ID   CP138_MYCTO             Reviewed;         441 AA.
AC   P9WPM2; L0T5T2; P63717; P96813;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 47.
DE   RecName: Full=Putative cytochrome P450 138;
DE            EC=1.14.-.-;
GN   Name=cyp138; OrderedLocusNames=MT0144;
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   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK44368.1; -; Genomic_DNA.
DR   PIR; C70616; C70616.
DR   RefSeq; WP_003400938.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WPM2; -.
DR   SMR; P9WPM2; -.
DR   EnsemblBacteria; AAK44368; AAK44368; MT0144.
DR   GeneID; 45424102; -.
DR   KEGG; mtc:MT0144; -.
DR   PATRIC; fig|83331.31.peg.156; -.
DR   HOGENOM; CLU_001570_5_1_11; -.
DR   Proteomes; UP000001020; Chromosome.
DR   GO; GO:0020037; F:heme binding; IEA:InterPro.
DR   GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR   GO; GO:0004497; F:monooxygenase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:InterPro.
DR   Gene3D; 1.10.630.10; -; 1.
DR   InterPro; IPR001128; Cyt_P450.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR002401; Cyt_P450_E_grp-I.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00463; EP450I.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   3: Inferred from homology;
KW   Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase.
FT   CHAIN           1..441
FT                   /note="Putative cytochrome P450 138"
FT                   /id="PRO_0000426927"
FT   BINDING         388
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /ligand_part="Fe"
FT                   /ligand_part_id="ChEBI:CHEBI:18248"
FT                   /note="axial binding residue"
FT                   /evidence="ECO:0000250"
SQ   SEQUENCE   441 AA;  49261 MW;  0E433656428A64EB CRC64;
     MSEVVTAAPA PPVVRLPPAV RGPKLFQGLA FVVSRRRLLG RFVRRYGKAF TANILMYGRV
     VVVADPQLAR QVFTSSPEEL GNIQPNLSRM FGSGSVFALD GDDHRRRRRL LAPPFHGKSM
     KNYETIIEEE TLRETANWPQ GQAFATLPSM MHITLNAILR AIFGAGGSEL DELRRLIPPW
     VTLGSRLAAL PKPKRDYGRL SPWGRLAEWR RQYDTVIDKL IEAERADPNF ADRTDVLALM
     LRSTYDDGSI MSRKDIGDEL LTLLAAGHET TAATLGWAFE RLSRHPDVLA ALVEEVDNGG
     HELRQAAILE VQRARTVIDF AARRVNPPVY QLGEWVIPRG YSIIINIAQI HGDPDVFPQP
     DRFDPQRYIG SKPSPFAWIP FGGGTRRCVG AAFANMEMDV VLRTVLRHFT LETTTAAGER
     SHGRGVAFTP KDGGRVVMRR R