P0A327
Gene name |
katA (BruAb2_0827) |
Protein name |
Catalase |
Names |
|
Species |
Brucella abortus biovar 1 (strain 9-941) |
KEGG Pathway |
bmb:BruAb2_0827 |
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 P0A327
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P0A327-F1 | Predicted | AlphaFoldDB |
No variants for P0A327
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P0A327 | |||||
No associated diseases with P0A327
5 regional properties for P0A327
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Aminoacyl-tRNA synthetase, class II (D/K/N) | 162 - 501 | IPR004364 |
| domain | OB-fold nucleic acid binding domain, AA-tRNA synthetase-type | 68 - 146 | IPR004365 |
| domain | Aminoacyl-tRNA synthetase, class II | 184 - 503 | IPR006195 |
| domain | Lysyl-tRNA synthetase, class II, C-terminal | 177 - 503 | IPR018149 |
| domain | Lysine-tRNA ligase, class II, N-terminal | 67 - 174 | IPR044136 |
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 |
|---|---|
| periplasmic space | The region between the inner (cytoplasmic) and outer membrane (Gram-negative Bacteria) or cytoplasmic membrane and cell wall (Fungi and Gram-positive Bacteria). |
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 |
| MTDRPIMTTS | AGAPIPDNQN | SLTAGERGPI | LMQDYQLIEK | LSHQNRERIP | ERAVHAKGWG |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AYGTLTITGD | ISRYTKAKVL | QPGAQTPMLA | RFSTVAGELG | AADAERDVRG | FALKFYTQEG |
| 130 | 140 | 150 | 160 | 170 | 180 |
| NWDLVGNNTP | VFFVRDPLKF | PDFIHTQKRH | PRTHLRSATA | MWDFWSLSPE | SLHQVTILMS |
| 190 | 200 | 210 | 220 | 230 | 240 |
| DRGLPTDVRH | INGYGSHTYS | FWNDAGERYW | VKFHFKTMQG | HKHWTNAEAE | QVIGRTREST |
| 250 | 260 | 270 | 280 | 290 | 300 |
| QEDLFSAIEN | GEFPKWKVQV | QIMPELDADK | TPYNPFDLTK | VWPHADYPPI | DIGVMELNRN |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PENYFTEVEN | AAFSPSNIVP | GIGFSPDKML | QARIFSYADA | HRHRLGTHYE | SIPVNQPKCP |
| 370 | 380 | 390 | 400 | 410 | 420 |
| VHHYHRDGQM | NVYGGIKTGN | PDAYYEPNSF | NGPVEQPSAK | EPPLCISGNA | DRYNHRIGND |
| 430 | 440 | 450 | 460 | 470 | 480 |
| DYSQPRALFN | LFDAAQKQRL | FSNIAAAMKG | VPGFIVERQL | GHFKLIHPEY | EAGVRKALKD |
| 490 | |||||
| AHGYDANTIA | LNEKITAAE |