A1TZH9
Gene name |
katG |
Protein name |
Catalase-peroxidase |
Names |
CP, Peroxidase/catalase |
Species |
Marinobacter nauticus (strain ATCC 700491 / DSM 11845 / VT8) (Marinobacter aquaeolei) |
KEGG Pathway |
maq:Maqu_1056 |
EC number |
1.11.1.21: 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 A1TZH9
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A1TZH9-F1 | Predicted | AlphaFoldDB |
No variants for A1TZH9
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A1TZH9 | |||||
No associated diseases with A1TZH9
4 regional properties for A1TZH9
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Haem peroxidase | 87 - 439 | IPR002016-1 |
| domain | Haem peroxidase | 410 - 718 | IPR002016-2 |
| binding_site | Peroxidases heam-ligand binding site | 267 - 277 | IPR019793 |
| active_site | Peroxidase, active site | 106 - 117 | IPR019794 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.11.1.21 | Peroxidases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
No GO annotations of cellular component
| Name | Definition |
|---|---|
| No GO annotations for cellular component |
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. |
2 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. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSETNSGGKC | PVMHGANSTE | NRDVMNWWPE | ALNLDILHQH | DHKTNPMGED | FDYREEVKKL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| DFEAVKKDLH | ALMTDSQDWW | PADWGHYGGL | MIRMSWHAAG | TYRIQDGRGG | GGTGNQRFAP |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LNSWPDNVSL | DKARRLLWPI | KKKYGNKLSW | ADLIILAGTV | AYESMGLPSY | GFSFGREDIW |
| 190 | 200 | 210 | 220 | 230 | 240 |
| HPEKDIYWGN | EKEWLAPSDE | RYGDVEKPDT | MENPLAAVQM | GLIYVNPEGV | NSQPDPIKTG |
| 250 | 260 | 270 | 280 | 290 | 300 |
| EQVRVTFARM | AMDDEETAAL | TAGGHTVGKC | HGNGDAGALG | PEPEAADVEE | QGFGWSNPNM |
| 310 | 320 | 330 | 340 | 350 | 360 |
| KGKAANAVTS | GIEGAWTTHP | TKFDMGYFDL | LFGYEWELKK | SPAGAWQWEP | INMKEEDKPL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| DASDPSKRHN | PIMTDADMAM | KMDPKYRAIC | EKFMADPEYF | KDCFARAWFK | LTHRDLGPKA |
| 430 | 440 | 450 | 460 | 470 | 480 |
| RYIGPEAPAE | DLIWQDPVPA | GSTDYCEEVV | KEKVADSGLS | ISEMVSTAWD | SARTFRGSDM |
| 490 | 500 | 510 | 520 | 530 | 540 |
| RGGANGARIR | LAPQKDWEGN | EPARLSKVLK | VYEQISAETG | ASVADVIVLA | GSVGIEKAAK |
| 550 | 560 | 570 | 580 | 590 | 600 |
| AAGYEVRVPF | LKGRGDATDE | MTDAPSFEYL | EPVADGFRNW | QKKDYIVKPE | ELLLDRAQLM |
| 610 | 620 | 630 | 640 | 650 | 660 |
| GLTAPEMTVL | IGGMRVLGTN | HGGTKYGVFT | DREGQLTNDF | FVNLTDMAYS | WKPVGNGTYE |
| 670 | 680 | 690 | 700 | 710 | 720 |
| IRDRKTDQTK | WTASRVDLVF | GSNSILRSYA | EVYAQDDNGE | KFVKDFIAAW | TKVMNNDRFD |
| VQA |