ID   CP144_MYCTU             Reviewed;         434 AA.
AC   P9WPL1; L0TAD0; O33180;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 44.
DE   RecName: Full=Cytochrome P450 144;
DE            EC=1.14.-.-;
GN   Name=cyp144; OrderedLocusNames=Rv1777; ORFNames=MTCY25C11.04;
OS   Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium tuberculosis complex.
OX   NCBI_TaxID=83332;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 25618 / H37Rv;
RX   PubMed=9634230; DOI=10.1038/31159;
RA   Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA   Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA   Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA   Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA   Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA   Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA   Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA   Barrell B.G.;
RT   "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT   genome sequence.";
RL   Nature 393:537-544(1998).
RN   [2]
RP   DISRUPTION PHENOTYPE, ACTIVITY REGULATION, AND SUBUNIT.
RX   PubMed=20621636; DOI=10.1016/j.bbapap.2010.05.015;
RA   Driscoll M.D., McLean K.J., Cheesman M.R., Jowitt T.A., Howard M.,
RA   Carroll P., Parish T., Munro A.W.;
RT   "Expression and characterization of Mycobacterium tuberculosis CYP144:
RT   common themes and lessons learned in the M. tuberculosis P450 enzyme
RT   family.";
RL   Biochim. Biophys. Acta 1814:76-87(2011).
CC   -!- COFACTOR:
CC       Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC   -!- ACTIVITY REGULATION: Inhibited by azole drugs.
CC       {ECO:0000269|PubMed:20621636}.
CC   -!- SUBUNIT: Monomer. {ECO:0000269|PubMed:20621636}.
CC   -!- DISRUPTION PHENOTYPE: Cells are more sensitive to azole inhibition.
CC       {ECO:0000269|PubMed:20621636}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AL123456; CCP44544.1; -; Genomic_DNA.
DR   PIR; B70511; B70511.
DR   RefSeq; NP_216293.1; NC_000962.3.
DR   RefSeq; WP_003408772.1; NC_000962.3.
DR   PDB; 5HDI; X-ray; 1.54 A; A/B=31-434.
DR   PDBsum; 5HDI; -.
DR   AlphaFoldDB; P9WPL1; -.
DR   SMR; P9WPL1; -.
DR   STRING; 83332.Rv1777; -.
DR   PaxDb; P9WPL1; -.
DR   DNASU; 885839; -.
DR   GeneID; 885839; -.
DR   KEGG; mtu:Rv1777; -.
DR   PATRIC; fig|83332.111.peg.1981; -.
DR   TubercuList; Rv1777; -.
DR   eggNOG; COG2124; Bacteria.
DR   OMA; PFRGHHR; -.
DR   PhylomeDB; P9WPL1; -.
DR   Proteomes; UP000001584; Chromosome.
DR   GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
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; IPR002397; Cyt_P450_B.
DR   InterPro; IPR017972; Cyt_P450_CS.
DR   InterPro; IPR036396; Cyt_P450_sf.
DR   Pfam; PF00067; p450; 1.
DR   PRINTS; PR00359; BP450.
DR   PRINTS; PR00385; P450.
DR   SUPFAM; SSF48264; SSF48264; 1.
DR   PROSITE; PS00086; CYTOCHROME_P450; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase;
KW   Reference proteome.
