CP121_MYCBO
ID CP121_MYCBO Reviewed; 396 AA.
AC P0A515; A0A1R3Y0Q8; Q59571; X2BJT7;
DT 15-MAR-2005, integrated into UniProtKB/Swiss-Prot.
DT 15-MAR-2005, sequence version 1.
DT 03-AUG-2022, entry version 94.
DE RecName: Full=Cytochrome P450 121;
DE EC=1.14.-.-;
DE AltName: Full=Cytochrome P450 MT2;
GN Name=cyp121; OrderedLocusNames=BQ2027_MB2299;
OS Mycobacterium bovis (strain ATCC BAA-935 / AF2122/97).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=233413;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=12788972; DOI=10.1073/pnas.1130426100;
RA Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M.,
RA Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B.,
RA Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J.,
RA Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.;
RT "The complete genome sequence of Mycobacterium bovis.";
RL Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND GENOME REANNOTATION.
RC STRAIN=ATCC BAA-935 / AF2122/97;
RX PubMed=28385856; DOI=10.1128/genomea.00157-17;
RA Malone K.M., Farrell D., Stuber T.P., Schubert O.T., Aebersold R.,
RA Robbe-Austerman S., Gordon S.V.;
RT "Updated reference genome sequence and annotation of Mycobacterium bovis
RT AF2122/97.";
RL Genome Announc. 5:E00157-E00157(2017).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413; Evidence={ECO:0000250};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; LT708304; SIU00911.1; -; Genomic_DNA.
DR RefSeq; NP_855948.1; NC_002945.3.
DR RefSeq; WP_003411685.1; NC_002945.4.
DR PDB; 5EDT; X-ray; 2.45 A; A=2-396.
DR PDBsum; 5EDT; -.
DR AlphaFoldDB; P0A515; -.
DR SMR; P0A515; -.
DR EnsemblBacteria; SIU00911; SIU00911; BQ2027_MB2299.
DR PATRIC; fig|233413.5.peg.2524; -.
DR OMA; FAHKYEP; -.
DR Proteomes; UP000001419; Chromosome.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 SUPFAM; SSF48264; SSF48264; 1.
DR PROSITE; PS00086; CYTOCHROME_P450; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Cytoplasm; Heme; Iron; Metal-binding; Monooxygenase;
KW Oxidoreductase.
FT CHAIN 1..396
FT /note="Cytochrome P450 121"
FT /id="PRO_0000052273"
FT BINDING 345
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 HELIX 21..28
FT /evidence="ECO:0007829|PDB:5EDT"
FT STRAND 30..35
FT /evidence="ECO:0007829|PDB:5EDT"
FT STRAND 41..45
FT /evidence="ECO:0007829|PDB:5EDT"
FT HELIX 48..56
FT /evidence="ECO:0007829|PDB:5EDT"
FT STRAND 60..62
FT /evidence="ECO:0007829|PDB:5EDT"
FT HELIX 63..66
FT /evidence="ECO:0007829|PDB:5EDT"
FT HELIX 80..83
FT /evidence="ECO:0007829|PDB:5EDT"
FT HELIX 85..91
FT /evidence="ECO:0007829|PDB:5EDT"
FT HELIX 95..101
FT /evidence="ECO:0007829|PDB:5EDT"
FT HELIX 109..127
FT /evidence="ECO:0007829|PDB:5EDT"
FT STRAND 129..132
FT /evidence="ECO:0007829|PDB:5EDT"
FT TURN 133..137
FT /evidence="ECO:0007829|PDB:5EDT"
FT HELIX 138..150
FT /evidence="ECO:0007829|PDB:5EDT"
FT HELIX 154..156
FT /evidence="ECO:0007829|PDB:5EDT"
FT HELIX 157..161
FT /evidence="ECO:0007829|PDB:5EDT"
FT HELIX 164..167
FT /evidence="ECO:0007829|PDB:5EDT"
FT HELIX 176..193
FT /evidence="ECO:0007829|PDB:5EDT"
FT HELIX 201..211
FT /evidence="ECO:0007829|PDB:5EDT"
FT HELIX 213..215
FT /evidence="ECO:0007829|PDB:5EDT"
FT HELIX 220..250
FT /evidence="ECO:0007829|PDB:5EDT"
FT HELIX 253..261
FT /evidence="ECO:0007829|PDB:5EDT"
FT HELIX 263..265
FT /evidence="ECO:0007829|PDB:5EDT"
FT HELIX 266..275
FT /evidence="ECO:0007829|PDB:5EDT"
FT STRAND 284..290
FT /evidence="ECO:0007829|PDB:5EDT"
FT STRAND 292..294
FT /evidence="ECO:0007829|PDB:5EDT"
FT STRAND 297..299
FT /evidence="ECO:0007829|PDB:5EDT"
FT STRAND 304..307
FT /evidence="ECO:0007829|PDB:5EDT"
FT HELIX 309..313
FT /evidence="ECO:0007829|PDB:5EDT"
FT TURN 316..318
FT /evidence="ECO:0007829|PDB:5EDT"
FT STRAND 319..321
FT /evidence="ECO:0007829|PDB:5EDT"
FT HELIX 341..343
FT /evidence="ECO:0007829|PDB:5EDT"
FT HELIX 348..365
FT /evidence="ECO:0007829|PDB:5EDT"
FT STRAND 370..373
FT /evidence="ECO:0007829|PDB:5EDT"
FT HELIX 375..377
FT /evidence="ECO:0007829|PDB:5EDT"
FT STRAND 383..386
FT /evidence="ECO:0007829|PDB:5EDT"
FT STRAND 393..395
FT /evidence="ECO:0007829|PDB:5EDT"
SQ SEQUENCE 396 AA; 43256 MW; 510C3B638419DCCB CRC64;
MTATVLLEVP FSARGDRIPD AVAELRTREP IRKVRTITGA EAWLVSSYAL CTQVLEDRRF
SMKETAAAGA PRLNALTVPP EVVNNMGNIA DAGLRKAVMK AITPKAPGLE QFLRDTANSL
LDNLITEGAP ADLRNDFADP LATALHCKVL GIPQEDGPKL FRSLSIAFMS SADPIPAAKI
NWDRDIEYMA GILENPNITT GLMGELSRLR KDPAYSHVSD ELFATIGVTF FGAGVISTGS
FLTTALISLI QRPQLRNLLH EKPELIPAGV EELLRINLSF ADGLPRLATA DIQVGDVLVR
KGELVLVLLE GANFDPEHFP NPGSIELDRP NPTSHLAFGR GQHFCPGSAL GRRHAQIGIE
ALLKKMPGVD LAVPIDQLVW RTRFQRRIPE RLPVLW
