P21179
Gene name |
katE (b1732, JW1721) |
Protein name |
Catalase HPII |
Names |
Hydroxyperoxidase II |
Species |
Escherichia coli (strain K12) |
KEGG Pathway |
eco:b1732 |
EC number |
1.11.1.6: Peroxidases |
Protein Class |
|
Descriptions
The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.
Autoinhibitory domains (AIDs)
Target domain |
|
Relief mechanism |
|
Assay |
cis-regPred |
Accessory elements
No accessory elements
Autoinhibited structure
Activated structure
47 structures for P21179
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1CF9 | X-ray | 180 A | A/B/C/D | 1-753 | PDB |
| 1GG9 | X-ray | 189 A | A/B/C/D | 1-753 | PDB |
| 1GGE | X-ray | 189 A | A/B/C/D | 1-753 | PDB |
| 1GGF | X-ray | 228 A | A/B/C/D | 1-753 | PDB |
| 1GGH | X-ray | 215 A | A/B/C/D | 1-753 | PDB |
| 1GGJ | X-ray | 192 A | A/B/C/D | 1-753 | PDB |
| 1GGK | X-ray | 226 A | A/B/C/D | 1-753 | PDB |
| 1IPH | X-ray | 280 A | A/B/C/D | 1-753 | PDB |
| 1P7Y | X-ray | 240 A | A/B/C/D | 1-753 | PDB |
| 1P7Z | X-ray | 221 A | A/B/C/D | 1-753 | PDB |
| 1P80 | X-ray | 165 A | A/B/C/D | 1-753 | PDB |
| 1P81 | X-ray | 181 A | A/B/C/D | 1-753 | PDB |
| 1QF7 | X-ray | 220 A | A/B/C/D | 1-753 | PDB |
| 1QWS | X-ray | 190 A | A/B/C/D | 1-753 | PDB |
| 1YE9 | X-ray | 280 A | PDB | ||
| 3P9P | X-ray | 150 A | A/B/C/D | 1-753 | PDB |
| 3P9Q | X-ray | 148 A | A/B/C/D | 1-753 | PDB |
| 3P9R | X-ray | 190 A | A/B/C/D | 1-753 | PDB |
| 3P9S | X-ray | 190 A | A/B/C/D | 1-753 | PDB |
| 3PQ2 | X-ray | 179 A | A/B/C/D | 1-753 | PDB |
| 3PQ3 | X-ray | 179 A | A/B/C/D | 1-753 | PDB |
| 3PQ4 | X-ray | 179 A | A/B/C/D | 1-753 | PDB |
| 3PQ5 | X-ray | 180 A | A/B/C/D | 1-753 | PDB |
| 3PQ6 | X-ray | 180 A | A/B/C/D | 1-753 | PDB |
| 3PQ7 | X-ray | 180 A | A/B/C/D | 1-753 | PDB |
| 3PQ8 | X-ray | 180 A | A/B/C/D | 1-753 | PDB |
| 3TTT | X-ray | 158 A | A/B/C/D | 1-753 | PDB |
| 3TTU | X-ray | 189 A | A/B/C/D | 1-753 | PDB |
| 3TTV | X-ray | 145 A | A/B/C/D | 1-753 | PDB |
| 3TTW | X-ray | 162 A | A/B/C/D | 1-753 | PDB |
| 3TTX | X-ray | 174 A | A/B/C/D | 1-753 | PDB |
| 3VU3 | X-ray | 285 A | A | 1-753 | PDB |
| 4BFL | X-ray | 164 A | A/B/C/D | 1-753 | PDB |
| 4ENP | X-ray | 150 A | A/B/C/D | 1-753 | PDB |
| 4ENQ | X-ray | 190 A | A/B/C/D | 1-753 | PDB |
| 4ENR | X-ray | 160 A | A/B/C/D | 1-753 | PDB |
| 4ENS | X-ray | 160 A | A/B/C/D | 1-753 | PDB |
| 4ENT | X-ray | 170 A | A/B/C/D | 1-753 | PDB |
| 4ENU | X-ray | 170 A | A/B/C/D | 1-753 | PDB |
| 4ENV | X-ray | 170 A | A/B/C/D | 1-753 | PDB |
| 4ENW | X-ray | 190 A | A/B/C/D | 1-753 | PDB |
| 5BV2 | X-ray | 153 A | P/Q/R/S | 1-753 | PDB |
| 6BY0 | X-ray | 293 A | A/B/C/D | 1-753 | PDB |
| 6ZTV | X-ray | 178 A | A/B/C/D | 1-753 | PDB |
| 6ZTW | X-ray | 184 A | A/B/C/D/E/F/G/H | 1-753 | PDB |
| 6ZTX | X-ray | 130 A | A/B/C/D | 1-753 | PDB |
| AF-P21179-F1 | Predicted | AlphaFoldDB |
No variants for P21179
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P21179 | |||||
No associated diseases with P21179
5 regional properties for P21179
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| binding_site | Catalase haem-binding site | 411 - 419 | IPR002226 |
| domain | Catalase immune-responsive domain | 499 - 562 | IPR010582 |
| domain | Catalase core domain | 81 - 469 | IPR011614 |
| active_site | Catalase active site | 117 - 133 | IPR024708 |
| domain | Large catalase, C-terminal domain | 599 - 746 | IPR041399 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.11.1.6 | Peroxidases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| catalase activity | Catalysis of the reaction: 2 hydrogen peroxide = O2 + 2 H2O. |
| heme binding | Binding to a heme, a compound composed of iron complexed in a porphyrin (tetrapyrrole) ring. |
| identical protein binding | Binding to an identical protein or proteins. |
| iron ion binding | Binding to an iron (Fe) ion. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| cellular response to DNA damage stimulus | Any process that results in a change in state or activity of a cell (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of a stimulus indicating damage to its DNA from environmental insults or errors during metabolism. |
| hydrogen peroxide catabolic process | The chemical reactions and pathways resulting in the breakdown of hydrogen peroxide (H2O2). |
| hyperosmotic response | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of detection of, or exposure to, a hyperosmotic environment, i.e. an environment with a higher concentration of solutes than the organism or cell. |
| response to oxidative stress | Any process that results in a change in state or activity of a cell or an organism (in terms of movement, secretion, enzyme production, gene expression, etc.) as a result of oxidative stress, a state often resulting from exposure to high levels of reactive oxygen species, e.g. superoxide anions, hydrogen peroxide (H2O2), and hydroxyl radicals. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 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 |