ID   NIFM_AZOCH              Reviewed;         293 AA.
AC   P23119;
DT   01-NOV-1991, integrated into UniProtKB/Swiss-Prot.
DT   01-NOV-1991, sequence version 1.
DT   25-MAY-2022, entry version 60.
DE   RecName: Full=Putative peptidyl-prolyl cis-trans isomerase NifM;
DE            Short=PPIase NifM;
DE            EC=5.2.1.8;
DE   AltName: Full=Rotamase NifM;
GN   Name=nifM;
OS   Azotobacter chroococcum mcd 1.
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Azotobacter.
OX   NCBI_TaxID=355;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX   PubMed=1885524; DOI=10.1128/jb.173.17.5457-5469.1991;
RA   Evans D.J., Jones R., Woodley P.R., Wilborn J.R., Robson R.L.;
RT   "Nucleotide sequence and genetic analysis of the Azotobacter chroococcum
RT   nifUSVWZM gene cluster, including a new gene (nifP) which encodes a serine
RT   acetyltransferase.";
RL   J. Bacteriol. 173:5457-5469(1991).
CC   -!- FUNCTION: Required for the activation and stabilization of the iron-
CC       component (NifH) of nitrogenase. Probable PPIase.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=[protein]-peptidylproline (omega=180) = [protein]-
CC         peptidylproline (omega=0); Xref=Rhea:RHEA:16237, Rhea:RHEA-
CC         COMP:10747, Rhea:RHEA-COMP:10748, ChEBI:CHEBI:83833,
CC         ChEBI:CHEBI:83834; EC=5.2.1.8;
CC   -!- SIMILARITY: Belongs to the PpiC/parvulin rotamase family.
CC       {ECO:0000305}.
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DR   EMBL; M60090; AAA22166.1; -; Genomic_DNA.
DR   PIR; H43706; H43706.
DR   AlphaFoldDB; P23119; -.
DR   SMR; P23119; -.
DR   GO; GO:0003755; F:peptidyl-prolyl cis-trans isomerase activity; IEA:UniProtKB-KW.
DR   GO; GO:0009399; P:nitrogen fixation; IEA:UniProtKB-KW.
DR   Gene3D; 3.10.50.40; -; 1.
DR   InterPro; IPR014282; Nitrogen_fix_NifM.
DR   InterPro; IPR046357; PPIase_dom_sf.
DR   InterPro; IPR000297; PPIase_PpiC.
DR   InterPro; IPR023058; PPIase_PpiC_CS.
DR   InterPro; IPR027304; Trigger_fact/SurA_dom_sf.
DR   Pfam; PF00639; Rotamase; 1.
DR   SUPFAM; SSF109998; SSF109998; 1.
DR   TIGRFAMs; TIGR02933; nifM_nitrog; 1.
DR   PROSITE; PS01096; PPIC_PPIASE_1; 1.
DR   PROSITE; PS50198; PPIC_PPIASE_2; 1.
PE   3: Inferred from homology;
KW   Isomerase; Nitrogen fixation; Rotamase.
FT   CHAIN           1..293
FT                   /note="Putative peptidyl-prolyl cis-trans isomerase NifM"
FT                   /id="PRO_0000193427"
FT   DOMAIN          142..244
FT                   /note="PpiC"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00278"
SQ   SEQUENCE   293 AA;  32979 MW;  7D987E2564DE5CDA CRC64;
     MSFEHPGDGD SRYYLLKIAH EQFGCAPGEL SEEQLQQAER IIGRQKHIED AVLRCPDAAG
     VVIPASQIEE AWTQIANRYE SAEALQQALD AQGLERVGMR AMLARELKVQ AVLDCICAGL
     PEISDTDVSL YYFNHAEQFK VPARHKARHI LVTINEDFPE NTREAARTRI EAILKRLRGK
     PERFAEQAAK HSECPTAMQG GLLGEVVPGT LYPELDACLF QMAQGQLSPV LESPIGFHVL
     FCESVSTARQ LTLEEILPRL RDRLQLRQRK AYQRKWLESL LQQNATLENL AHG