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Catalase HPII (EC 1.11.1.6) (Hydroxyperoxidase II)

 CATE_ECOLI              Reviewed;         753 AA.
P21179; P76906; P78066; P78168;
01-MAY-1991, integrated into UniProtKB/Swiss-Prot.
01-MAY-1991, sequence version 1.
28-MAR-2018, entry version 174.
RecName: Full=Catalase HPII;
EC=1.11.1.6;
AltName: Full=Hydroxyperoxidase II;
Name=katE; OrderedLocusNames=b1732, JW1721;
Escherichia coli (strain K12).
Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
Enterobacteriaceae; Escherichia.
NCBI_TaxID=83333;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], AND PROTEIN SEQUENCE OF 1-10.
STRAIN=K12;
PubMed=1987146;
von Ossowski I., Mulvey M.R., Leco P.A., Borys A., Loewen P.C.;
"Nucleotide sequence of Escherichia coli katE, which encodes catalase
HPII.";
J. Bacteriol. 173:514-520(1991).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=9097039; DOI=10.1093/dnares/3.6.363;
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.;
"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.";
DNA Res. 3:363-377(1996).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / MG1655 / ATCC 47076;
PubMed=9278503; DOI=10.1126/science.277.5331.1453;
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.;
"The complete genome sequence of Escherichia coli K-12.";
Science 277:1453-1462(1997).
[4]
SEQUENCE REVISION TO 198.
PubMed=16397293; DOI=10.1093/nar/gkj405;
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.;
"Escherichia coli K-12: a cooperatively developed annotation snapshot
-- 2005.";
Nucleic Acids Res. 34:1-9(2006).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
PubMed=16738553; DOI=10.1038/msb4100049;
Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
"Highly accurate genome sequences of Escherichia coli K-12 strains
MG1655 and W3110.";
Mol. Syst. Biol. 2:E1-E5(2006).
[6]
CROSS-LINK 392-HIS--TYR-415.
PubMed=9144772; DOI=10.1002/pro.5560060507;
Bravo J., Fita I., Ferrer J.C., Ens W., Hillar A., Switala J.,
Loewen P.C.;
"Identification of a novel bond between a histidine and the essential
tyrosine in catalase HPII of Escherichia coli.";
Protein Sci. 6:1016-1023(1997).
[7]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
PubMed=7663946; DOI=10.1016/S0969-2126(01)00182-4;
Bravo J., Verdaguer N., Tormo J., Betzel C., Switala J., Loewen P.C.,
Fita I.;
"Crystal structure of catalase HPII from Escherichia coli.";
Structure 3:491-502(1995).
[8]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
PubMed=10091651; DOI=10.1110/ps.8.3.490;
Sevinc M.S., Mate M.J., Switala J., Fita I., Loewen P.C.;
"Role of the lateral channel in catalase HPII of Escherichia coli.";
Protein Sci. 8:490-498(1999).
[9]
X-RAY CRYSTALLOGRAPHY (1.89 ANGSTROMS).
PubMed=11455600; DOI=10.1002/prot.1092;
Melik-Adamyan W.R., Bravo J., Carpena X., Switala J., Mate M.J.,
Fita I., Loewen P.C.;
"Substrate flow in catalases deduced from the crystal structures of
active site variants of HPII from Escherichia coli.";
Proteins 44:270-281(2001).
-!- FUNCTION: Decomposes hydrogen peroxide into water and oxygen;
serves to protect cells from the toxic effects of hydrogen
peroxide.
-!- CATALYTIC ACTIVITY: 2 H(2)O(2) = O(2) + 2 H(2)O.
{ECO:0000255|PROSITE-ProRule:PRU10013}.
-!- COFACTOR:
Name=heme; Xref=ChEBI:CHEBI:30413;
-!- SUBUNIT: Homotetramer.
-!- INTERACTION:
Self; NbExp=2; IntAct=EBI-549879, EBI-549879;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
-!- INDUCTION: By entry into stationary phase.
-!- SIMILARITY: Belongs to the catalase family. HPII subfamily.
{ECO:0000305}.
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EMBL; M55161; AAA24039.1; -; Genomic_DNA.
EMBL; U00096; AAT48137.1; -; Genomic_DNA.
EMBL; AP009048; BAA15513.1; -; Genomic_DNA.
