A9MTH7
Gene name |
moaA |
Protein name |
GTP 3',8-cyclase |
Names |
Molybdenum cofactor biosynthesis protein A |
Species |
Salmonella paratyphi B (strain ATCC BAA-1250 / SPB7) |
KEGG Pathway |
spq:SPAB_02714 |
EC number |
4.1.99.22: Other carbon-carbon 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
1 structures for A9MTH7
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-A9MTH7-F1 | Predicted | AlphaFoldDB |
No variants for A9MTH7
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for A9MTH7 | |||||
No associated diseases with A9MTH7
4 regional properties for A9MTH7
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | MoaA/NifB/PqqE, iron-sulphur binding, conserved site | 20 - 31 | IPR000385 |
| domain | Elp3/MiaA/NifB-like, radical SAM core domain | 14 - 226 | IPR006638 |
| domain | Radical SAM | 8 - 234 | IPR007197 |
| domain | Molybdenum cofactor biosynthesis protein A-like, twitch domain | 186 - 321 | IPR010505 |
Functions
| Description | ||
|---|---|---|
| EC Number | 4.1.99.22 | Other carbon-carbon lyases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
1 GO annotations of cellular component
| Name | Definition |
|---|---|
| molybdopterin synthase complex | A protein complex that possesses molybdopterin synthase activity. In E. coli, the complex is a heterotetramer consisting of two MoaD and two MoaE subunits. |
5 GO annotations of molecular function
| Name | Definition |
|---|---|
| 4 iron, 4 sulfur cluster binding | Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands. |
| GTP 3',8'-cyclase activity | Catalysis of the reaction: GTP=(8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate. |
| GTP binding | Binding to GTP, guanosine triphosphate. |
| metal ion binding | Binding to a metal ion. |
| S-adenosyl-L-methionine binding | Binding to S-adenosyl-L-methionine. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| Mo-molybdopterin cofactor biosynthetic process | The chemical reactions and pathways resulting in the formation of the Mo-molybdopterin cofactor, essential for the catalytic activity of some enzymes. The cofactor consists of a mononuclear molybdenum (Mo) ion coordinated by one or two molybdopterin ligands. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MASQLTDAFA | RKFYYLRLSI | TDVCNFRCTY | CLPDGYKPGG | VTNNGFLTVD | EIRRVTRAFA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SLGTEKVRLT | GGEPSLRRDF | TDIIAAVGEN | DAIRQIAVTT | NGYRLARDAA | SWREAGLTGV |
| 130 | 140 | 150 | 160 | 170 | 180 |
| NVSVDSLDAR | QFHAITGQDK | FRQVMAGIDA | AFDAGFEKVK | VNTVLMRDVN | HHQLDTFLAW |
| 190 | 200 | 210 | 220 | 230 | 240 |
| IQPRPIQLRF | IELMETGEGS | DLFRKHHISG | QVLRDELIKR | GWIHQLRQRS | DGPAQVFCHP |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DYAGEIGLIM | PYEKDFCATC | NRLRVSSVGK | LHLCLFGDGG | VSLRDLLQDD | AQQYALEERI |
| 310 | 320 | ||||
| SDALREKKQT | HFLHQSNTGI | TQNLSYIGG |