Q55DH8
Gene name |
catB (DDB_G0269108) |
Protein name |
Catalase-B |
Names |
|
Species |
Dictyostelium discoideum (Slime mold) |
KEGG Pathway |
ddi:DDB_G0269108 |
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 Q55DH8
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q55DH8-F1 | Predicted | AlphaFoldDB |
No variants for Q55DH8
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q55DH8 | |||||
No associated diseases with Q55DH8
5 regional properties for Q55DH8
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| binding_site | Catalase haem-binding site | 352 - 360 | IPR002226 |
| domain | Catalase immune-responsive domain | 439 - 504 | IPR010582 |
| domain | Catalase core domain | 22 - 410 | IPR011614 |
| active_site | Catalase active site | 58 - 74 | IPR024708 |
| domain | Large catalase, C-terminal domain | 539 - 683 | 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. |
4 GO annotations of biological process
| Name | Definition |
|---|---|
| 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. |
| response to reactive oxygen species | 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 a reactive oxygen species stimulus. Reactive oxygen species include singlet oxygen, superoxide, and oxygen free radicals. |
| sorocarp development | The process whose specific outcome is the progression of the sorocarp over time, from its formation to the mature structure. The process begins with the aggregation of individual cells and ends with the mature sorocarp. The sorocarp is a structure containing a spore-bearing sorus that sits on top of a stalk. An example of this process is found in Dictyostelium discoideum. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MNKKLEQLEK | FKTNDKNPVY | STTNTGVSLS | DDANSLKAGP | RGPTLLEDFV | LREKITHFDH |
| 70 | 80 | 90 | 100 | 110 | 120 |
| ERIPERIVHA | RGTGAHGYFL | SYKDHSKLTK | ADFLSKQDKK | TPVFIRISTV | QGPRGSADTV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| RDVHGFAVKF | YTDEGNYDLV | GNNMPVFFIQ | DASSFPDFVH | AVKMEPQNEM | PTGGSAHDTF |
| 190 | 200 | 210 | 220 | 230 | 240 |
| YDFCGLKPES | AHSVLWVMSD | RGIPISLRHQ | QGFGVHSYRF | INQEGKSTFV | KLHWKPLSGT |
| 250 | 260 | 270 | 280 | 290 | 300 |
| CSLLWDEAQK | IAGKDCDYHR | RRFWEDIESG | DFPQWELGAQ | LLDEDLQKKF | DFDILDPTKL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| IPEELTPVIP | LGRMVIDRNP | DNFFAETEQV | AFCVSHVVPG | IDFSNDPLLQ | GRIFSYLDTQ |
| 370 | 380 | 390 | 400 | 410 | 420 |
| LSRLGGPNFN | EIPINRPVCP | FANNQRDGIH | RMTINKGGAS | YFPNSIDKGY | PLLKEPSANK |
| 430 | 440 | 450 | 460 | 470 | 480 |
| GGFRPYPENI | SGTKSYDRSE | TFEDHFSQAT | MFWNSMSQHE | KNHIIAAYTF | EISKCSRPEV |
| 490 | 500 | 510 | 520 | 530 | 540 |
| RTRYVNNILV | NIDSVLAEKV | AKNLGVKIEP | TSTKPIKKIM | VKPSPALSQP | NLLSGDIVSR |
| 550 | 560 | 570 | 580 | 590 | 600 |
| RISVIIEKGV | DYDDVINFKD | DMEKRGAMVM | LVSSTLAQVE | CSGGEMLSPK | GTIIGNPSIF |
| 610 | 620 | 630 | 640 | 650 | 660 |
| FDAVYVPKST | EEATKILSDD | GNFLHYILEA | FKHLKTIAFG | GSVSVIKELL | RLPQDHGLLL |
| 670 | 680 | 690 | |||
| GNGYKDITEQ | FFYSLAHHRV | WERESKVSKI | PA |