P55305
Gene name |
catA (AN8637) |
Protein name |
Catalase A |
Names |
Spore-specific catalase |
Species |
Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139) (Aspergillus nidulans) |
KEGG Pathway |
ani:AN8637.2 |
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
1 structures for P55305
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P55305-F1 | Predicted | AlphaFoldDB |
No variants for P55305
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P55305 | |||||
No associated diseases with P55305
5 regional properties for P55305
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| binding_site | Catalase haem-binding site | 376 - 384 | IPR002226 |
| domain | Catalase immune-responsive domain | 457 - 520 | IPR010582 |
| domain | Catalase core domain | 43 - 433 | IPR011614 |
| active_site | Catalase active site | 82 - 98 | IPR024708 |
| domain | Large catalase, C-terminal domain | 556 - 695 | 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 | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| cytosol | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. |
3 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. |
| metal ion binding | Binding to a metal ion. |
6 GO annotations of biological process
| Name | Definition |
|---|---|
| cellular response to heat | 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 heat stimulus, a temperature stimulus above the optimal temperature for that organism. |
| cellular response to hydrogen peroxide | 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 hydrogen peroxide (H2O2) stimulus. |
| cellular response to iron ion starvation | 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 deprivation of iron ions. |
| hydrogen peroxide catabolic process | The chemical reactions and pathways resulting in the breakdown of hydrogen peroxide (H2O2). |
| 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. |
| sporulation resulting in formation of a cellular spore | The process in which a relatively unspecialized cell acquires the specialized features of a cellular spore, a cell form that can be used for dissemination, for survival of adverse conditions because of its heat and dessication resistance, and/or for reproduction. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MATSITAGLQ | KAQQAVQDTA | TKNKKIVDIS | HDTVNVHTDQ | EQRTDFGVAI | TDPDHWLRVT |
| 70 | 80 | 90 | 100 | 110 | 120 |
| NETHSGPSLL | EDHIARERIH | RFDHERIPER | VVHARGTGAY | GNFTLKESIE | DLTYAGVLTD |
| 130 | 140 | 150 | 160 | 170 | 180 |
| TSRNTPVFVR | FSTVQGSRGS | ADTVRDVRGF | AVKFYTDEGN | WDIVGNNIPV | FFIQDAIKFP |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DFVHAVKPEP | HNEVPQAQTA | HNNFWDFVYL | HPEATHMFMW | AMSDRAIPRS | YRMMQGFGVN |
| 250 | 260 | 270 | 280 | 290 | 300 |
| TFSLVNKEGK | RHFVKFHWIP | HLGVHSLVWD | EALKLAGQDP | DFHRKDLMEA | IDNKAYPKWD |
| 310 | 320 | 330 | 340 | 350 | 360 |
| FAIQAIPEED | QDKFEFDIFD | ATKVWPEEQV | PLRVVGELEL | NRNIDEFFPE | TEQVAFCTSH |
| 370 | 380 | 390 | 400 | 410 | 420 |
| IVPGIDFSDD | PLLQGRNFSY | QDTQISRLGV | NWEEIPINRP | VCPFLNHNRD | GAKRHRITKG |
| 430 | 440 | 450 | 460 | 470 | 480 |
| TVNYWPNRFE | ANPPASDKGF | KSHPAPITGR | KRRDLTPKFK | EYHNQAQLFY | NSLSEVEKVH |
| 490 | 500 | 510 | 520 | 530 | 540 |
| VKKAFSFELD | HCDDPIVYER | LAGQRLAEID | LPLAQAVAEM | VGAPIPTKAL | RDNHGKTSVR |
| 550 | 560 | 570 | 580 | 590 | 600 |
| LSQFDFTPKA | PGIISRRIAI | IIGDGYDKIA | FNGMKAAILA | AQALPFVIGT | KRSAIYAQGE |
| 610 | 620 | 630 | 640 | 650 | 660 |
| DKNSSKGVIP | DHMYDGMRST | MFDATFIPGG | SHIETLQKNG | QIRYWIAETF | GHLKALGAMG |
| 670 | 680 | 690 | 700 | 710 | 720 |
| EAAQLVKEVL | GNVMGVQIAG | ADSAEPVEWY | GVVTARGPES | AESLSEGFKV | LKDAGDFTSK |
| 730 | 740 | ||||
| FFYQISQHRN | WQRELDGLAS | TVAF |