Rv1908c - catalase-peroxidase-peroxynitritase T katG

Expression: Most Significant Conditions for Rv1908c

Protein Domains

Gene Information
Locus	Rv1908c
Symbol	katG
Gene Name	catalase-peroxidase-peroxynitritase T katG
Location	2153889 - 2156111 (-)
Species	Mycobacterium tuberculosis H37Rv complete genome.
Length	Gene:2223 bp Protein:741 aa
External Links	Tuberculist Target Gene Information String Protein-Protein Interactions STITCH Chemical-Protein Interactions Search Google Scholar
Orthologs
Orthogroup Number	18922
Related Genes	MAP1668c MAV_2753 MSMEG_3729 MT1959 MUL_2190 nfa29500 SCO0560
Transcriptional Regulation
Operons	View gene in operon browser
Regulatory Network	Search for regulators of Rv1908c
Expression Correlation	Genes with Correlated Expression Scatterplot of Gene Expression

Sequence

Proteins

>Rv1908c Transcript 1
MPEQHPPITETTTGAASNGCPVVGHMKYPVEGGGNQDWWPNRLNLKVLHQNPAVADPMGA
AFDYAAEVATIDVDALTRDIEEVMTTSQPWWPADYGHYGPLFIRMAWHAAGTYRIHDGRG
GAGGGMQRFAPLNSWPDNASLDKARRLLWPVKKKYGKKLSWADLIVFAGNCALESMGFKT
FGFGFGRVDQWEPDEVYWGKEATWLGDERYSGKRDLENPLAAVQMGLIYVNPEGPNGNPD
PMAAAVDIRETFRRMAMNDVETAALIVGGHTFGKTHGAGPADLVGPEPEAAPLEQMGLGW
KSSYGTGTGKDAITSGIEVVWTNTPTKWDNSFLEILYGYEWELTKSPAGAWQYTAKDGAG
AGTIPDPFGGPGRSPTMLATDLSLRVDPIYERITRRWLEHPEELADEFAKAWYKLIHRDM
GPVARYLGPLVPKQTLLWQDPVPAVSHDLVGEAEIASLKSQIRASGLTVSQLVSTAWAAA
SSFRGSDKRGGANGGRIRLQPQVGWEVNDPDGDLRKVIRTLEEIQESFNSAAPGNIKVSF
ADLVVLGGCAAIEKAAKAAGHNITVPFTPGRTDASQEQTDVESFAVLEPKADGFRNYLGK
GNPLPAEYMLLDKANLLTLSAPEMTVLVGGLRVLGANYKRLPLGVFTEASESLTNDFFVN
LLDMGITWEPSPADDGTYQGKDGSGKVKWTGSRVDLVFGSNSELRALVEVYGADDAQPKF
VQDFVAAWDKVMNLDRFDVR*

