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CP130_MYCTO
ID   CP130_MYCTO             Reviewed;         405 AA.
AC   P9WPN4; L0T6B9; Q11062;
DT   16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT   16-APR-2014, sequence version 1.
DT   03-AUG-2022, entry version 38.
DE   RecName: Full=Cytochrome P450 130;
DE            EC=1.14.-.-;
GN   Name=cyp130; OrderedLocusNames=MT1295;
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   -!- SUBUNIT: Homodimer. {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR   EMBL; AE000516; AAK45553.1; -; Genomic_DNA.
DR   PIR; H70752; H70752.
DR   RefSeq; WP_003406352.1; NZ_KK341227.1.
DR   AlphaFoldDB; P9WPN4; -.
DR   SMR; P9WPN4; -.
DR   BindingDB; P9WPN4; -.
DR   EnsemblBacteria; AAK45553; AAK45553; MT1295.
DR   GeneID; 45425226; -.
DR   KEGG; mtc:MT1295; -.
DR   PATRIC; fig|83331.31.peg.1398; -.
DR   HOGENOM; CLU_033716_0_2_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; 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   Heme; Iron; Metal-binding; Monooxygenase; Oxidoreductase.
FT   CHAIN           1..405
FT                   /note="Cytochrome P450 130"
FT                   /id="PRO_0000426921"
FT   BINDING         93
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         97
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000250"
FT   BINDING         101
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000250"
FT   BINDING         243
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000250"
FT   BINDING         295
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000250"
FT   BINDING         318
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000250"
FT   BINDING         348
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000250"
FT   BINDING         352
FT                   /ligand="heme"
FT                   /ligand_id="ChEBI:CHEBI:30413"
FT                   /evidence="ECO:0000250"
FT   BINDING         354
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   405 AA;  44581 MW;  72DEAE6CB688FA48 CRC64;
     MTSVMSHEFQ LATAETWPNP WPMYRALRDH DPVHHVVPPQ RPEYDYYVLS RHADVWSAAR
     DHQTFSSAQG LTVNYGELEM IGLHDTPPMV MQDPPVHTEF RKLVSRGFTP RQVETVEPTV
     RKFVVERLEK LRANGGGDIV TELFKPLPSM VVAHYLGVPE EDWTQFDGWT QAIVAANAVD
     GATTGALDAV GSMMAYFTGL IERRRTEPAD DAISHLVAAG VGADGDTAGT LSILAFTFTM
     VTGGNDTVTG MLGGSMPLLH RRPDQRRLLL DDPEGIPDAV EELLRLTSPV QGLARTTTRD
     VTIGDTTIPA GRRVLLLYGS ANRDERQYGP DAAELDVTRC PRNILTFSHG AHHCLGAAAA
     RMQCRVALTE LLARCPDFEV AESRIVWSGG SYVRRPLSVP FRVTS
 
 
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