FT   CHAIN           1..434
FT                   /note="Cytochrome P450 144"
FT                   /id="PRO_0000052307"
FT   BINDING         124
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         128
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         132
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000250"
FT   BINDING         326
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000250"
FT   BINDING         383
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000250"
FT   BINDING         385
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"
FT   HELIX           43..47
FT                   /evidence="ECO:0007829|PDB:5HDI"
FT   HELIX           50..59
FT                   /evidence="ECO:0007829|PDB:5HDI"
FT   STRAND          61..64
FT                   /evidence="ECO:0007829|PDB:5HDI"
FT   STRAND          68..73
FT                   /evidence="ECO:0007829|PDB:5HDI"
FT   HELIX           76..83
FT                   /evidence="ECO:0007829|PDB:5HDI"
FT   TURN            86..88
FT                   /evidence="ECO:0007829|PDB:5HDI"
FT   STRAND          95..99
FT                   /evidence="ECO:0007829|PDB:5HDI"
FT   STRAND          105..109
FT                   /evidence="ECO:0007829|PDB:5HDI"
FT   HELIX           120..122
FT                   /evidence="ECO:0007829|PDB:5HDI"
FT   HELIX           127..136
FT                   /evidence="ECO:0007829|PDB:5HDI"
FT   HELIX           141..162
FT                   /evidence="ECO:0007829|PDB:5HDI"
FT   STRAND          167..169
FT                   /evidence="ECO:0007829|PDB:5HDI"
FT   HELIX           170..173
FT                   /evidence="ECO:0007829|PDB:5HDI"
FT   TURN            174..177
FT                   /evidence="ECO:0007829|PDB:5HDI"
FT   HELIX           178..187
FT                   /evidence="ECO:0007829|PDB:5HDI"
FT   HELIX           194..201
FT                   /evidence="ECO:0007829|PDB:5HDI"
FT   HELIX           203..209
FT                   /evidence="ECO:0007829|PDB:5HDI"
FT   HELIX           214..240
FT                   /evidence="ECO:0007829|PDB:5HDI"
FT   HELIX           246..255
FT                   /evidence="ECO:0007829|PDB:5HDI"
FT   HELIX           261..275
FT                   /evidence="ECO:0007829|PDB:5HDI"
FT   HELIX           277..292
FT                   /evidence="ECO:0007829|PDB:5HDI"
FT   HELIX           294..302
FT                   /evidence="ECO:0007829|PDB:5HDI"
FT   HELIX           304..306
FT                   /evidence="ECO:0007829|PDB:5HDI"
FT   HELIX           307..317
FT                   /evidence="ECO:0007829|PDB:5HDI"
FT   STRAND          320..322
FT                   /evidence="ECO:0007829|PDB:5HDI"
FT   STRAND          324..328
FT                   /evidence="ECO:0007829|PDB:5HDI"
FT   STRAND          330..334
FT                   /evidence="ECO:0007829|PDB:5HDI"
FT   STRAND          337..339
FT                   /evidence="ECO:0007829|PDB:5HDI"
FT   STRAND          344..347
FT                   /evidence="ECO:0007829|PDB:5HDI"
FT   HELIX           349..352
FT                   /evidence="ECO:0007829|PDB:5HDI"
FT   TURN            356..358
FT                   /evidence="ECO:0007829|PDB:5HDI"
FT   HELIX           381..383
FT                   /evidence="ECO:0007829|PDB:5HDI"
FT   HELIX           388..404
FT                   /evidence="ECO:0007829|PDB:5HDI"
FT   STRAND          407..414
FT                   /evidence="ECO:0007829|PDB:5HDI"
FT   STRAND          421..423
FT                   /evidence="ECO:0007829|PDB:5HDI"
FT   STRAND          429..434
FT                   /evidence="ECO:0007829|PDB:5HDI"
SQ   SEQUENCE   434 AA;  47219 MW;  030ECFE134BC050C CRC64;
     MRRSPKGSPG AVLDLQRRVD QAVSADHAEL MTIAKDANTF FGAESVQDPY PLYERMRAAG
     SVHRIANSDF YAVCGWDAVN EAIGRPEDFS SNLTATMTYT AEGTAKPFEM DPLGGPTHVL
     ATADDPAHAV HRKLVLRHLA AKRIRVMEQF TVQAADRLWV DGMQDGCIEW MGAMANRLPM
     MVVAELIGLP DPDIAQLVKW GYAATQLLEG LVENDQLVAA GVALMELSGY IFEQFDRAAA
     DPRDNLLGEL ATACASGELD TLTAQVMMVT LFAAGGESTA ALLGSAVWIL ATRPDIQQQV
     RANPELLGAF IEETLRYEPP FRGHYRHVRN ATTLDGTELP ADSHLLLLWG AANRDPAQFE
     APGEFRLDRA GGKGHISFGK GAHFCVGAAL ARLEARIVLR LLLDRTSVIE AADVGGWLPS
     ILVRRIERLE LAVQ