Reviewed, UniProtKB/Swiss-Prot A0R609 (KATG1_MYCS2)

Names and origin

Protein names

Recommended name:
    Catalase-peroxidase 1
      Short name=CP 1
    EC=1.11.1.6
    EC=1.11.1.7
Alternative name(s):
    Peroxidase/catalase 1

Gene names

Name:	katG1
Ordered Locus Names:	MSMEG_6384

Organism

Mycobacterium smegmatis (strain ATCC 700084 / mc(2)155) [Complete proteome] [HAMAP]

Taxonomic identifier

246196 [NCBI]

Taxonomic lineage

Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium

Protein attributes

Sequence length	739 AA.
Sequence status	Complete.
Protein existence	Inferred from homology.

General annotation (Comments)

Function	Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. May play a role in the intracellular survival of mycobacteria. HAMAP MF_01961
Catalytic activity	2 H2O2 = O2 + 2 H2O. HAMAP MF_01961 Donor + H2O2 = oxidized donor + 2 H2O. HAMAP MF_01961
Cofactor	Binds 1 heme B (iron-protoporphyrin IX) group per dimer. HAMAP MF_01961
Subunit structure	Homodimer or homotetramer By similarity. HAMAP MF_01961
Post-translational modification	The covalent Trp-Tyr-Met adduct is important for the catalase, but not the peroxidase activity of the enzyme By similarity. HAMAP MF_01961
Disruption phenotype	Defects cause isoniazid (INH) resistance. Ref.1
Sequence similarities	Belongs to the peroxidase family. Peroxidase/catalase subfamily.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	hydrogen peroxide catabolic process Inferred from electronic annotation. Source: UniProtKB-KW oxidation reduction Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	catalase activity Inferred from electronic annotation. Source: HAMAP heme binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 739	739	Catalase-peroxidase 1 HAMAP MF_01961		PRO_0000293596
Sites
	Active site	114	1	Proton acceptor By similarity
	Metal binding	277	1	Iron (heme axial ligand) By similarity
	Site	110	1	Transition state stabilizer By similarity
Amino acid modifications
	Cross-link	113 ↔ 236		Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-262) By similarity
	Cross-link	236 ↔ 262		Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-113) By similarity
Experimental info
	Sequence conflict	374 – 378	5	AHEDG → PTRTA in CAA67268. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	A0R609-1 [UniParc]. Last modified January 9, 2007. Version 1. Checksum: 5E87F6B884D832ED	FASTA	739	81,115
	10 20 30 40 50 60 MPEDRPIEDS PPIGEAQTDA PAGGCPAGFG RIKPPVAGGS NRDWWPNQLN LKILQKNPDV 70 80 90 100 110 120 INPLDEDFDY RSAVQNLDVD ALRADIVEVM HTSQDWWPAD FGHYGPLFIR MAWHAAGTYR 130 140 150 160 170 180 VSDGRGGAGA GMQRFAPLNS WPDNASLDKA RRLLWPVKKK YGKNLSWADL IVYAGNVALE 190 200 210 220 230 240 DMGFRTAGFA FGREDRWEPE EDVYWGPEQE WLDDKRYTGE RDLENPLAAV QMGLIYVNPE 250 260 270 280 290 300 GPNGNPDPQA SAIDIRETFG RMAMNDVETA ALIVGGHTFG KTHGNGDASL VGPEPEAAPL 310 320 330 340 350 360 EEVGLGWRNP QGTGVGKDAI TSGLEVTWTH TPTKWDNSFL EILYGNEWEL TKSPAGANQW 370 380 390 400 410 420 KPKDNGWANS VPLAHEDGKT HPSMLTSDLA LRVDPIYEQI TRRWLDHPEE LAEEFAKAWF 430 440 450 460 470 480 KLLHRDMGPV TRYLGPEVPK DTWLWQDNIP AGNDLSDDEV AKLKELIADS GLTVSQLVST 490 500 510 520 530 540 AWKAASTFRS SDLRGGANGG RIRLQPQLGW EANEPDELAQ VVRKYEEIQK ASGINVSFAD 550 560 570 580 590 600 LVVLGGNVGV EKAAKAAGFD VTVPFTPGRG DATQEETDVD SFAYLEPKAD GFRNYLGKGS 610 620 630 640 650 660 DLPAEFKLID RANLLGLSAP EMTTLVGGLR VLDVNHGGTK HGVLTDKPGA LTTDFFVNLL 670 680 690 700 710 720 DMSTAWKPSP ADDGTYIGTD RATGSPKWTG TRVDLVFASN SQLRALAEVY AEDDSKEKFV 730 KDFVAAWTKV MDADRFDVA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Analysis of isoniazid-resistant transposon mutants of Mycobacterium smegmatis." Billman-Jacobe H., Sloan J., Coppel R.L. FEMS Microbiol. Lett. 144:47-52(1996) [PubMed: 8870251] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], DISRUPTION PHENOTYPE.
[2]	Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M. Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].

Cross-references

Sequence databases
EMBL GenBank DDBJ	X98718 Genomic DNA. Translation: CAA67268.1. CP000480 Genomic DNA. Translation: ABK73944.1.
RefSeq	YP_890597.1.
3D structure databases
SMR	A0R609. Positions 32-738.
ModBase	Search...
Protein-protein interaction databases
STRING	A0R609.
Genome annotation databases
GeneID	4536370.
GenomeReviews	Gene locus MSMEG_6384 in contig CP000480_GR.
KEGG	msm:MSMEG_6384.
NMPDR	fig|246196.1.peg.6346.
TIGR	MSMEG_6384.
Phylogenomic databases
eggNOG	COG0376.
HOGENOM	HBG285610.
OMA	NGWANSV.
PhylomeDB	A0R609.
Family and domain databases
HAMAP	MF_01961. Catal-peroxid. [Tree]
InterPro	IPR000763. Catalase_peroxidase. IPR010255. Haem_peroxidase. IPR002016. Haem_peroxidase_pln/fun/bac. IPR019794. Peroxidases_AS. IPR019793. Peroxidases_heam-ligand_BS. [Graphical view]
Pfam	PF00141. peroxidase. 2 hits. [Graphical view]
PRINTS	PR00460. BPEROXIDASE. PR00458. PEROXIDASE.
TIGRFAMs	TIGR00198. cat_per_HPI. 1 hit.
PROSITE	PS00435. PEROXIDASE_1. 1 hit. PS00436. PEROXIDASE_2. 1 hit. PS50873. PEROXIDASE_4. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

KATG1_MYCS2

Accession

Primary (citable) accession number: A0R609
Secondary accession number(s): O05763, Q59557

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 10, 2007
Last sequence update:	January 9, 2007
Last modified:	February 9, 2010
This is version 25 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes)