Q87DG7
Gene name |
cysNC (PD_0718) |
Protein name |
Bifunctional enzyme CysN/CysC |
Names |
|
Species |
Xylella fastidiosa (strain Temecula1 / ATCC 700964) |
KEGG Pathway |
xft:PD_0718 |
EC number |
2.7.1.25: Phosphotransferases with an alcohol group as acceptor |
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 Q87DG7
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q87DG7-F1 | Predicted | AlphaFoldDB |
No variants for Q87DG7
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q87DG7 | |||||
No associated diseases with Q87DG7
5 regional properties for Q87DG7
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Translational (tr)-type GTP-binding domain | 14 - 228 | IPR000795 |
| conserved_site | Tr-type G domain, conserved site | 72 - 87 | IPR031157 |
| domain | Sulfate adenylyltransferase subunit CysN, GTP-binding domain | 18 - 227 | IPR041757 |
| domain | Sulfate adenylyltransferase subunit CysN, Domain II | 236 - 314 | IPR044138 |
| domain | Sulfate adenylyltransferase subunit CysN, Domain III | 320 - 420 | IPR044139 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.7.1.25 | Phosphotransferases with an alcohol group as acceptor |
| 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 |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| adenylylsulfate kinase activity | Catalysis of the reaction: ATP + adenylylsulfate = ADP + 3'-phosphoadenosine 5'-phosphosulfate. |
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| GTP binding | Binding to GTP, guanosine triphosphate. |
| GTPase activity | Catalysis of the reaction: GTP + H2O = GDP + H+ + phosphate. |
| sulfate adenylyltransferase (ATP) activity | Catalysis of the reaction: ATP + sulfate = diphosphate + adenylylsulfate. |
3 GO annotations of biological process
| Name | Definition |
|---|---|
| hydrogen sulfide biosynthetic process | The chemical reactions and pathways resulting in the formation of hydrogen sulfide, H2S. |
| phosphorylation | The process of introducing a phosphate group into a molecule, usually with the formation of a phosphoric ester, a phosphoric anhydride or a phosphoric amide. |
| sulfate assimilation | The pathways by which inorganic sulfate is processed and incorporated into sulfated compounds. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MQSVIAYLKQ | QEIKPLLRFI | TCGSVDDGKS | TLIGHLLYDS | QCLAEDQLAD | LTVDSQRYGT |
| 70 | 80 | 90 | 100 | 110 | 120 |
| QGEHIDYALL | LDGLAAEREQ | GITIDVAYRY | FDTEKRKFIV | ADCPGHAQYT | RNMATGASSA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DAAVVLVDAR | KGLLTQTRRH | SYIVALLGIR | HVVLAVNKMD | LVGYDQQTFE | AIASDYLALA |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AKLGINQVQC | IPLSALEGDN | LCKRSARMLW | YVGPSLLEYL | EALEPADVDL | AAAMCLPVQW |
| 250 | 260 | 270 | 280 | 290 | 300 |
| VNRPDSQFRG | FTGTLAAGRV | RSGDGVVVLP | SGCVSRVVRV | FNGDTEVHEA | VAGQAVTLTL |
| 310 | 320 | 330 | 340 | 350 | 360 |
| ADEIDISRGD | VIAATDDPPE | VADQVTAYVL | WMDDTALLPG | RRYWLKLGAR | MVAASVSDIK |
| 370 | 380 | 390 | 400 | 410 | 420 |
| HRVDVNTQEQ | RVAQRLQLNE | LGYCQLSLDA | PVAFVPYARN | RVLGSFILID | RQSNATVGAG |
| 430 | 440 | 450 | 460 | 470 | 480 |
| TLDSGVHCAS | NVHWQPLDID | HVARARIKGQ | TPKVLWFTGL | SGAGKSAIAN | IVDKRLHALG |
| 490 | 500 | 510 | 520 | 530 | 540 |
| YHTFILDGDN | VRHGLNRDLS | FTVEDRVENI | RRVAEVARLM | VDAGLVVLVS | FISPFRDERQ |
| 550 | 560 | 570 | 580 | 590 | 600 |
| LARERFAADE | FVEVFVDVPL | AVAEARDVKG | LYAKARAGLI | TDFTGIDSPY | EPPQHPELHL |
| 610 | 620 | ||||
| RADQGTPEQL | ASQVLSLLGV | EGK |