Reviewed, UniProtKB/Swiss-Prot P13029 (KATG_ECOLI)

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
    Hydroperoxidase I
      Short name=HPI

Gene names

Name:	katG
Ordered Locus Names:	b3942, JW3914

Organism

Escherichia coli (strain K12) [Complete proteome] [HAMAP]

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	726 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.
Catalytic activity	2 H(2)O(2) = O(2) + 2 H(2)O. Donor + H(2)O(2) = oxidized donor + 2 H(2)O.
Cofactor	Binds 2 heme B (iron-protoporphyrin IX) groups per tetramer.
Subunit structure	Homotetramer.
Induction	By hydrogen peroxide.
Post-translational modification	The N-terminus is blocked. 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=35 mM for H(2)O(2) for the catalase reaction (at pH 5.5-6.0) KM=4.2 mM for H(2)O(2) for the catalase reaction (at pH 7.0) KM=3.9 mM for H(2)O(2) for the catalase reaction (at pH 7.5) KM=60 µM for H(2)O(2) for the peroxidase reaction KM=24 µM for ABTS for the peroxidase reaction Vmax=3730 µmol/min/mg enzyme for H(2)O(2) for the catalase reaction (at pH 5.5-6.0) Vmax=2220 µmol/min/mg enzyme for H(2)O(2) for the catalase reaction (at pH 7.0) Vmax=18 µmol/min/mg enzyme for ABTS for the peroxidase reaction pH dependence: Optimum pH is 4.25 for the peroxidase reaction and 7.5 for the catalase reaction.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Ligand	Heme Iron Metal-binding
Molecular function	Oxidoreductase Peroxidase
Technical term	3D-structure Complete proteome 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
Cellular component	cytosol Inferred from direct assay. Source: UniProtKB
Molecular function	catalase activity Inferred from electronic annotation. Source: InterPro heme binding Inferred from electronic annotation. Source: InterPro iron ion binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 726

726

Catalase-peroxidase

PRO_0000055564

Sites

Active site

106

1

Proton acceptor By similarity

Metal binding

267

1

Iron (heme axial ligand)

Site

102

1

Transition state stabilizer By similarity

Amino acid modifications

Cross-link

105 ↔ 226

Tryptophyl-tyrosyl-methioninium (Trp-Tyr) (with M-252)

Cross-link

226 ↔ 252

Tryptophyl-tyrosyl-methioninium (Tyr-Met) (with W-105)

Experimental info

Sequence conflict

621

1

A → G in AAA24040. Ref.1

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

726

Helix Strand Turn

Details...

