Reviewed, UniProtKB/Swiss-Prot P21179 (CATE_ECOLI)

Names and origin

Protein names

Recommended name:
    Catalase HPII
    EC=1.11.1.6
Alternative name(s):
    Hydroxyperoxidase II

Gene names

Name:	katE
Ordered Locus Names:	b1732, JW1721

Organism

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

Taxonomic identifier

83333 [NCBI]

Taxonomic lineage

Bacteria › Proteobacteria › Gammaproteobacteria › Enterobacteriales › Enterobacteriaceae › Escherichia

Protein attributes

Sequence length	753 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Decomposes hydrogen peroxide into water and oxygen; serves to protect cells from the toxic effects of hydrogen peroxide.
Catalytic activity	2 H2O2 = O2 + 2 H2O.
Cofactor	Heme group.
Subunit structure	Homotetramer.
Subcellular location	Cytoplasm Probable.
Induction	By entry into stationary phase.
Sequence similarities	Belongs to the catalase family. HPII subfamily.

Ontologies

Keywords
Biological process	Hydrogen peroxide
Cellular component	Cytoplasm
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: EC 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 – 753

753

Catalase HPII

PRO_0000084971

Sites

Active site

128

1

By similarity

Active site

201

1

By similarity

Metal binding

415

1

Iron (heme axial ligand)

Amino acid modifications

Cross-link

392 ↔ 415

3'-histidyl-3-tyrosine (His-Tyr)

Secondary structure

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753

Helix Strand Turn

Details...

