[1]	NUCLEOTIDE SEQUENCE [GENOMIC DNA]. STRAIN=BCG; PubMed=7746145 [NCBI, ExPASy, EBI, Israel, Japan] Heym B., Alzari P.M., Honore N., Cole S.T.; "Missense mutations in the catalase-peroxidase gene, katG, are associated with isoniazid resistance in Mycobacterium tuberculosis."; Mol. Microbiol. 15:235-245(1995).
[2]	NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. STRAIN=ATCC BAA-935 / AF2122/97; DOI=10.1073/pnas.1130426100; PubMed=12788972 [NCBI, ExPASy, EBI, Israel, Japan] Garnier T., Eiglmeier K., Camus J.-C., Medina N., Mansoor H., Pryor M., Duthoy S., Grondin S., Lacroix C., Monsempe C., Simon S., Harris B., Atkin R., Doggett J., Mayes R., Keating L., Wheeler P.R., Parkhill J., Barrell B.G., Cole S.T., Gordon S.V., Hewinson R.G.; "The complete genome sequence of Mycobacterium bovis."; Proc. Natl. Acad. Sci. U.S.A. 100:7877-7882(2003).
[3]	FUNCTION, AND SUBUNIT. DOI=10.1016/j.bbagen.2005.12.026; PubMed=16563633 [NCBI, ExPASy, EBI, Israel, Japan] Kang S.-K., Lee J.-H., Lee Y.-C., Kim C.-H.; "Catalase-peroxidase of Mycobacterium bovis BCG converts isoniazid to isonicotinamide, but not to isonicotinic acid: differentiation parameter between enzymes of Mycobacterium bovis BCG and Mycobacterium tuberculosis."; Biochim. Biophys. Acta 1760:724-729(2006).

Comments

FUNCTION: Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. May play a role in the intracellular survival of mycobacteria.
CATALYTIC ACTIVITY: 2 H₂O₂ = O₂ + 2 H₂O.
CATALYTIC ACTIVITY: Donor + H₂O₂ = oxidized donor + 2 H₂O.
COFACTOR: Binds 1 heme B (iron-protoporphyrin IX) group per dimer (By similarity).
SUBUNIT: Homodimer.
PTM: The covalent Trp-Tyr-Met adduct is important for the catalase, but not the peroxidase activity of the enzyme (By similarity).
SIMILARITY: Belongs to the peroxidase family. Peroxidase/catalase subfamily.

Copyright

Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.

Cross-references

Sequence databases

EMBL

X83277; CAA58266.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]
BX248340; CAD94645.1; -; Genomic_DNA.	[EMBL / GenBank / DDBJ] [CoDingSequence]

RefSeq

NP_855594.1; -.

3D structure databases

HSSP

Q939D2; 1MWV. [HSSP ENTRY / PDB]

SMR

P46817; 26-740.

ModBase

P46817.

Protein family/group databases

PeroxiBase

2434; MboCP01_BCG.
4578; MboCP01_AF2122.

Family and domain databases

InterPro

IPR000763; Catalase_proxase.
IPR002016; Haem_peroxidase_pln/fun/bac.
Graphical view of domain structure.

Pfam

PF00141; peroxidase; 2.
Pfam graphical view of domain structure.

PRINTS

PR00460; BPEROXIDASE.
PR00458; PEROXIDASE.

TIGRFAMs

TIGR00198; cat_per_HPI; 1.

PROSITE

PS00435; PEROXIDASE_1; 1.
PS00436; PEROXIDASE_2; 1.
PS50873; PEROXIDASE_4; 1.
PROSITE graphical view of domain structure (profiles).

BLOCKS

P46817.

Genome annotation databases

GeneID

1093267; -.

GenomeReviews

BX248333_GR; Mb1943c.

KEGG

mbo:Mb1943c; -.

Phylogenomic databases

HOGENOM

P46817; -.

Genome annotation databases

CMR

P46817; Mb1943c.

Other

ProtoNet

P46817.

UniRef

View cluster of proteins with at least 50% / 90% / 100% identity.

Keywords

Complete proteome; Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase; Peroxidase.

Features

Feature table viewer

`Key`	`From To`	`Length`	`Description`	`FTId`
`CHAIN`	`1 740`	`740`	`Peroxidase/catalase.`	`PRO_0000055571`
`ACT_SITE`	`108 108`		`Proton acceptor (By similarity).`
`METAL`	`270 270`		`Iron (heme axial ligand) (By similarity).`
`SITE`	`104 104`	`1`	`Transition state stabilizer (By similarity).`
`CROSSLNK`	`107 229`		`Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-255) (By similarity).`
`CROSSLNK`	`229 255`		`Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-107) (By similarity).`
`CONFLICT`	`234 234`		`G -> A (in Ref. 1; CAA58266).`

Sequence information

Length: 740 AA [This is the length of the unprocessed precursor]

Molecular weight: 80562 Da [This is the MW of the unprocessed precursor]

CRC64: 8231F1E473397908 [This is a checksum on the sequence]

        10         20         30         40         50         60 
MPEQHPPITE TTTGAASNGC PVVGHMKYPV EGGGNQDWWP NRLNLKVLHQ NPAVADPMGA 

        70         80         90        100        110        120 
AFDYAAEVAT IDVDALTRDI EEVMTTSQPW WPADYGHYGP LFIRMAWHAA GTYRIHDGRG 

       130        140        150        160        170        180 
GAGGGMQRFA PLNSWPDNAS LDKARRLLWP VKKKYGKKLS WADLIVFAGN CALESMGFKT 

       190        200        210        220        230        240 
FGFGFGRVDQ WEPDEVYWGK EATWLGDERY SGKRDLENPL AAVQMGLIYV NPEGPNGNPD 

       250        260        270        280        290        300 
PMAAAVDIRE TFRRMAMNDV ETAALIVGGH TFGKTHGAGP ADLVGPEPEA APLEQMGLGW 

       310        320        330        340        350        360 
KSSYGTGTGK DAITSGIEVV WTNTPTKWDN SFLEILYGYE WELTKSPAGA WQYTAKDGAG 

       370        380        390        400        410        420 
AGTIPDPFGG PGRSPTMLAT DLSLRVDPIY ERITRRWLEH PEELADEFAK AWYKLIHRDM 

       430        440        450        460        470        480 
GPVARYLGPL VPKQTLLWQD PVPAVSHDLV GEAEIASLKS QILASGLTVS QLVSTAWAAA 

       490        500        510        520        530        540 
SSFRGSDKRG GANGGRIRLQ PQVGWEVNDP DGDLRKVIRT LEEIQESFNS AAPGNIKVSF 

       550        560        570        580        590        600 
ADLVVLGGCA AIEKAAKAAG HNITVPFTPG RTDASQEQTD VESFAVLEPK ADGFRNYLGK 

       610        620        630        640        650        660 
GNPLPAEYML LDKANLLTLS APEMTVLVGG LRVLGANYKR LPLGVFTEAS ESLTNDFFVN 

       670        680        690        700        710        720 
LLDMGITWEP SPADDGTYQG KDGSGKVKWT GSRVDLVFGS NSELRALVEV YGADDAQPKF 

       730        740 
VQDFVAAWDK VMNLDRFDVR

P46817 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
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	BLAST submission on ExPASy/SIB or at NCBI (USA)		Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
	ScanProsite, MotifScan		Submit a homology modeling request to SWISS-MODEL
	NPSA Sequence analysis tools