Rv3545c - cytochrome P450 125 cyp125
Protein Domains

Gene Information
LocusRv3545c
Symbolcyp125
Gene Namecytochrome P450 125 cyp125
Location3984144 - 3985445 (-)
SpeciesMycobacterium tuberculosis H37Rv complete genome.
LengthGene:1302 bp
Protein:434 aa
External LinksTuberculist
Target Gene Information
String Protein-Protein Interactions
STITCH Chemical-Protein Interactions
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Orthologs
Orthogroup Number20615
Related GenesMAP0522 MAV_0616 Mkms_4763 Mmcs_4677 MSMEG_5995 MT3649 MUL_4106 Mvan_5258 nfa5180 SAV838
Transcriptional Regulation
Operons View gene in operon browser
Regulatory Network
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Expression Correlation Genes with Correlated Expression
Scatterplot of Gene Expression

Sequence
Proteins
Genomic Sequence
Community Annotations Pending Curatorial Review
FieldValueStatusCreatorDate
InteractionRegulatory Rv3574activepriyadarshinipriyanka20012012-10-05
Co-expression (Functional linkage)
SL. Kendall,P. Burgess,R. Balhana,M. Withers,A. Ten Bokum,JS. Lott,C. Gao,I. Uhia Castro,NG. Stoker Cholesterol utilisation in mycobacteria is controlled by two TetR-type transcriptional regulators; kstR and kstR2. Microbiology (Reading, England) 2010
InteractionRegulatory Rv3574activepriyadarshinipriyanka20012012-10-05
Co-expression (Functional linkage)
SL. Kendall, M. Withers et al. A highly conserved transcriptional repressor controls a large regulon involved in lipid degradation in Mycobacterium smegmatis and Mycobacterium tuberculosis. Mol. Microbiol. 2007
InteractionRegulatory Rv3574activejgalag2012-10-05
Co-expression (Functional linkage)
JK. Capyk, R. Kalscheuer et al. Mycobacterial cytochrome p450 125 (cyp125) catalyzes the terminal hydroxylation of c27 steroids. J. Biol. Chem. 2009
InteractionRegulatory Rv3574activejgalag2012-10-05
Co-expression (Functional linkage)
KJ. McLean, P. Lafite et al. The Structure of Mycobacterium tuberculosis CYP125: molecular basis for cholesterol binding in a P450 needed for host infection. J. Biol. Chem. 2009
InteractionRegulatedBy Rv3416activeyamir.moreno2012-10-05
One hybrid reporter system. Physical binding of the regulator to the regulated promoter proved by using electrophoretic mobility shift assay. .
M. Guo, H. Feng et al. Dissecting transcription regulatory pathways through a new bacterial one-hybrid reporter system. Genome Res. 2009
InteractionRegulatedBy Rv2034activeyamir.moreno2012-10-05
One hybrid reporter system. Physical binding of the regulator to the regulated promoter proved by using electrophoretic mobility shift assay. .
M. Guo, H. Feng et al. Dissecting transcription regulatory pathways through a new bacterial one-hybrid reporter system. Genome Res. 2009
InteractionRegulatedBy Rv2017activeyamir.moreno2012-10-05
One hybrid reporter system. Physical binding of the regulator to the regulated promoter proved by using electrophoretic mobility shift assay. .
M. Guo, H. Feng et al. Dissecting transcription regulatory pathways through a new bacterial one-hybrid reporter system. Genome Res. 2009
InteractionRegulatedBy Rv1956activeyamir.moreno2012-10-05
One hybrid reporter system. Physical binding of the regulator to the regulated promoter proved by using electrophoretic mobility shift assay. .
M. Guo, H. Feng et al. Dissecting transcription regulatory pathways through a new bacterial one-hybrid reporter system. Genome Res. 2009
InteractionRegulatedBy Rv0818activeyamir.moreno2012-10-05
One hybrid reporter system. Physical binding of the regulator to the regulated promoter proved by using electrophoretic mobility shift assay. .
M. Guo, H. Feng et al. Dissecting transcription regulatory pathways through a new bacterial one-hybrid reporter system. Genome Res. 2009
InteractionRegulatedBy Rv0445cactiveyamir.moreno2012-10-05
One hybrid reporter system. Physical binding of the regulator to the regulated promoter proved by using electrophoretic mobility shift assay. .
M. Guo, H. Feng et al. Dissecting transcription regulatory pathways through a new bacterial one-hybrid reporter system. Genome Res. 2009
InteractionRegulatedBy Rv3574activeyamir.moreno2012-10-05
Literature previously reported link (from Balazsi et al. 2008). Traceable author statement to experimental support.
G. Balázsi, AP. Heath et al. The temporal response of the Mycobacterium tuberculosis gene regulatory network during growth arrest. Mol. Syst. Biol. 2008
TermEC:1.14.13.- Oxidoreductases. Acting on paired donors, with incorporation or reduction of With NADH or NADPH as one donor, and incorporation of one atom - NRactivensampson2012-03-05
Assay of protein purified to homogeneity from a heterlogous host
JK. Capyk, R. Kalscheuer et al. Mycobacterial cytochrome p450 125 (cyp125) catalyzes the terminal hydroxylation of c27 steroids. J. Biol. Chem. 2009
TermEC:1.1.1.- Oxidoreductases. Acting on the CH-OH group of donors. With NAD(+) or NADP(+) as acceptor. - NRactivensampson2012-03-05
Assay of protein purified to homogeneity from a heterlogous host
JK. Capyk, R. Kalscheuer et al. Mycobacterial cytochrome p450 125 (cyp125) catalyzes the terminal hydroxylation of c27 steroids. J. Biol. Chem. 2009
TermEC:1.2.1.- Oxidoreductases. Acting on the aldehyde or oxo group of donors. With NAD(+) or NADP(+) as acceptor. - NRactivensampson2012-03-05
Assay of protein purified to homogeneity from a heterlogous host
JK. Capyk, R. Kalscheuer et al. Mycobacterial cytochrome p450 125 (cyp125) catalyzes the terminal hydroxylation of c27 steroids. J. Biol. Chem. 2009