PIR; A39129; A39129.
RefSeq; WP_000077872.1; NZ_LN832404.1.
RefSeq; YP_025308.1; NC_000913.3.
PDB; 1CF9; X-ray; 1.80 A; A/B/C/D=1-753.
PDB; 1GG9; X-ray; 1.89 A; A/B/C/D=1-753.
PDB; 1GGE; X-ray; 1.89 A; A/B/C/D=1-753.
PDB; 1GGF; X-ray; 2.28 A; A/B/C/D=1-753.
PDB; 1GGH; X-ray; 2.15 A; A/B/C/D=1-753.
PDB; 1GGJ; X-ray; 1.92 A; A/B/C/D=1-753.
PDB; 1GGK; X-ray; 2.26 A; A/B/C/D=1-753.
PDB; 1IPH; X-ray; 2.80 A; A/B/C/D=1-753.
PDB; 1P7Y; X-ray; 2.40 A; A/B/C/D=1-753.
PDB; 1P7Z; X-ray; 2.21 A; A/B/C/D=1-753.
PDB; 1P80; X-ray; 1.65 A; A/B/C/D=1-753.
PDB; 1P81; X-ray; 1.81 A; A/B/C/D=1-753.
PDB; 1QF7; X-ray; 2.20 A; A/B/C/D=1-753.
PDB; 1QWS; X-ray; 1.90 A; A/B/C/D=1-753.
PDB; 1YE9; X-ray; 2.80 A; A/B/C/D/I/J/K/L=75-300, E/F/G/H/M/N/O/P=309-567.
PDB; 3P9P; X-ray; 1.50 A; A/B/C/D=1-753.
PDB; 3P9Q; X-ray; 1.48 A; A/B/C/D=1-753.
PDB; 3P9R; X-ray; 1.90 A; A/B/C/D=1-753.
PDB; 3P9S; X-ray; 1.90 A; A/B/C/D=1-753.
PDB; 3PQ2; X-ray; 1.79 A; A/B/C/D=1-753.
PDB; 3PQ3; X-ray; 1.79 A; A/B/C/D=1-753.
PDB; 3PQ4; X-ray; 1.79 A; A/B/C/D=1-753.
PDB; 3PQ5; X-ray; 1.80 A; A/B/C/D=1-753.
PDB; 3PQ6; X-ray; 1.80 A; A/B/C/D=1-753.
PDB; 3PQ7; X-ray; 1.80 A; A/B/C/D=1-753.
PDB; 3PQ8; X-ray; 1.80 A; A/B/C/D=1-753.
PDB; 3TTT; X-ray; 1.58 A; A/B/C/D=1-753.
PDB; 3TTU; X-ray; 1.89 A; A/B/C/D=1-753.
PDB; 3TTV; X-ray; 1.45 A; A/B/C/D=1-753.
PDB; 3TTW; X-ray; 1.62 A; A/B/C/D=1-753.
PDB; 3TTX; X-ray; 1.74 A; A/B/C/D=1-753.
PDB; 3VU3; X-ray; 2.85 A; A=1-753.
PDB; 4BFL; X-ray; 1.64 A; A/B/C/D=1-753.
PDB; 4ENP; X-ray; 1.50 A; A/B/C/D=1-753.
PDB; 4ENQ; X-ray; 1.90 A; A/B/C/D=1-753.
PDB; 4ENR; X-ray; 1.60 A; A/B/C/D=1-753.
PDB; 4ENS; X-ray; 1.60 A; A/B/C/D=1-753.
PDB; 4ENT; X-ray; 1.70 A; A/B/C/D=1-753.
PDB; 4ENU; X-ray; 1.70 A; A/B/C/D=1-753.
PDB; 4ENV; X-ray; 1.70 A; A/B/C/D=1-753.
PDB; 4ENW; X-ray; 1.90 A; A/B/C/D=1-753.
PDB; 5BV2; X-ray; 1.53 A; P/Q/R/S=1-753.
PDB; 6BY0; X-ray; 2.93 A; A/B/C/D=1-753.
PDBsum; 1CF9; -.
PDBsum; 1GG9; -.
PDBsum; 1GGE; -.
PDBsum; 1GGF; -.
PDBsum; 1GGH; -.
