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