Q8IQF1
Gene name |
Mocs1 (lxd, CG33048) |
Protein name |
Molybdenum cofactor biosynthesis protein 1 |
Names |
|
Species |
Drosophila melanogaster (Fruit fly) |
KEGG Pathway |
dme:Dmel_CG33048 |
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 Q8IQF1
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q8IQF1-F1 | Predicted | AlphaFoldDB |
No variants for Q8IQF1
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q8IQF1 | |||||
No associated diseases with Q8IQF1
5 regional properties for Q8IQF1
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| conserved_site | MoaA/NifB/PqqE, iron-sulphur binding, conserved site | 76 - 87 | IPR000385 |
| domain | Molybdopterin cofactor biosynthesis C (MoaC) domain | 412 - 547 | IPR002820 |
| domain | Elp3/MiaA/NifB-like, radical SAM core domain | 70 - 272 | IPR006638 |
| domain | Radical SAM | 64 - 276 | IPR007197 |
| domain | Molybdenum cofactor biosynthesis protein A-like, twitch domain | 240 - 368 | 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. |
| cyclic pyranopterin monophosphate synthase activity | Catalysis of the reaction: (8S)-3',8-cyclo-7,8-dihydroguanosine 5'-triphosphate = cyclic pyranopterin phosphate + diphosphate. |
| 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. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| inter-male aggressive behavior | Aggressive behavior based on competition between males of the same species over access to resources such as females, dominance, status, etc. and characterized by noise, threats, and is often less injurious. |
| 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. |
3 homologous proteins in AiPD
| 10 | 20 | 30 | 40 | 50 | 60 |
| MRLLARHAIR | LLGQENSAGE | VASLSRGAIR | LKATTGYLNL | ATASVQPLEP | EKQVLRKNSP |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LTDSFGRHHT | YLRISLTERC | NLRCDYCMPA | EGVPLQPKNK | LLTTEEILRL | ARIFVEQGVR |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KIRLTGGEPT | VRRDIVEIVA | QMKALPELEQ | IGITTNGLVL | TRLLLPLQRA | GLDNLNISLD |
| 190 | 200 | 210 | 220 | 230 | 240 |
| TLKRDRFEKI | TRRKGWERVI | AGIDLAVQLG | YRPKVNCVLM | RDFNEDEICD | FVEFTRNRPV |
| 250 | 260 | 270 | 280 | 290 | 300 |
| DVRFIEYMPF | SGNKWHTERL | ISYKDTLQII | RQRWPDFKAL | PNGPNDTSKA | YAVPGFKGQV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| GFITSMTEHF | CGTCNRLRLT | ADGNIKVCLF | GNKEFSLRDA | MRDESVSEEQ | LVDLIGAAVQ |
| 370 | 380 | 390 | 400 | 410 | 420 |
| RKKKQHADAA | PRLHHHLHPY | SYHHAYHTSR | LQLQARNYSQ | LTHVDGQGKA | QMVDVGAKPS |
| 430 | 440 | 450 | 460 | 470 | 480 |
| TTRLARAEAT | VQVGEKLTQL | IADNQVAKGD | VLTVAQIAGI | MGAKRTAELI | PLCHNISLSS |
| 490 | 500 | 510 | 520 | 530 | 540 |
| VKVQATLLKT | EQSVRLEATV | RCSGQTGVEM | EALTAVSVAA | LTVYDMCKAV | SHDICITNVR |
| 550 | 560 | ||||
| LLSKSGGKRD | FQREEPQNGI | VTEVE |