PDBsum; 1GGJ; -.
PDBsum; 1GGK; -.
PDBsum; 1IPH; -.
PDBsum; 1P7Y; -.
PDBsum; 1P7Z; -.
PDBsum; 1P80; -.
PDBsum; 1P81; -.
PDBsum; 1QF7; -.
PDBsum; 1QWS; -.
PDBsum; 1YE9; -.
PDBsum; 3P9P; -.
PDBsum; 3P9Q; -.
PDBsum; 3P9R; -.
PDBsum; 3P9S; -.
PDBsum; 3PQ2; -.
PDBsum; 3PQ3; -.
PDBsum; 3PQ4; -.
PDBsum; 3PQ5; -.
PDBsum; 3PQ6; -.
PDBsum; 3PQ7; -.
PDBsum; 3PQ8; -.
PDBsum; 3TTT; -.
PDBsum; 3TTU; -.
PDBsum; 3TTV; -.
PDBsum; 3TTW; -.
PDBsum; 3TTX; -.
PDBsum; 3VU3; -.
PDBsum; 4BFL; -.
PDBsum; 4ENP; -.
PDBsum; 4ENQ; -.
PDBsum; 4ENR; -.
PDBsum; 4ENS; -.
PDBsum; 4ENT; -.
PDBsum; 4ENU; -.
PDBsum; 4ENV; -.
PDBsum; 4ENW; -.
PDBsum; 5BV2; -.
PDBsum; 6BY0; -.
ProteinModelPortal; P21179; -.
SMR; P21179; -.
BioGrid; 4263059; 36.
BioGrid; 850594; 1.
DIP; DIP-10052N; -.
IntAct; P21179; 11.
STRING; 316385.ECDH10B_1870; -.
PeroxiBase; 5321; EcoKat05.
SWISS-2DPAGE; P21179; -.
EPD; P21179; -.
PaxDb; P21179; -.
PRIDE; P21179; -.
EnsemblBacteria; AAT48137; AAT48137; b1732.
EnsemblBacteria; BAA15513; BAA15513; BAA15513.
GeneID; 946234; -.
KEGG; ecj:JW1721; -.
KEGG; eco:b1732; -.
PATRIC; fig|1411691.4.peg.524; -.
EchoBASE; EB0504; -.
EcoGene; EG10509; katE.
eggNOG; ENOG4105CH6; Bacteria.
eggNOG; COG0753; LUCA.
HOGENOM; HOG000087851; -.
InParanoid; P21179; -.
KO; K03781; -.
OMA; VMWQMSD; -.
PhylomeDB; P21179; -.
BioCyc; EcoCyc:HYDROPEROXIDII-MONOMER; -.
BioCyc; MetaCyc:HYDROPEROXIDII-MONOMER; -.
SABIO-RK; P21179; -.
EvolutionaryTrace; P21179; -.
PRO; PR:P21179; -.
Proteomes; UP000000318; Chromosome.
Proteomes; UP000000625; Chromosome.
GO; GO:0005737; C:cytoplasm; IDA:EcoliWiki.
GO; GO:0005829; C:cytosol; HDA:UniProtKB.
GO; GO:0004096; F:catalase activity; IDA:EcoCyc.
GO; GO:0020037; F:heme binding; IDA:EcoliWiki.
GO; GO:0042802; F:identical protein binding; IDA:EcoCyc.
GO; GO:0005506; F:iron ion binding; IDA:EcoliWiki.
GO; GO:0006974; P:cellular response to DNA damage stimulus; IEP:EcoliWiki.
GO; GO:0042744; P:hydrogen peroxide catabolic process; IMP:EcoliWiki.
GO; GO:0006972; P:hyperosmotic response; IEP:EcoCyc.
GO; GO:0006979; P:response to oxidative stress; IMP:EcoliWiki.
Gene3D; 2.40.180.10; -; 1.
Gene3D; 3.40.50.880; -; 1.
InterPro; IPR018028; Catalase.
InterPro; IPR024708; Catalase_AS.
InterPro; IPR024712; Catalase_clade2.
InterPro; IPR011614; Catalase_core.
InterPro; IPR037060; Catalase_core_sf.
InterPro; IPR002226; Catalase_haem_BS.
InterPro; IPR010582; Catalase_immune_responsive.
