Q7SID3
Gene name |
|
Protein name |
Cobalt-containing nitrile hydratase subunit beta |
Names |
L-NHase, L-nitrilase |
Species |
Pseudonocardia thermophila |
KEGG Pathway |
|
EC number |
4.2.1.84: Hydro-lyases |
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
15 structures for Q7SID3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| 1IRE | X-ray | 180 A | B | 1-228 | PDB |
| 1UGP | X-ray | 163 A | B | 1-226 | PDB |
| 1UGQ | X-ray | 200 A | B | 1-228 | PDB |
| 1UGR | X-ray | 180 A | B | 1-228 | PDB |
| 1UGS | X-ray | 200 A | B | 1-228 | PDB |
| 3VYH | X-ray | 163 A | B | 1-233 | PDB |
| 4OB0 | X-ray | 120 A | B | 1-233 | PDB |
| 4OB1 | X-ray | 163 A | B | 1-233 | PDB |
| 4OB2 | X-ray | 152 A | B | 1-233 | PDB |
| 4OB3 | X-ray | 192 A | B | 1-233 | PDB |
| 7SJZ | X-ray | 185 A | B | 1-233 | PDB |
| 7W8L | X-ray | 230 A | B | 1-233 | PDB |
| 7W8M | X-ray | 260 A | B | 1-233 | PDB |
| 8I6N | X-ray | 220 A | B | 1-233 | PDB |
| AF-Q7SID3-F1 | Predicted | AlphaFoldDB |
No variants for Q7SID3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q7SID3 | |||||
No associated diseases with Q7SID3
1 regional properties for Q7SID3
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Nitrile hydratase beta subunit domain | 1 - 224 | IPR024690 |
Functions
| Description | ||
|---|---|---|
| EC Number | 4.2.1.84 | Hydro-lyases |
| 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 |
|---|---|
| indole-3-acetonitrile nitrile hydratase activity | Catalysis of the reaction: indole-3-acetonitrile + H2O = indole-3-acetamide. |
| nitrile hydratase activity | Catalysis of the reaction: an aliphatic amide = a nitrile + H2O. |
| transition metal ion binding | Binding to a transition metal ions; a transition metal is an element whose atom has an incomplete d-subshell of extranuclear electrons, or which gives rise to a cation or cations with an incomplete d-subshell. Transition metals often have more than one valency state. Biologically relevant transition metals include vanadium, manganese, iron, copper, cobalt, nickel, molybdenum and silver. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| nitrile catabolic process | The chemical reactions and pathways resulting in the breakdown of a nitrile, an organic compound containing trivalent nitrogen attached to one carbon atom. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MNGVYDVGGT | DGLGPINRPA | DEPVFRAEWE | KVAFAMFPAT | FRAGFMGLDE | FRFGIEQMNP |
| 70 | 80 | 90 | 100 | 110 | 120 |
| AEYLESPYYW | HWIRTYIHHG | VRTGKIDLEE | LERRTQYYRE | NPDAPLPEHE | QKPELIEFVN |
| 130 | 140 | 150 | 160 | 170 | 180 |
| QAVYGGLPAS | REVDRPPKFK | EGDVVRFSTA | SPKGHARRAR | YVRGKTGTVV | KHHGAYIYPD |
| 190 | 200 | 210 | 220 | 230 | |
| TAGNGLGECP | EHLYTVRFTA | QELWGPEGDP | NSSVYYDCWE | PYIELVDTKA | AAA |