Q87I38
Gene name |
katG2 |
Protein name |
Catalase-peroxidase 2 |
Names |
CP 2, Peroxidase/catalase 2 |
Species |
Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633) |
KEGG Pathway |
vpa:VPA0768 |
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 Q87I38
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q87I38-F1 | Predicted | AlphaFoldDB |
No variants for Q87I38
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q87I38 | |||||
No associated diseases with Q87I38
5 regional properties for Q87I38
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Aminoacyl-tRNA synthetase, class II (D/K/N) | 155 - 492 | IPR004364 |
| domain | OB-fold nucleic acid binding domain, AA-tRNA synthetase-type | 63 - 138 | IPR004365 |
| domain | Aminoacyl-tRNA synthetase, class II | 176 - 491 | IPR006195 |
| domain | Lysyl-tRNA synthetase, class II, C-terminal | 169 - 494 | IPR018149 |
| domain | Lysine-tRNA ligase, class II, N-terminal | 63 - 165 | IPR044136 |
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 |
| MSNTNGGSVG | KCPVMHGGQT | STDKSVMDWW | PNALNLDILH | QHDSKTNPFG | PDFNYKEELK |
| 70 | 80 | 90 | 100 | 110 | 120 |
| KLDVDALKQD | LKDLMTNSQV | WWPADWGHYG | GLMIRMAWHA | AGSYRIADGR | GGAATGNQRF |
| 130 | 140 | 150 | 160 | 170 | 180 |
| APLNSWPDNA | NLDKARRLLW | PIKRKYGNKL | SWADLIILAG | NMAYESMGFK | TFGFGFGRED |
| 190 | 200 | 210 | 220 | 230 | 240 |
| IWHPEKDTYW | GSEQEWLAPS | GAKNSRYSGE | RDLENPLAAV | MMGLIYVNPE | GVDGNPDPLK |
| 250 | 260 | 270 | 280 | 290 | 300 |
| TAQDMRVTFA | RMAMNDEETV | ALTAGGHTVG | KCHGNGDAAN | LGPDPEGADV | HEQGLGWMNH |
| 310 | 320 | 330 | 340 | 350 | 360 |
| KTRGIGRDTV | TSGLEGAWTT | HPTQWDNGYF | YLLFKYDWEL | KKSPAGAWQW | EPIDIEEQDK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| PVDVEDGSKR | YNPIMTDADM | ALKMDPEYRK | ISERFQQDPA | YFEDMFARAW | FKLTHRDMGP |
| 430 | 440 | 450 | 460 | 470 | 480 |
| KSCYLGPDVP | SEDLIWQDPT | PAGKTDYNVD | LVKGKIEASG | LSIADLVATA | WDSARTYRGS |
| 490 | 500 | 510 | 520 | 530 | 540 |
| DRRGGANGAR | IRLAPQKDWQ | GNEPERLSRV | LAVLESIAAE | EGCSVADAIV | LAGNVGIELA |
| 550 | 560 | 570 | 580 | 590 | 600 |
| ARAAGHDVSV | PFAPGRGDAS | QDMTDVESFE | VLEPVADGFR | NWLKKDYVVK | PEELLLDRAQ |
| 610 | 620 | 630 | 640 | 650 | 660 |
| LMGLTAPEMT | VLIGGLRVLG | SNYGGSKDGV | FTDRVGTLSN | DFFVNLTDMA | YTWKPAGENQ |
| 670 | 680 | 690 | 700 | 710 | 720 |
| YEIRDRKTDQ | VKWTATRVDL | VFGSNSILRS | YAEVYAQDDN | QEKFIHDFVA | AWTKVMNADR |
| FDLQ |