ID   Y2525_MYCTO             Reviewed;         419 AA.
AC   Q7D745;
DT   10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT   10-AUG-2010, sequence version 2.
DT   25-MAY-2022, entry version 88.
DE   RecName: Full=Putative trans-acting enoyl reductase MT2525;
DE            EC=1.3.1.-;
GN   OrderedLocusNames=MT2525;
OS   Mycobacterium tuberculosis (strain CDC 1551 / Oshkosh).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=CDC 1551 / Oshkosh;
RX   PubMed=12218036; DOI=10.1128/jb.184.19.5479-5490.2002;
RA   Fleischmann R.D., Alland D., Eisen J.A., Carpenter L., White O.,
RA   Peterson J.D., DeBoy R.T., Dodson R.J., Gwinn M.L., Haft D.H., Hickey E.K.,
RA   Kolonay J.F., Nelson W.C., Umayam L.A., Ermolaeva M.D., Salzberg S.L.,
RA   Delcher A., Utterback T.R., Weidman J.F., Khouri H.M., Gill J., Mikula A.,
RA   Bishai W., Jacobs W.R. Jr., Venter J.C., Fraser C.M.;
RT   "Whole-genome comparison of Mycobacterium tuberculosis clinical and
RT   laboratory strains.";
RL   J. Bacteriol. 184:5479-5490(2002).
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC       protein {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the saccharopine dehydrogenase family. Enoyl
CC       reductase subfamily. {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAK46824.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AE000516; AAK46824.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_003412609.1; NZ_KK341227.1.
DR   AlphaFoldDB; Q7D745; -.
DR   EnsemblBacteria; AAK46824; AAK46824; MT2525.
DR   KEGG; mtc:MT2525; -.
DR   PATRIC; fig|83331.31.peg.2724; -.
DR   HOGENOM; CLU_031002_0_2_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR   InterPro; IPR036291; NAD(P)-bd_dom_sf.
DR   InterPro; IPR005097; Sacchrp_dh_NADP.
DR   Pfam; PF03435; Sacchrp_dh_NADP; 1.
DR   SUPFAM; SSF51735; SSF51735; 1.
PE   3: Inferred from homology;
KW   Cell membrane; Isopeptide bond; Membrane; Oxidoreductase; Transmembrane;
KW   Transmembrane helix; Ubl conjugation.
FT   CHAIN           1..419
FT                   /note="Putative trans-acting enoyl reductase MT2525"
FT                   /id="PRO_0000396095"
FT   TRANSMEM        284..304
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   REGION          197..232
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        127
FT                   /note="Isoglutamyl lysine isopeptide (Lys-Gln) (interchain
FT                   with Q-Cter in protein Pup)"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   419 AA;  44379 MW;  83DA2104BC7DC630 CRC64;
     MTATPREFDI VLYGATGFVG KLTAEYLARA GGDARIALAG RSTQRVLAVR EALGESAQTW
     PILTADASLP STLQAMAARA QVVVTTVGPY TRYGLPLVAA CAAAGTDYAD LTGEPMFMRN
     SIDLYHKQAA DTGARIVHAC GFDSVPSDLS VYALYHAARE DGAGELTDTN CVVRSFKGGF
     SGGTIASMLE VLSTASNDPD ARRQLSDPYM LSPDRGAEPE LGPQPDLPSR RGRRLAPELA
     GVWTAGFIMA PTNTRIVRRS NALLDWAYGR RFRYSETMSV GSTVLAPVVS VVGGGVGNAM
     FGLASRYIRL LPRGLVKRVV PKPGTGPSAA ARERGYYRIE TYTTTTTGAR YLARMAQDGD
     PGYKATSVLL GECGLALALD RDKLSDMRGV LTPAAAMGDA LLERLPAAGV SLQTTRLAS