InterPro; IPR020835; Catalase_sf.
InterPro; IPR029062; Class_I_gatase-like.
PANTHER; PTHR42821; PTHR42821; 1.
Pfam; PF00199; Catalase; 1.
Pfam; PF06628; Catalase-rel; 1.
PIRSF; PIRSF038927; Catalase_clade2; 1.
PRINTS; PR00067; CATALASE.
SMART; SM01060; Catalase; 1.
SUPFAM; SSF52317; SSF52317; 1.
SUPFAM; SSF56634; SSF56634; 1.
PROSITE; PS00437; CATALASE_1; 1.
PROSITE; PS00438; CATALASE_2; 1.
PROSITE; PS51402; CATALASE_3; 1.
1: Evidence at protein level;
3D-structure; Complete proteome; Cytoplasm; Direct protein sequencing;
Heme; Hydrogen peroxide; Iron; Metal-binding; Oxidoreductase;
Peroxidase; Reference proteome.
CHAIN 1 753 Catalase HPII.
/FTId=PRO_0000084971.
ACT_SITE 128 128 {ECO:0000255|PROSITE-ProRule:PRU10013}.
ACT_SITE 201 201 {ECO:0000255|PROSITE-ProRule:PRU10013}.
METAL 415 415 Iron (heme axial ligand).
CROSSLNK 392 415 3'-histidyl-3-tyrosine (His-Tyr).
HELIX 19 22 {ECO:0000244|PDB:5BV2}.
STRAND 32 34 {ECO:0000244|PDB:1QWS}.
TURN 45 47 {ECO:0000244|PDB:1GG9}.
HELIX 53 56 {ECO:0000244|PDB:3TTV}.
HELIX 63 67 {ECO:0000244|PDB:3TTV}.
HELIX 68 70 {ECO:0000244|PDB:3TTV}.
STRAND 87 89 {ECO:0000244|PDB:3TTV}.
STRAND 95 98 {ECO:0000244|PDB:3TTV}.
HELIX 108 118 {ECO:0000244|PDB:3TTV}.
STRAND 126 128 {ECO:0000244|PDB:1IPH}.
STRAND 130 142 {ECO:0000244|PDB:3TTV}.
TURN 145 147 {ECO:0000244|PDB:3TTV}.
HELIX 151 153 {ECO:0000244|PDB:3TTV}.
STRAND 160 167 {ECO:0000244|PDB:3TTV}.
STRAND 169 171 {ECO:0000244|PDB:3TTV}.
STRAND 179 181 {ECO:0000244|PDB:3TTV}.
STRAND 184 191 {ECO:0000244|PDB:3TTV}.
STRAND 194 205 {ECO:0000244|PDB:3TTV}.
HELIX 211 213 {ECO:0000244|PDB:3TTV}.
HELIX 214 221 {ECO:0000244|PDB:3TTV}.
TURN 225 227 {ECO:0000244|PDB:3TTV}.
HELIX 237 245 {ECO:0000244|PDB:3TTV}.
HELIX 247 249 {ECO:0000244|PDB:3TTV}.
HELIX 250 257 {ECO:0000244|PDB:3TTV}.
HELIX 259 261 {ECO:0000244|PDB:3TTV}.
STRAND 262 264 {ECO:0000244|PDB:3TTV}.
HELIX 266 268 {ECO:0000244|PDB:3TTV}.
STRAND 277 280 {ECO:0000244|PDB:3TTV}.
STRAND 286 295 {ECO:0000244|PDB:3TTV}.
HELIX 304 313 {ECO:0000244|PDB:3TTV}.
HELIX 317 328 {ECO:0000244|PDB:3TTV}.
STRAND 333 342 {ECO:0000244|PDB:3TTV}.
HELIX 343 345 {ECO:0000244|PDB:3TTV}.
STRAND 349 351 {ECO:0000244|PDB:3TTV}.
TURN 362 364 {ECO:0000244|PDB:3TTV}.
STRAND 368 377 {ECO:0000244|PDB:3TTV}.
HELIX 382 385 {ECO:0000244|PDB:3TTV}.
TURN 386 388 {ECO:0000244|PDB:3TTV}.
HELIX 406 423 {ECO:0000244|PDB:3TTV}.