Helix

53 – 56

4

Helix

63 – 67

5

Helix

68 – 71

4

Beta strand

87 – 89

3

Beta strand

95 – 98

4

Helix

108 – 118

11

Beta strand

130 – 142

13

Turn

145 – 147

3

Helix

151 – 153

3

Beta strand

160 – 171

12

Beta strand

177 – 181

5

Beta strand

183 – 191

9

Beta strand

194 – 205

12

Helix

211 – 213

3

Helix

214 – 221

8

Turn

225 – 228

4

Helix

237 – 245

9

Helix

247 – 249

3

Helix

250 – 257

8

Helix

259 – 261

3

Beta strand

262 – 264

3

Helix

266 – 268

3

Beta strand

277 – 280

4

Beta strand

286 – 295

10

Helix

304 – 313

10

Helix

317 – 327

11

Beta strand

333 – 342

10

Helix

343 – 345

3

Beta strand

349 – 351

3

Turn

362 – 364

3

Beta strand

368 – 377

10

Helix

382 – 385

4

Turn

386 – 388

3

Helix

406 – 423

18

Helix

428 – 430

3

Helix

432 – 434

3

Beta strand

459 – 462

4

Turn

465 – 468

4

Beta strand

477 – 479

3

Beta strand

488 – 495

8

Helix

499 – 501

3

Helix

506 – 513

8

Helix

517 – 532

16

Helix

537 – 548

12

Helix

552 – 561

10

Helix

568 – 571

4

Helix

586 – 588

3

Beta strand

589 – 593

5

Beta strand

602 – 606

5

Helix

613 – 625

13

Beta strand

629 – 641

13

Beta strand

647 – 649

3

Turn

654 – 656

3

Helix

659 – 661

3

Beta strand

663 – 667

5

Helix

673 – 676

4

Helix

679 – 690

12

Beta strand

695 – 698

4

Helix

699 – 706

8

Turn

707 – 709

3

Beta strand

718 – 724

7

Helix

726 – 737

12

Helix

742 – 744

3

Helix

745 – 748

4

Sequences

	Sequence		Length	Mass (Da)
	P21179-1 [UniParc]. Last modified May 1, 1991. Version 1. Checksum: 1F034E4866A70FB9	FASTA	753	84,163
	10 20 30 40 50 60 MSQHNEKNPH QHQSPLHDSS EAKPGMDSLA PEDGSHRPAA EPTPPGAQPT APGSLKAPDT 70 80 90 100 110 120 RNEKLNSLED VRKGSENYAL TTNQGVRIAD DQNSLRAGSR GPTLLEDFIL REKITHFDHE 130 140 150 160 170 180 RIPERIVHAR GSAAHGYFQP YKSLSDITKA DFLSDPNKIT PVFVRFSTVQ GGAGSADTVR 190 200 210 220 230 240 DIRGFATKFY TEEGIFDLVG NNTPIFFIQD AHKFPDFVHA VKPEPHWAIP QGQSAHDTFW 250 260 270 280 290 300 DYVSLQPETL HNVMWAMSDR GIPRSYRTME GFGIHTFRLI NAEGKATFVR FHWKPLAGKA 310 320 330 340 350 360 SLVWDEAQKL TGRDPDFHRR ELWEAIEAGD FPEYELGFQL IPEEDEFKFD FDLLDPTKLI 370 380 390 400 410 420 PEELVPVQRV GKMVLNRNPD NFFAENEQAA FHPGHIVPGL DFTNDPLLQG RLFSYTDTQI 430 440 450 460 470 480 SRLGGPNFHE IPINRPTCPY HNFQRDGMHR MGIDTNPANY EPNSINDNWP RETPPGPKRG 490 500 510 520 530 540 GFESYQERVE GNKVRERSPS FGEYYSHPRL FWLSQTPFEQ RHIVDGFSFE LSKVVRPYIR 550 560 570 580 590 600 ERVVDQLAHI DLTLAQAVAK NLGIELTDDQ LNITPPPDVN GLKKDPSLSL YAIPDGDVKG 610 620 630 640 650 660 RVVAILLNDE VRSADLLAIL KALKAKGVHA KLLYSRMGEV TADDGTVLPI AATFAGAPSL 670 680 690 700 710 720 TVDAVIVPCG NIADIADNGD ANYYLMEAYK HLKPIALAGD ARKFKATIKI ADQGEEGIVE 730 740 750 ADSADGSFMD ELLTLMAAHR VWSRIPKIDK IPA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Nucleotide sequence of Escherichia coli katE, which encodes catalase HPII." von Ossowski I., Mulvey M.R., Leco P.A., Borys A., Loewen P.C. J. Bacteriol. 173:514-520(1991) [PubMed: 1987146] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-10. Strain: K12.
[2]	"A 570-kb DNA sequence of the Escherichia coli K-12 genome corresponding to the 28.0-40.1 min region on the linkage map." Aiba H., Baba T., Fujita K., Hayashi K., Inada T., Isono K., Itoh T., Kasai H., Kashimoto K., Kimura S., Kitakawa M., Kitagawa M., Makino K., Miki T., Mizobuchi K., Mori H., Mori T., Motomura K. , Nakade S., Nakamura Y., Nashimoto H., Nishio Y., Oshima T., Saito N., Sampei G., Seki Y., Sivasundaram S., Tagami H., Takeda J., Takemoto K., Takeuchi Y., Wada C., Yamamoto Y., Horiuchi T. DNA Res. 3:363-377(1996) [PubMed: 9097039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: K12 / W3110 / ATCC 27325 / DSM 5911.
[3]	"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.
[4]	"Escherichia coli K-12: a cooperatively developed annotation snapshot -- 2005." Riley M., Abe T., Arnaud M.B., Berlyn M.K.B., Blattner F.R., Chaudhuri R.R., Glasner J.D., Horiuchi T., Keseler I.M., Kosuge T., Mori H., Perna N.T., Plunkett G. III, Rudd K.E., Serres M.H., Thomas G.H., Thomson N.R., Wishart D., Wanner B.L. Nucleic Acids Res. 34:1-9(2006) [PubMed: 16397293] [Abstract] Cited for: SEQUENCE REVISION TO 198.
[5]	"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.
[6]	"Identification of a novel bond between a histidine and the essential tyrosine in catalase HPII of Escherichia coli." Bravo J., Fita I., Ferrer J.C., Ens W., Hillar A., Switala J., Loewen P.C. Protein Sci. 6:1016-1023(1997) [PubMed: 9144772] [Abstract] Cited for: CROSS-LINK 392-HIS--TYR-415.
[7]	"Crystal structure of catalase HPII from Escherichia coli." Bravo J., Verdaguer N., Tormo J., Betzel C., Switala J., Loewen P.C., Fita I. Structure 3:491-502(1995) [PubMed: 7663946] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
[8]	"Role of the lateral channel in catalase HPII of Escherichia coli." Sevinc M.S., Mate M.J., Switala J., Fita I., Loewen P.C. Protein Sci. 8:490-498(1999) [PubMed: 10091651] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[9]	"Substrate flow in catalases deduced from the crystal structures of active site variants of HPII from Escherichia coli." Melik-Adamyan W.R., Bravo J., Carpena X., Switala J., Mate M.J., Fita I., Loewen P.C. Proteins 44:270-281(2001) [PubMed: 11455600] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS).
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

