CRC64;
     MSRTLRLVEP AGPAPGEKPL RVAIASNDLE NLDAHFGSAR QIAVYEVWKT GARFVEVHQF
     SSATDQKGRH DELEDRIGPK LEALSGCTLV FALAVGGPSA ARMVRAGMHP IKRKEPEPIS
     AVIEQVQVML NGTPPPFLRK VLGTWEKPDF TADFEEEEV