A6TGM5
Gene name |
pepQ |
Protein name |
Xaa-Pro dipeptidase |
Names |
X-Pro dipeptidase, Imidodipeptidase, Proline dipeptidase, Prolidase |
Species |
Klebsiella pneumoniae subsp pneumoniae (strain ATCC 700721 / MGH 78578) |
KEGG Pathway |
kpn:KPN_04341 |
EC number |
3.4.13.9: Dipeptidases |
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 A6TGM5
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A6TGM5-F1 | Predicted | AlphaFoldDB |
No variants for A6TGM5
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A6TGM5 | |||||
No associated diseases with A6TGM5
3 regional properties for A6TGM5
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | ArgE/DapE/ACY1/CPG2/YscS, conserved site | 76 - 85 | IPR001261-1 |
| conserved_site | ArgE/DapE/ACY1/CPG2/YscS, conserved site | 140 - 179 | IPR001261-2 |
| domain | Peptidase M20, dimerisation domain | 209 - 306 | IPR011650 |
Functions
| Description | ||
|---|---|---|
| EC Number | 3.4.13.9 | Dipeptidases |
| 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 |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| metal ion binding | Binding to a metal ion. |
| metalloexopeptidase activity | Catalysis of the hydrolysis of a peptide bond not more than three residues from the N- or C-terminus of a polypeptide chain by a mechanism in which water acts as a nucleophile, one or two metal ions hold the water molecule in place, and charged amino acid side chains are ligands for the metal ions. |
| phosphoric triester hydrolase activity | Catalysis of the hydrolysis of a phosphoric triester. |
| proline dipeptidase activity | Catalysis of the reaction: H2O + a dipeptide with proline at the C-terminal <=> L-proline + a standard alpha amino acid. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| proteolysis | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MESLAALYKN | HIVTLQERTR | DVLARFQMDA | LLIHSGELVN | VFLDDHPYPF | KVNPQFKAWV |
| 70 | 80 | 90 | 100 | 110 | 120 |
| PVTQVPNCWL | LVDGVNKPKL | WFYLPVDYWH | NVEPLPTSFW | TEEIDVIALP | KADGIGSQLP |
| 130 | 140 | 150 | 160 | 170 | 180 |
| AARGNIGYIG | PVPERALGLG | IAADKINPKG | VIDYLHYYRA | YKTDYELACM | REAQKSAVNG |
| 190 | 200 | 210 | 220 | 230 | 240 |
| HRAAYEAFQS | GMSEFDINQA | YLTATGHRDT | DVPYSNIVAL | NEHASVLHYT | KLDHRAPAEM |
| 250 | 260 | 270 | 280 | 290 | 300 |
| RSFLLDAGAE | YNGYAADLTR | TWAAHGDNDF | AHLIKDVNDE | QLALISTMKA | GTSYIDYHIQ |
| 310 | 320 | 330 | 340 | 350 | 360 |
| FHQRIAKLLR | KHQLVTDMSE | EAMVENDLTG | PFMPHGIGHP | LGLQVHDVAG | FMQDDTGTHL |
| 370 | 380 | 390 | 400 | 410 | 420 |
| AAPSKYPYLR | CTRIIEPRMV | LTIEPGIYFI | ESLLAPWREG | PFSKHFNWQK | IDAMKPFGGI |
| 430 | 440 | ||||
| RIEDNVVIHE | NSIENMTRDL | KLA |