Helix

447 – 458

12

Helix

464 – 475

12

Turn

480 – 483

4

Helix

491 – 493

3

Helix

497 – 499

3

Helix

501 – 503

3

Helix

506 – 509

4

Helix

510 – 520

11

Helix

525 – 541

17

Turn

542 – 545

4

Helix

561 – 563

3

Helix

566 – 570

5

Beta strand

575 – 577

3

Turn

578 – 581

4

Helix

591 – 601

11

Helix

606 – 619

14

Beta strand

623 – 625

3

Helix

641 – 647

7

Beta strand

651 – 657

7

Beta strand

663 – 667

5

Turn

668 – 670

3

Beta strand

673 – 677

5

Helix

679 – 686

8

Helix

688 – 698

11

Helix

703 – 718

16

Turn

719 – 721

3

Sequences

	Sequence		Length	Mass (Da)
	P13029-1 [UniParc]. Last modified October 1, 1993. Version 2. Checksum: 24D32EBED5DE9BD6	FASTA	726	80,024
	10 20 30 40 50 60 MSTSDDIHNT TATGKCPFHQ GGHDQSAGAG TTTRDWWPNQ LRVDLLNQHS NRSNPLGEDF 70 80 90 100 110 120 DYRKEFSKLD YYGLKKDLKA LLTESQPWWP ADWGSYAGLF IRMAWHGAGT YRSIDGRGGA 130 140 150 160 170 180 GRGQQRFAPL NSWPDNVSLD KARRLLWPIK QKYGQKISWA DLFILAGNVA LENSGFRTFG 190 200 210 220 230 240 FGAGREDVWE PDLDVNWGDE KAWLTHRHPE ALAKAPLGAT EMGLIYVNPE GPDHSGEPLS 250 260 270 280 290 300 AAAAIRATFG NMGMNDEETV ALIAGGHTLG KTHGAGPTSN VGPDPEAAPI EEQGLGWAST 310 320 330 340 350 360 YGSGVGADAI TSGLEVVWTQ TPTQWSNYFF ENLFKYEWVQ TRSPAGAIQF EAVDAPEIIP 370 380 390 400 410 420 DPFDPSKKRK PTMLVTDLTL RFDPEFEKIS RRFLNDPQAF NEAFARAWFK LTHRDMGPKS 430 440 450 460 470 480 RYIGPEVPKE DLIWQDPLPQ PIYNPTEQDI IDLKFAIADS GLSVSELVSV AWASASTFRG 490 500 510 520 530 540 GDKRGGANGA RLALMPQRDW DVNAAAVRAL PVLEKIQKES GKASLADIIV LAGVVGVEKA 550 560 570 580 590 600 ASAAGLSIHV PFAPGRVDAR QDQTDIEMFE LLEPIADGFR NYRARLDVST TESLLIDKAQ 610 620 630 640 650 660 QLTLTAPEMT ALVGGMRVLG ANFDGSKNGV FTDRVGVLSN DFFVNLLDMR YEWKATDESK 670 680 690 700 710 720 ELFEGRDRET GEVKFTASRA DLVFGSNSVL RAVAEVYASS DAHEKFVKDF VAAWVKVMNL DRFDLL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of katG, encoding catalase HPI of Escherichia coli." Triggs-Raine B.L., Doble B.W., Mulvey M.R., Sorby P.A., Loewen P.C. J. Bacteriol. 170:4415-4419(1988) [PubMed: 3045098] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
[2]	"The complete genome sequence of Escherichia coli K-12." Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V., Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F., Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B., Shao Y. Science 277:1453-1474(1997) [PubMed: 9278503] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / MG1655 / ATCC 47076.
[3]	"Highly accurate genome sequences of Escherichia coli K-12 strains MG1655 and W3110." Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S., Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T. Mol. Syst. Biol. 2:E1-E5(2006) [PubMed: 16738553] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[4]	"Analysis of the Escherichia coli genome. III. DNA sequence of the region from 87.2 to 89.2 minutes." Plunkett G. III, Burland V., Daniels D.L., Blattner F.R. Nucleic Acids Res. 21:3391-3398(1993) [PubMed: 8346018] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 1-339. Strain: K12 / MG1655 / ATCC 47076.
[5]	"Analysis of the Escherichia coli genome. IV. DNA sequence of the region from 89.2 to 92.8 minutes." Blattner F.R., Burland V.D., Plunkett G. III, Sofia H.J., Daniels D.L. Nucleic Acids Res. 21:5408-5417(1993) [PubMed: 8265357] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] OF 309-726. Strain: K12 / MG1655 / ATCC 47076.
[6]	"Purification of the o-dianisidine peroxidase from Escherichia coli B." Claiborne A., Fridovich I. J. Biol. Chem. 254:4245-4252(1979) [PubMed: 374409] [Abstract] Cited for: BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, HEME-BINDING.
[7]	"Characterization of the catalase-peroxidase KatG from Burkholderia pseudomallei by mass spectrometry." Donald L.J., Krokhin O.V., Duckworth H.W., Wiseman B., Deemagarn T., Singh R., Switala J., Carpena X., Fita I., Loewen P.C. J. Biol. Chem. 278:35687-35692(2003) [PubMed: 12832453] [Abstract] Cited for: COVALENT BOND.
[8]	"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.
[9]	"Structure of the C-terminal domain of the catalase-peroxidase KatG from Escherichia coli." Carpena X., Melik-Adamyan W., Loewen P.C., Fita I. Acta Crystallogr. D 60:1824-1832(2004) [PubMed: 15388929] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 422-726.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M21516 Genomic DNA. Translation: AAA24040.1.
U00096 Genomic DNA. Translation: AAC76924.1.
AP009048 Genomic DNA. Translation: BAE77368.1.
L19201 Genomic DNA. Translation: AAB03074.1.
U00006 Genomic DNA. Translation: AAC43048.1.

PIR

CSECHP. A65201.

RefSeq

AP_003867.1.
NP_418377.1.

3D structure databases

PDBMSD

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1U2J	X-ray	2.30	A/B/C/D/E/F/G/H	422-726	[»]
1U2K	X-ray	2.00	A	422-726	[»]
1U2L	X-ray	2.30	A/B	422-726	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:10053N.

Protein family/group databases

PeroxiBase

2394. EcoCP01_K-12.

2-D gel databases

SWISS-2DPAGE

P13029.

Genome annotation databases

GeneID

948431.

GenomeReviews

Gene locus b3942 in contig U00096_GR.
Gene locus JW3914 in contig AP009048_GR.

KEGG

ecj:JW3914.
eco:b3942.

Organism-specific databases

EchoBASE

EB0506.

EcoGene

EG10511. katG.

CMR

Search...

Phylogenomic databases

HOGENOM

P13029.

Enzyme and pathway databases

BioCyc

EcoCyc:HYDROPEROXIDI-MON.
MetaCyc:HYDROPEROXIDI-MON.

Family and domain databases

HAMAP

MF_01961.
[Tree]

InterPro

IPR000763. Catalase_proxase.
IPR002016. Haem_peroxidase_pln/fun/bac.
[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_ECOLI

Accession

Primary (citable) accession number: P13029
Secondary accession number(s): Q2M8N8

Entry history

Integrated into UniProtKB/Swiss-Prot:	January 1, 1990
Last sequence update:	October 1, 1993
Last modified:	November 25, 2008
This is version 99 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)