ID CP130_MYCTU Reviewed; 405 AA.
AC P9WPN5; L0T6B9; Q11062;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=Cytochrome P450 130;
DE EC=1.14.-.-;
GN Name=cyp130; OrderedLocusNames=Rv1256c; ORFNames=MTCY50.26;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011445;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
RN [3]
RP X-RAY CRYSTALLOGRAPHY (1.46 ANGSTROMS) IN COMPLEX WITH HEME AND SUBSTRATE
RP ANALOGS, ACTIVITY REGULATION, AND SUBUNIT.
RX PubMed=18089574; DOI=10.1074/jbc.m708734200;
RA Ouellet H., Podust L.M., de Montellano P.R.;
RT "Mycobacterium tuberculosis CYP130: crystal structure, biophysical
RT characterization, and interactions with antifungal azole drugs.";
RL J. Biol. Chem. 283:5069-5080(2008).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF 2-405 IN COMPLEX WITH HEME AND
RP SUBSTRATE ANALOGS AND OF MUTANT ALA-243, MUTAGENESIS OF GLY-243, ACTIVITY
RP REGULATION, AND SUBUNIT.
RX PubMed=19605350; DOI=10.1074/jbc.m109.017632;
RA Podust L.M., Ouellet H., von Kries J.P., de Montellano P.R.;
RT "Interaction of Mycobacterium tuberculosis CYP130 with heterocyclic
RT arylamines.";
RL J. Biol. Chem. 284:25211-25219(2009).
CC -!- COFACTOR:
CC Name=heme; Xref=ChEBI:CHEBI:30413;
CC -!- ACTIVITY REGULATION: Inhibited by azole drugs.
CC {ECO:0000269|PubMed:18089574, ECO:0000269|PubMed:19605350}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18089574,
CC ECO:0000269|PubMed:19605350}.
CC -!- SIMILARITY: Belongs to the cytochrome P450 family. {ECO:0000305}.
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DR EMBL; AL123456; CCP44012.1; -; Genomic_DNA.
DR PIR; H70752; H70752.
DR RefSeq; NP_215772.1; NC_000962.3.
DR RefSeq; WP_003406352.1; NZ_NVQJ01000049.1.
DR PDB; 2UUQ; X-ray; 1.46 A; A=1-405.
DR PDB; 2UVN; X-ray; 3.00 A; A/B=1-405.
DR PDB; 2WGY; X-ray; 1.50 A; A=2-405.
DR PDB; 2WH8; X-ray; 1.70 A; A/B/C/D=2-405.
DR PDB; 2WHF; X-ray; 1.58 A; A=2-405.
DR PDBsum; 2UUQ; -.
DR PDBsum; 2UVN; -.
DR PDBsum; 2WGY; -.
DR PDBsum; 2WH8; -.
DR PDBsum; 2WHF; -.
DR AlphaFoldDB; P9WPN5; -.
DR SMR; P9WPN5; -.
DR STRING; 83332.Rv1256c; -.
DR BindingDB; P9WPN5; -.
DR ChEMBL; CHEMBL5357; -.
DR DrugBank; DB07705; (S)-econazole.
DR DrugBank; DB07972; 1-(3-METHYLPHENYL)-1H-BENZIMIDAZOL-5-AMINE.
DR DrugBank; DB07971; 5-AMINO-2-{4-[(4-AMINOPHENYL)SULFANYL]PHENYL}-1H-ISOINDOLE-1,3(2H)-DIONE.
DR DrugCentral; P9WPN5; -.
DR PaxDb; 83332-Rv1256c; -.
DR DNASU; 887059; -.
DR GeneID; 45425226; -.
DR GeneID; 887059; -.
DR KEGG; mtu:Rv1256c; -.
DR TubercuList; Rv1256c; -.
DR eggNOG; COG2124; Bacteria.
DR InParanoid; P9WPN5; -.
DR OrthoDB; 3213397at2; -.
DR PhylomeDB; P9WPN5; -.
DR PRO; PR:P9WPN5; -.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0020037; F:heme binding; IDA:MTBBASE.
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 CDD; cd11078; CYP130-like; 1.
DR Gene3D; 1.10.630.10; Cytochrome P450; 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 PANTHER; PTHR46696:SF2; CYTOCHROME P450 130; 1.
DR PANTHER; PTHR46696; P450, PUTATIVE (EUROFUNG)-RELATED; 1.
DR Pfam; PF00067; p450; 1.
DR PRINTS; PR00359; BP450.
