CP121_MYCTO
ID CP121_MYCTO Reviewed; 396 AA.
AC P9WPP6; L0TAQ4; P0A514; Q59571;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 37.
DE RecName: Full=Mycocyclosin synthase;
DE EC=1.14.19.70 {ECO:0000250|UniProtKB:P9WPP7};
DE AltName: Full=Cytochrome P450 121;
DE AltName: Full=Cytochrome P450 MT2;
GN Name=cyp121; OrderedLocusNames=MT2336;
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 -!- FUNCTION: Catalyzes C-C bond formation between the carbons ortho to the
CC phenolic hydroxyl of cyclo(L-tyr-L-tyr) (cYY) producing mycocyclosin.
CC Can also use cyclo(L-Tyr-L-Phe) (cYF), cyclo(L-Tyr-L-Trp) (cYW) and
CC cyclo(L-Tyr-L-3,4-dihydroxyphenylalanine) (cY-DOPA) as substrate.
CC {ECO:0000250|UniProtKB:P9WPP7}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=cyclo(L-tyrosyl-L-tyrosyl) + 2 H(+) + O2 + 2 reduced [2Fe-2S]-
CC [ferredoxin] = 2 H2O + mycoclysin + 2 oxidized [2Fe-2S]-[ferredoxin];
CC Xref=Rhea:RHEA:35547, Rhea:RHEA-COMP:10000, Rhea:RHEA-COMP:10001,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:15379,
CC ChEBI:CHEBI:33737, ChEBI:CHEBI:33738, ChEBI:CHEBI:65063,
CC ChEBI:CHEBI:71596; EC=1.14.19.70;
CC Evidence={ECO:0000250|UniProtKB:P9WPP7};
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; AE000516; AAK46620.1; -; Genomic_DNA.
DR PIR; H70730; H70730.
DR RefSeq; WP_003411685.1; NZ_KK341227.1.
DR AlphaFoldDB; P9WPP6; -.
DR SMR; P9WPP6; -.
DR EnsemblBacteria; AAK46620; AAK46620; MT2336.
DR KEGG; mtc:MT2336; -.
DR PATRIC; fig|83331.31.peg.2513; -.
DR HOGENOM; CLU_033716_1_1_11; -.
DR Proteomes; UP000001020; 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 3: Inferred from homology;
KW Cytoplasm; Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000250"
FT CHAIN 2..396
FT /note="Mycocyclosin synthase"
FT /id="PRO_0000426915"
FT BINDING 77
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 85..86
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 237
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 286
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250"
FT BINDING 301
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 343
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000250"
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 /evidence="ECO:0000250"
FT BINDING 385
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT SITE 168
FT /note="Participates in a stacking interactions with the
FT tyrosyl of cYY"
FT /evidence="ECO:0000250"
FT SITE 182
FT /note="Participates in a stacking interactions with the
FT tyrosyl of cYY"
FT /evidence="ECO:0000250"
FT SITE 346
FT /note="Important for the position of heme"
FT /evidence="ECO:0000250"
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