HELIX 428 430 {ECO:0000244|PDB:3TTV}.
HELIX 432 434 {ECO:0000244|PDB:3TTV}.
STRAND 459 462 {ECO:0000244|PDB:3TTV}.
TURN 465 468 {ECO:0000244|PDB:3TTV}.
STRAND 477 479 {ECO:0000244|PDB:3TTV}.
STRAND 488 495 {ECO:0000244|PDB:3TTV}.
HELIX 499 501 {ECO:0000244|PDB:3TTV}.
HELIX 506 514 {ECO:0000244|PDB:3TTV}.
HELIX 517 532 {ECO:0000244|PDB:3TTV}.
HELIX 537 548 {ECO:0000244|PDB:3TTV}.
HELIX 552 561 {ECO:0000244|PDB:3TTV}.
HELIX 568 571 {ECO:0000244|PDB:3TTV}.
HELIX 586 588 {ECO:0000244|PDB:3TTV}.
STRAND 590 593 {ECO:0000244|PDB:3TTV}.
STRAND 602 606 {ECO:0000244|PDB:3TTV}.
STRAND 609 611 {ECO:0000244|PDB:1IPH}.
HELIX 613 625 {ECO:0000244|PDB:3TTV}.
STRAND 629 641 {ECO:0000244|PDB:3TTV}.
STRAND 647 649 {ECO:0000244|PDB:3TTV}.
TURN 654 656 {ECO:0000244|PDB:3TTV}.
HELIX 659 661 {ECO:0000244|PDB:3TTV}.
STRAND 663 667 {ECO:0000244|PDB:3TTV}.
HELIX 672 674 {ECO:0000244|PDB:3TTV}.
TURN 675 677 {ECO:0000244|PDB:3TTV}.
HELIX 679 690 {ECO:0000244|PDB:3TTV}.
STRAND 695 698 {ECO:0000244|PDB:3TTV}.
HELIX 699 708 {ECO:0000244|PDB:3TTV}.
STRAND 718 723 {ECO:0000244|PDB:3TTV}.
HELIX 726 737 {ECO:0000244|PDB:3TTV}.
HELIX 742 744 {ECO:0000244|PDB:3TTV}.
HELIX 745 748 {ECO:0000244|PDB:3TTV}.
STRAND 749 751 {ECO:0000244|PDB:1P80}.
SEQUENCE 753 AA; 84163 MW; 1F034E4866A70FB9 CRC64;
MSQHNEKNPH QHQSPLHDSS EAKPGMDSLA PEDGSHRPAA EPTPPGAQPT APGSLKAPDT
RNEKLNSLED VRKGSENYAL TTNQGVRIAD DQNSLRAGSR GPTLLEDFIL REKITHFDHE
RIPERIVHAR GSAAHGYFQP YKSLSDITKA DFLSDPNKIT PVFVRFSTVQ GGAGSADTVR
DIRGFATKFY TEEGIFDLVG NNTPIFFIQD AHKFPDFVHA VKPEPHWAIP QGQSAHDTFW
DYVSLQPETL HNVMWAMSDR GIPRSYRTME GFGIHTFRLI NAEGKATFVR FHWKPLAGKA
SLVWDEAQKL TGRDPDFHRR ELWEAIEAGD FPEYELGFQL IPEEDEFKFD FDLLDPTKLI
PEELVPVQRV GKMVLNRNPD NFFAENEQAA FHPGHIVPGL DFTNDPLLQG RLFSYTDTQI
SRLGGPNFHE IPINRPTCPY HNFQRDGMHR MGIDTNPANY EPNSINDNWP RETPPGPKRG
GFESYQERVE GNKVRERSPS FGEYYSHPRL FWLSQTPFEQ RHIVDGFSFE LSKVVRPYIR
ERVVDQLAHI DLTLAQAVAK NLGIELTDDQ LNITPPPDVN GLKKDPSLSL YAIPDGDVKG
RVVAILLNDE VRSADLLAIL KALKAKGVHA KLLYSRMGEV TADDGTVLPI AATFAGAPSL
TVDAVIVPCG NIADIADNGD ANYYLMEAYK HLKPIALAGD ARKFKATIKI ADQGEEGIVE
ADSADGSFMD ELLTLMAAHR VWSRIPKIDK IPA


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