A0KEL3
Gene name |
pepQ |
Protein name |
Xaa-Pro dipeptidase |
Names |
X-Pro dipeptidase, Imidodipeptidase, Proline dipeptidase, Prolidase |
Species |
Aeromonas hydrophila subsp. hydrophila (strain ATCC 7966 / DSM 30187 / BCRC 13018 / CCUG 14551 / JCM 1027 / KCTC 2358 / NCIMB 9240 / NCTC 8049) |
KEGG Pathway |
aha:AHA_0141 |
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 A0KEL3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A0KEL3-F1 | Predicted | AlphaFoldDB |
No variants for A0KEL3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A0KEL3 | |||||
No associated diseases with A0KEL3
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 |
| MSSYSQLFAQ | HLDTLQQRTR | DILQQQGLSG | LAIHSGQTHR | IFLDDQDYPF | KVNPQFKAWL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| PVLDNPHCWL | LVDGVNKPVL | LFYRPVDFWH | KVAELPNAFW | VDFFDIRFLT | RPEQVADHLP |
| 130 | 140 | 150 | 160 | 170 | 180 |
| ANKQEWAYLG | GHLEVAELLG | LGQPNPEAVL | NYLHYHRAYK | TAYELECLRD | ANRIGVRGHI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AAKDSFMAGA | SEFEINLAYM | KAVGQGANEA | PYGNIVAINR | NAAILHYTHL | SAQRVPDAER |
| 250 | 260 | 270 | 280 | 290 | 300 |
| YSFLIDAGVD | VHGYASDITR | TWAWRRGEFA | DLIAALDAQQ | QEIIEEIKPG | RRYSELHLQM |
| 310 | 320 | 330 | 340 | 350 | 360 |
| HHRLARLLQA | TELVDMSVDE | MIHTGVTNVF | FPHGLGHFLG | LQVHDAGGFM | QDERGTHLSA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| PEQFPYLRCT | RVMEVGQVFT | IEPGLYFIDS | LLEPLRLGEQ | GKRVNWNKVE | ALRPYGGIRI |
| 430 | |||||
| EDNVVLHANG | VENLTRQAGL |