Genomic Sequence

>Rv1908c
GTGCCCGAGCAACACCCACCCATTACAGAAACCACCACCGGAGCCGCTAGCAACGGCTGT
CCCGTCGTGGGTCATATGAAATACCCCGTCGAGGGCGGCGGAAACCAGGACTGGTGGCCC
AACCGGCTCAATCTGAAGGTACTGCACCAAAACCCGGCCGTCGCTGACCCGATGGGTGCG
GCGTTCGACTATGCCGCGGAGGTCGCGACCATCGACGTTGACGCCCTGACGCGGGACATC
GAGGAAGTGATGACCACCTCGCAGCCGTGGTGGCCCGCCGACTACGGCCACTACGGGCCG
CTGTTTATCCGGATGGCGTGGCACGCTGCCGGCACCTACCGCATCCACGACGGCCGCGGC
GGCGCCGGGGGCGGCATGCAGCGGTTCGCGCCGCTTAACAGCTGGCCCGACAACGCCAGC
TTGGACAAGGCGCGCCGGCTGCTGTGGCCGGTCAAGAAGAAGTACGGCAAGAAGCTCTCA
TGGGCGGACCTGATTGTTTTCGCCGGCAACTGCGCGCTGGAATCGATGGGCTTCAAGACG
TTCGGGTTCGGCTTCGGCCGGGTCGACCAGTGGGAGCCCGATGAGGTCTATTGGGGCAAG
GAAGCCACCTGGCTCGGCGATGAGCGTTACAGCGGTAAGCGGGATCTGGAGAACCCGCTG
GCCGCGGTGCAGATGGGGCTGATCTACGTGAACCCGGAGGGGCCGAACGGCAACCCGGAC
CCCATGGCCGCGGCGGTCGACATTCGCGAGACGTTTCGGCGCATGGCCATGAACGACGTC
GAAACAGCGGCGCTGATCGTCGGCGGTCACACTTTCGGTAAGACCCATGGCGCCGGCCCG
GCCGATCTGGTCGGCCCCGAACCCGAGGCTGCTCCGCTGGAGCAGATGGGCTTGGGCTGG
AAGAGCTCGTATGGCACCGGAACCGGTAAGGACGCGATCACCAGCGGCATCGAGGTCGTA
TGGACGAACACCCCGACGAAATGGGACAACAGTTTCCTCGAGATCCTGTACGGCTACGAG
TGGGAGCTGACGAAGAGCCCTGCTGGCGCTTGGCAATACACCGCCAAGGACGGCGCCGGT
GCCGGCACCATCCCGGACCCGTTCGGCGGGCCAGGGCGCTCCCCGACGATGCTGGCCACT
GACCTCTCGCTGCGGGTGGATCCGATCTATGAGCGGATCACGCGTCGCTGGCTGGAACAC
CCCGAGGAATTGGCCGACGAGTTCGCCAAGGCCTGGTACAAGCTGATCCACCGAGACATG
GGTCCCGTTGCGAGATACCTTGGGCCGCTGGTCCCCAAGCAGACCCTGCTGTGGCAGGAT
CCGGTCCCTGCGGTCAGCCACGACCTCGTCGGCGAAGCCGAGATTGCCAGCCTTAAGAGC
CAGATCCGGGCATCGGGATTGACTGTCTCACAGCTAGTTTCGACCGCATGGGCGGCGGCG
TCGTCGTTCCGTGGTAGCGACAAGCGCGGCGGCGCCAACGGTGGTCGCATCCGCCTGCAG
CCACAAGTCGGGTGGGAGGTCAACGACCCCGACGGGGATCTGCGCAAGGTCATTCGCACC
CTGGAAGAGATCCAGGAGTCATTCAACTCCGCGGCGCCGGGGAACATCAAAGTGTCCTTC
GCCGACCTCGTCGTGCTCGGTGGCTGTGCCGCCATAGAGAAAGCAGCAAAGGCGGCTGGC
CACAACATCACGGTGCCCTTCACCCCGGGCCGCACGGATGCGTCGCAGGAACAAACCGAC
GTGGAATCCTTTGCCGTGCTGGAGCCCAAGGCAGATGGCTTCCGAAACTACCTCGGAAAG
GGCAACCCGTTGCCGGCCGAGTACATGCTGCTCGACAAGGCGAACCTGCTTACGCTCAGT
GCCCCTGAGATGACGGTGCTGGTAGGTGGCCTGCGCGTCCTCGGCGCAAACTACAAGCGC
TTACCGCTGGGCGTGTTCACCGAGGCCTCCGAGTCACTGACCAACGACTTCTTCGTGAAC
CTGCTCGACATGGGTATCACCTGGGAGCCCTCGCCAGCAGATGACGGGACCTACCAGGGC
AAGGATGGCAGTGGCAAGGTGAAGTGGACCGGCAGCCGCGTGGACCTGGTCTTCGGGTCC
AACTCGGAGTTGCGGGCGCTTGTCGAGGTCTATGGCGCCGATGACGCGCAGCCGAAGTTC
GTGCAGGACTTCGTCGCTGCCTGGGACAAGGTGATGAACCTCGACAGGTTCGACGTGCGC
TGA

