Q52438
Gene name |
bphA1 |
Protein name |
Biphenyl dioxygenase subunit alpha |
Names |
Biphenyl 2,3-dioxygenase |
Species |
Pseudomonas sp (strain KKS102) |
KEGG Pathway |
|
EC number |
1.14.12.18: With NADH or NADPH as one donor, and incorporation of two atoms of oxygen into one donor |
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 Q52438
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q52438-F1 | Predicted | AlphaFoldDB |
No variants for Q52438
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q52438 | |||||
No associated diseases with Q52438
4 regional properties for Q52438
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Aromatic-ring-hydroxylating dioxygenase, alpha subunit, C-terminal domain | 185 - 450 | IPR015879 |
| binding_site | Aromatic-ring-hydroxylating dioxygenase, 2Fe-2S-binding site | 101 - 124 | IPR015881 |
| domain | Rieske [2Fe-2S] iron-sulphur domain | 58 - 142 | IPR017941 |
| domain | Ring-hydroxylating dioxygenase, alpha subunit NdoB-like, C-terminal | 205 - 449 | IPR043266 |
Functions
| Description | ||
|---|---|---|
| EC Number | 1.14.12.18 | With NADH or NADPH as one donor, and incorporation of two atoms of oxygen into one donor |
| 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 |
|---|---|
| 2 iron, 2 sulfur cluster binding | Binding to a 2 iron, 2 sulfur (2Fe-2S) cluster; this cluster consists of two iron atoms, with two inorganic sulfur atoms found between the irons and acting as bridging ligands. |
| biphenyl 2,3-dioxygenase activity | Catalysis of the reaction: biphenyl + NADH + H+ + O2 = (2R,3S)-3-phenylcyclohexa-3,5-diene-1,2-diol + NAD+. This reaction requires Fe2+. |
| iron ion binding | Binding to an iron (Fe) ion. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| aromatic compound catabolic process | The chemical reactions and pathways resulting in the breakdown of aromatic compounds, any substance containing an aromatic carbon ring. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MGIYSEREVQ | AVPMTFKRRW | TDEAIRALVD | QDKGLIDPRI | YADQDLYEIE | LERIFARSWL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LLGHEAHIPK | TGDYLTTYMG | EDPVIMVRQK | DGSIKVFLNQ | CRHRGMRICR | SDAGNAKAFT |
| 130 | 140 | 150 | 160 | 170 | 180 |
| CTYHGWAYDI | AGNLVNVPYE | KEAFCDKKEG | DCGFDKADWG | PLQARVETYK | GLIFANWDAE |
| 190 | 200 | 210 | 220 | 230 | 240 |
| APDLKTYLSD | AMPYMDVMLD | RTEAGTTVVG | GMQKWVIPCN | WKFAAEQFCS | DMYHAGTMAH |
| 250 | 260 | 270 | 280 | 290 | 300 |
| LSGVLSSLPP | EMDLTQVQMS | KNGSQFRAAW | GGHGSGWFIN | DAAILMAVMG | PKITQYWTQG |
| 310 | 320 | 330 | 340 | 350 | 360 |
| PAAEKAAKRL | NQMPTQTMFG | QHMTVFPTCS | FLPGINTIRS | WHPRGPNEVE | CGPSWSSMPM |
| 370 | 380 | 390 | 400 | 410 | 420 |
| RPEDIKEEFR | RQNIRTFNAG | GTFEQDDGEN | WVEIQRGLRG | HKAKSAPLCA | QMGLNVPNKS |
| 430 | 440 | 450 | |||
| NPDFPGKTAY | VYAEEAARGM | YHHWARMMSE | PNWETLKP |