DR SUPFAM; SSF48264; Cytochrome P450; 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..405
FT /note="Cytochrome P450 130"
FT /id="PRO_0000052285"
FT BINDING 93
FT /ligand="substrate"
FT BINDING 97
FT /ligand="substrate"
FT BINDING 101
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000269|PubMed:18089574,
FT ECO:0000269|PubMed:19605350"
FT BINDING 243
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000269|PubMed:18089574,
FT ECO:0000269|PubMed:19605350"
FT BINDING 295
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000269|PubMed:18089574,
FT ECO:0000269|PubMed:19605350"
FT BINDING 318
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000269|PubMed:18089574,
FT ECO:0000269|PubMed:19605350"
FT BINDING 348
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000269|PubMed:18089574,
FT ECO:0000269|PubMed:19605350"
FT BINDING 352
FT /ligand="heme"
FT /ligand_id="ChEBI:CHEBI:30413"
FT /evidence="ECO:0000269|PubMed:18089574,
FT ECO:0000269|PubMed:19605350"
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 MUTAGEN 243
FT /note="G->A: The binding mode of azoles and some arylamines
FT are reverted from type II to type I because of hydrophobic
FT and steric interactions with the alanine side chain."
FT /evidence="ECO:0000269|PubMed:19605350"
FT TURN 14..18
FT /evidence="ECO:0007829|PDB:2UUQ"
FT HELIX 21..30
FT /evidence="ECO:0007829|PDB:2UUQ"
FT STRAND 32..36
FT /evidence="ECO:0007829|PDB:2UUQ"
FT HELIX 42..44
FT /evidence="ECO:0007829|PDB:2UUQ"
FT STRAND 46..49
FT /evidence="ECO:0007829|PDB:2UUQ"
FT HELIX 52..60
FT /evidence="ECO:0007829|PDB:2UUQ"
FT TURN 62..64
FT /evidence="ECO:0007829|PDB:2UUQ"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:2UUQ"
FT STRAND 71..73
FT /evidence="ECO:0007829|PDB:2UUQ"
FT HELIX 77..81
FT /evidence="ECO:0007829|PDB:2UUQ"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:2UUQ"
FT HELIX 89..91
FT /evidence="ECO:0007829|PDB:2UUQ"
FT HELIX 96..105
FT /evidence="ECO:0007829|PDB:2UUQ"
FT HELIX 110..133
FT /evidence="ECO:0007829|PDB:2UUQ"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:2UUQ"
FT HELIX 139..142
FT /evidence="ECO:0007829|PDB:2UUQ"
FT TURN 143..145
FT /evidence="ECO:0007829|PDB:2UUQ"
FT HELIX 146..155
FT /evidence="ECO:0007829|PDB:2UUQ"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:2UUQ"
FT HELIX 163..178
FT /evidence="ECO:0007829|PDB:2UUQ"
FT HELIX 187..204
FT /evidence="ECO:0007829|PDB:2UUQ"
FT HELIX 212..218
FT /evidence="ECO:0007829|PDB:2UUQ"
FT TURN 219..222
FT /evidence="ECO:0007829|PDB:2UUQ"
FT HELIX 227..244
FT /evidence="ECO:0007829|PDB:2UUQ"
FT HELIX 246..260
FT /evidence="ECO:0007829|PDB:2UUQ"
FT HELIX 263..271
FT /evidence="ECO:0007829|PDB:2UUQ"
FT HELIX 273..275
FT /evidence="ECO:0007829|PDB:2UUQ"
FT HELIX 276..287
FT /evidence="ECO:0007829|PDB:2UUQ"
FT STRAND 293..299
FT /evidence="ECO:0007829|PDB:2UUQ"
FT STRAND 301..303
FT /evidence="ECO:0007829|PDB:2UUQ"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:2UUQ"
FT STRAND 313..316
FT /evidence="ECO:0007829|PDB:2UUQ"
FT HELIX 318..321
FT /evidence="ECO:0007829|PDB:2UUQ"
FT HELIX 325..328
FT /evidence="ECO:0007829|PDB:2UUQ"
FT TURN 330..333
FT /evidence="ECO:0007829|PDB:2UUQ"
FT HELIX 357..374
FT /evidence="ECO:0007829|PDB:2UUQ"
FT STRAND 377..380
FT /evidence="ECO:0007829|PDB:2UUQ"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:2UUQ"
FT STRAND 391..393
FT /evidence="ECO:0007829|PDB:2UUQ"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:2UUQ"
FT STRAND 400..403
FT /evidence="ECO:0007829|PDB:2UUQ"
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
//