Community Annotations Pending Curatorial Review

Field	Value	Status	Creator	Date
Term	TBRXN:SPODM superoxide dismutase - ISS	active	njamshidi	2012-10-05
	KatG is a bifunctional enzyme . PMID 15840564 RA. Ghiladi, GM. Knudsen et al. The Met-Tyr-Trp cross-link in Mycobacterium tuberculosis catalase-peroxidase (KatG): autocatalytic formation and effect on enzyme catalysis and spectroscopic properties. J. Biol. Chem. 2005
Term	EC:1.15.1.1 Superoxide dismutase. - ISS	active	njamshidi	2012-10-05
	KatG is a bifunctional enzyme . PMID 15840564 RA. Ghiladi, GM. Knudsen et al. The Met-Tyr-Trp cross-link in Mycobacterium tuberculosis catalase-peroxidase (KatG): autocatalytic formation and effect on enzyme catalysis and spectroscopic properties. J. Biol. Chem. 2005
Term	TBRXN:PRDX Peroxidase (multiple substrates) - ISS	active	njamshidi	2012-10-05
	added during gap filling; peroxidase activity of multiple substrates has been associated based on sequence (verfified again by SEED), methanol metabolism has been demonstrated in literature (PMID 12486050) authors,SW. Park,EH. Hwang,H. Park,JA. Kim,J. Heo,KH. Lee,T. Song,E. Kim,YT. Ro,SW. Kim,YM. Kim Growth of mycobacteria on carbon monoxide and methanol. J. Bacteriol. 2003
Term	EC:1.11.1.7 Peroxidase. - ISS	active	njamshidi	2012-10-05
	added during gap filling; peroxidase activity of multiple substrates has been associated based on sequence (verfified again by SEED), methanol metabolism has been demonstrated in literature (PMID 12486050) authors,SW. Park,EH. Hwang,H. Park,JA. Kim,J. Heo,KH. Lee,T. Song,E. Kim,YT. Ro,SW. Kim,YM. Kim Growth of mycobacteria on carbon monoxide and methanol. J. Bacteriol. 2003
Term	TBRXN:CAT catalase - ISS	active	njamshidi	2012-10-05
	PMID: 15231843. the catalase activity is more crucial to its survival than the peroxidase activity PMID: 16315359 authors,NA. Eady,NA. Jesmin,S. Servos,AE. Cass,JM. Nagy,KA. Brown Probing the function of Mycobacterium tuberculosis catalase-peroxidase by site-directed mutagenesis. Dalton Trans 2005
Term	EC:1.11.1.6 Catalase. - ISS	active	njamshidi	2012-10-05
	PMID: 15231843. the catalase activity is more crucial to its survival than the peroxidase activity PMID: 16315359 authors,NA. Eady,NA. Jesmin,S. Servos,AE. Cass,JM. Nagy,KA. Brown Probing the function of Mycobacterium tuberculosis catalase-peroxidase by site-directed mutagenesis. Dalton Trans 2005
Term	TBRXN:CAT catalase - ISS	active	njamshidi	2012-10-05
	PMID: 15231843. the catalase activity is more crucial to its survival than the peroxidase activity PMID: 16315359 authors,T. Bertrand,NA. Eady,JN. Jones,null. Jesmin,JM. Nagy,B. Jamart-Grégoire,EL. Raven,KA. Brown Crystal structure of Mycobacterium tuberculosis catalase-peroxidase. J. Biol. Chem. 2004
Term	EC:1.11.1.6 Catalase. - ISS	active	njamshidi	2012-10-05
	PMID: 15231843. the catalase activity is more crucial to its survival than the peroxidase activity PMID: 16315359 authors,T. Bertrand,NA. Eady,JN. Jones,null. Jesmin,JM. Nagy,B. Jamart-Grégoire,EL. Raven,KA. Brown Crystal structure of Mycobacterium tuberculosis catalase-peroxidase. J. Biol. Chem. 2004
Term	TBRXN:CAT catalase - IDA	active	njamshidi	2012-10-05