M55161 Genomic DNA. Translation: AAA24039.1.
U00096 Genomic DNA. Translation: AAT48137.1.
AP009048 Genomic DNA. Translation: BAA15513.1.

PIR

A39129.

RefSeq

AP_002351.1.
YP_025308.1.

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1CF9	X-ray	1.80	A/B/C/D	1-753	[»]
1GG9	X-ray	1.89	A/B/C/D	1-753	[»]
1GGE	X-ray	1.89	A/B/C/D	1-753	[»]
1GGF	X-ray	2.28	A/B/C/D	1-753	[»]
1GGH	X-ray	2.15	A/B/C/D	1-753	[»]
1GGJ	X-ray	1.92	A/B/C/D	1-753	[»]
1GGK	X-ray	2.26	A/B/C/D	1-753	[»]
1IPH	X-ray	2.80	A/B/C/D	1-753	[»]
1P7Y	X-ray	2.40	A/B/C/D	1-753	[»]
1P7Z	X-ray	2.21	A/B/C/D	1-753	[»]
1P80	X-ray	1.65	A/B/C/D	1-753	[»]
1P81	X-ray	1.81	A/B/C/D	1-753	[»]
1QF7	X-ray	2.20	A/B/C/D	1-753	[»]
1QWS	X-ray	1.90	A/B/C/D	1-753	[»]
1YE9	X-ray	2.80	A/B/C/D/I/J/K/L	75-300	[»]
			E/F/G/H/M/N/O/P	309-567	[»]

ModBase

Search...

Protein-protein interaction databases

DIP

DIP:10052N.

Protein family/group databases

PeroxiBase

5321. EcoKatE.

2-D gel databases

SWISS-2DPAGE

P21179.

Genome annotation databases

GeneID

946234.

GenomeReviews

Gene locus JW1721 in contig AP009048_GR.
Gene locus b1732 in contig U00096_GR.

KEGG

ecj:JW1721.
eco:b1732.

Organism-specific databases

EchoBASE

EB0504.

EcoGene

EG10509. katE.

CMR

Search...

Phylogenomic databases

HOGENOM

P21179.

OMA

P21179. FCFEVGK.

Enzyme and pathway databases

BioCyc

EcoCyc:HYDROPEROXIDII-MON.
MetaCyc:HYDROPEROXIDII-MON.

Family and domain databases

InterPro

IPR002226. Catalase.
IPR010582. Catalase-rel_immune_responsive.
IPR011614. Catalase_N.
IPR018028. Catalase_rel_subgroup.
[Graphical view]

Gene3D

G3DSA:2.40.180.10. Catalase_N. 1 hit.

PANTHER

PTHR11465. Catalase. 1 hit.

Pfam

PF00199. Catalase. 1 hit.
PF06628. Catalase-rel. 1 hit.
[Graphical view]

PRINTS

PR00067. CATALASE.

ProDom

PD000510. Catalase. 1 hit.
[Graphical view] [Entries sharing at least one domain]

PROSITE

PS00437. CATALASE_1. 1 hit.
PS00438. CATALASE_2. 1 hit.
PS51402. CATALASE_3. 1 hit.
[Graphical view]

ProtoNet

Search...

Entry information

Entry name

CATE_ECOLI

Accession

Primary (citable) accession number: P21179
Secondary accession number(s): P76906, P78066, P78168

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 1, 1991
Last sequence update:	May 1, 1991
Last modified:	June 16, 2009
This is version 96 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)