Reviewed, UniProtKB/Swiss-Prot P14412 (KATG_BACST)

Names and origin

Protein names

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

Gene names

Name:	katG
Synonyms:	cat, perA

Organism

Bacillus stearothermophilus (Geobacillus stearothermophilus)

Taxonomic identifier

1422 [NCBI]

Taxonomic lineage

Bacteria › Firmicutes › Bacillales › Bacillaceae › Geobacillus

Protein attributes

Sequence length	735 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Bifunctional enzyme with both catalase and broad-spectrum peroxidase activity. Displays also NADH oxidase, INH lyase and isonicotinoyl-NAD synthase activity. 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.
Post-translational modification	The covalent Trp-Tyr-Met adduct is important for the catalase, but not the peroxidase activity of the enzyme By similarity.
Sequence similarities	Belongs to the peroxidase family. Peroxidase/catalase subfamily.
biophysicochemical properties	Kinetic parameters: KM=90 mM for H2O2 for the catalase reaction (at pH 5.5-6.0) HAMAP MF_01961 KM=3.7 mM for H2O2 for the catalase reaction (at pH 7.0) KM=210 mM for H2O2 for the peroxidase reaction KM=31 mM for ABTS for the peroxidase reaction Vmax=5670 µmol/min/mg enzyme for H2O2 for the catalase reaction (at pH 5.5-6.0) Vmax=3410 µmol/min/mg enzyme for H2O2 for the catalase reaction (at pH 7.0) Vmax=8 µmol/min/mg enzyme for ABTS for the peroxidase reaction pH dependence: Optimum pH is 4.0 for the peroxidase reaction.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
Technical term	Direct protein sequencing
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 – 735	735	Catalase-peroxidase HAMAP MF_01961		PRO_0000055567
Sites
	Active site	101	1	Proton acceptor By similarity
	Metal binding	264	1	Iron (heme axial ligand) By similarity
	Site	97	1	Transition state stabilizer By similarity
Amino acid modifications
	Cross-link	100 ↔ 223		Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-249) By similarity
	Cross-link	223 ↔ 249		Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-100) By similarity

Sequences

	Sequence		Length	Mass (Da)
	P14412-1 [UniParc]. Last modified February 1, 1996. Version 2. Checksum: 7131204A4BFABEF1	FASTA	735	82,989
	10 20 30 40 50 60 MENQNRQNAA QCPFHGSVTN QSSNRTTNKD WWPNQLNLSI LHQHDRKTNP HDEEFNYAEE 70 80 90 100 110 120 FQKLDYWALK EDLRKLMTES QDWWPADYGH YGPLFIRMAW HSAGTYRIGD GRGGASTGTQ 130 140 150 160 170 180 RFAPLNSWPD NANLDKARRL LWPIKKKYGN KISWADLFIL AGNVAIESMG GKTIGFGGGR 190 200 210 220 230 240 VDVWHPEEDV YWGSEKEWLA SERYSGDREL ENPLAAVQMG LIYVNPEGPD GKPDPKAAAR 250 260 270 280 290 300 DIRETFRRMG MNDEETVALI AGGHTFGKAH GAGPATHVGP EPEAAPIEAQ GLGWISSYGK 310 320 330 340 350 360 GKGSDTITSG IEGAWTPTPT QWDTSYFDML FGYDWWLTKS PAGAWQWMAV DPDEKDLAPD 370 380 390 400 410 420 AEDPSKKVPT MMMTTDLALR FDPEYEKIAR RFHQNPEEFA EAFARAWFKL THRDMGPKTR 430 440 450 460 470 480 YLGPEVPKED FIWQDPIPEV DYELTEAEIE EIKAKILNSG LTVSELVKTA WASASTFRNS 490 500 510 520 530 540 DKRGGANGAR IRLAPQKDWE VNEPERLAKV LSVYEDIQRE LPKKVSIADL IVLGGSAAVE 550 560 570 580 590 600 KAARDAGFDV KVPFFPGRGD ATQEQTDVES FAVLEPFADG FRNYQKQEYS VPPEELLVDK 610 620 630 640 650 660 AQLLGLTAPE MTVLVGGLRV LGANYRDLPH GVFTDRIGVL TNDFFVNLLD MNYEWVPTDS 670 680 690 700 710 720 GIYEIRDRKT GEVRWTATRV DLIFGSNSIL RSYAEFYAQD DNQEKFVRDF INAWVKVMNA 730 DRFDLVKKAR ESVTA

References

[1]	"Cloning, nucleotide sequence, and expression in Escherichia coli of the Bacillus stearothermophilus peroxidase gene (perA)." Loprasert S., Negoro S., Okada H. J. Bacteriol. 171:4871-4875(1989) [PubMed: 2670897] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE. Strain: ATCC 8005 / IAM11001.
[2]	Trakulnaleamsai S., Aihara S., Miyai K., Suga Y., Yomo T., Negoro S., Urabe I. Submitted (FEB-1992) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION.
[3]	"Evolutionary molecular engineering by random elongation mutagenesis." Matsuura T., Miyai K., Trakulnaleaamsai S., Yomo T., Shima Y., Miki S., Yamamoto K., Urabe I. Nat. Biotechnol. 17:58-61(1999) [PubMed: 9920270] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[4]	"Comparative study of catalase-peroxidases (KatGs)." Singh R., Wiseman B., Deemagarn T., Jha V., Switala J., Loewen P.C. Arch. Biochem. Biophys. 471:207-214(2008) [PubMed: 18178143] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES.

Cross-references

Sequence databases
EMBLGenBankDDBJ	M29876 mRNA. Translation: AAA22655.1. AB020234 Genomic DNA. Translation: BAA37114.1.
PIR	JS0520.
3D structure databases
HSSP	HSSP built from PDB template 1MWV based on UniProtKB Q939D2.
ModBase	Search...
Protein family/group databases
PeroxiBase	2437. GstCP01.
Enzyme and pathway databases
BRENDA	1.11.1.6. 266715.
Family and domain databases
HAMAP	MF_01961. [Tree]
InterPro	IPR000763. Catalase_proxase. 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

KATG_BACST

Accession

Primary (citable) accession number: P14412

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	February 1, 1996
Last modified:	May 5, 2009
This is version 70 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

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