	PMID: 15231843. the catalase activity is more crucial to its survival than the peroxidase activity PMID: 16315359 authors,NA. Eady,NA. Jesmin,S. Servos,AE. Cass,JM. Nagy,KA. Brown Probing the function of Mycobacterium tuberculosis catalase-peroxidase by site-directed mutagenesis. Dalton Trans 2005
Term	EC:1.11.1.6 Catalase. - IDA	active	njamshidi	2012-10-05
	PMID: 15231843. the catalase activity is more crucial to its survival than the peroxidase activity PMID: 16315359 authors,NA. Eady,NA. Jesmin,S. Servos,AE. Cass,JM. Nagy,KA. Brown Probing the function of Mycobacterium tuberculosis catalase-peroxidase by site-directed mutagenesis. Dalton Trans 2005
Term	TBRXN:CAT catalase - IDA	active	njamshidi	2012-10-05
	PMID: 15231843. the catalase activity is more crucial to its survival than the peroxidase activity PMID: 16315359 authors,T. Bertrand,NA. Eady,JN. Jones,null. Jesmin,JM. Nagy,B. Jamart-Grégoire,EL. Raven,KA. Brown Crystal structure of Mycobacterium tuberculosis catalase-peroxidase. J. Biol. Chem. 2004
Term	EC:1.11.1.6 Catalase. - IDA	active	njamshidi	2012-10-05
	PMID: 15231843. the catalase activity is more crucial to its survival than the peroxidase activity PMID: 16315359 authors,T. Bertrand,NA. Eady,JN. Jones,null. Jesmin,JM. Nagy,B. Jamart-Grégoire,EL. Raven,KA. Brown Crystal structure of Mycobacterium tuberculosis catalase-peroxidase. J. Biol. Chem. 2004
Interaction	Transcription Rv1909c	active	kaveri.verma	2012-10-05
	Mutation studies AS. Pym, P. Domenech et al. Regulation of catalase-peroxidase (KatG) expression, isoniazid sensitivity and virulence by furA of Mycobacterium tuberculosis. Mol. Microbiol. 2001
Interaction	PhysicalInteraction Rv1908c	active	jgalag	2012-10-05
	Yeast two-hybrid (Physical interaction) M. Wilming & K. Johnsson Inter- and intramolecular domain interactions of the catalase-peroxidase KatG from M. tuberculosis. FEBS Lett. 2001
Interaction	PhysicalInteraction Rv1908c	active	jgalag	2012-10-05
	Yeast two-hybrid (Physical interaction) M. Wilming & K. Johnsson Inter- and intramolecular domain interactions of the catalase-peroxidase KatG from M. tuberculosis. FEBS Lett. 2001
Interaction	Regulatory Rv0117	active	shahanup86	2012-10-05
	Co-expression (Functional linkage) M. Guo, H. Feng et al. Dissecting transcription regulatory pathways through a new bacterial one-hybrid reporter system. Genome Res. 2009
Interaction	RegulatedBy Rv3416	active	yamir.moreno	2012-10-05
	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
Interaction	RegulatedBy Rv2034	active	yamir.moreno	2012-10-05
	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
Interaction	RegulatedBy Rv0117	active	yamir.moreno	2012-10-05
	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
Interaction	RegulatedBy Rv0117	active	yamir.moreno	2012-10-05
	E.coli orthology based inference. Orthologous pair regulator-target found in E.coli. G. Balázsi, AP. Heath et al. The temporal response of the Mycobacterium tuberculosis gene regulatory network during growth arrest. Mol. Syst. Biol. 2008
Interaction	RegulatedBy Rv0117	active	yamir.moreno	2012-10-05
	E.coli orthology based inference. Orthologous pair regulator-target found in E.coli. authors,M. Madan Babu,SA. Teichmann,L. Aravind Evolutionary dynamics of prokaryotic transcriptional regulatory networks. J. Mol. Biol. 2006