O33465
Gene name |
metH |
Protein name |
Methionine synthase |
Names |
5-methyltetrahydrofolate--homocysteine methyltransferase, Methionine synthase, vitamin-B12 dependent, MS |
Species |
Pseudomonas putida (Arthrobacter siderocapsulatus) |
KEGG Pathway |
|
EC number |
2.1.1.13: Methyltransferases |
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 O33465
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-O33465-F1 | Predicted | AlphaFoldDB |
No variants for O33465
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for O33465 | |||||
No associated diseases with O33465
5 regional properties for O33465
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | S-adenosylmethionine synthetase, N-terminal | 6 - 103 | IPR022628 |
| domain | S-adenosylmethionine synthetase, central domain | 118 - 235 | IPR022629 |
| domain | S-adenosylmethionine synthetase, C-terminal | 237 - 376 | IPR022630 |
| conserved_site | S-adenosylmethionine synthetase, conserved site | 120 - 130 | IPR022631-1 |
| conserved_site | S-adenosylmethionine synthetase, conserved site | 263 - 271 | IPR022631-2 |
Functions
| Description | ||
|---|---|---|
| EC Number | 2.1.1.13 | Methyltransferases |
| 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 |
|---|---|
| cobalamin binding | Binding to cobalamin (vitamin B12), a water-soluble vitamin characterized by possession of a corrin nucleus containing a cobalt atom. |
| metal ion binding | Binding to a metal ion. |
| methionine synthase activity | Catalysis of the reaction: (6S)-5-methyl-5,6,7,8-tetrahydrofolate + L-homocysteine = (6S)-5,6,7,8-tetrahydrofolate + L-methionine. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| methylation | The process in which a methyl group is covalently attached to a molecule. |
| pteridine-containing compound metabolic process | The chemical reactions and pathways involving any compound containing pteridine (pyrazino(2,3-dipyrimidine)), e.g. pteroic acid, xanthopterin and folic acid. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MSDRSARLQA | LQNALKERIL | ILDGGMGTMI | QSYRLEEHDY | RGTRFADWPS | DVKGNNDLLL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| LSRPDVIAAI | EKAYLDAGAD | ILETNTFNAT | QISQADYGME | SLVYELNVEG | ARIARQVADA |
| 130 | 140 | 150 | 160 | 170 | 180 |
| KTLETPDKPR | FVAGVLGPTS | RTCSISPDVN | DPGYRNVTFD | ELVENYIEAT | RGLIEGGADL |
| 190 | 200 | 210 | 220 | 230 | 240 |
| ILIETIFDTL | NAKAAIFAVQ | QVFEEDAVEL | PIMISGTITD | ASGRTLSGQT | TEAFWNSVRH |
| 250 | 260 | 270 | 280 | 290 | 300 |
| AKPISVGLNC | ALGAKDLRPY | LEELSTKADT | HVSAHPNAGL | PNAFGEYDET | PAEMAAVVEE |
| 310 | 320 | 330 | 340 | 350 | 360 |
| FAASGFLNII | GGCSGTTPGH | IQAIAEAVAK | YKPREIPEIA | KACRLSGLEP | FTIDGQSLFV |
| 370 | 380 | 390 | 400 | 410 | 420 |
| NVGERTNITG | SAKFARLIRE | ENYTEALEVA | LQQVEAGAQV | IDINMDEGML | DSQAAMVRFL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| NMIAGEPDIS | RVPIMIDSSK | GEVIEAGLKC | IQGKGIVNSI | SMKEGVEQFK | HHARLCKRYG |
| 490 | 500 | 510 | 520 | 530 | 540 |
| AAVVVMAFDE | VGQADTAARK | KEICKRSYDI | LVNEVGFPPE | DIIFDPNIFA | VATGIEEHNN |
| 550 | 560 | 570 | 580 | 590 | 600 |
| YAVDFIEACA | YIRDHLPHAL | TSGGVSNVSF | SFRGNNPVRE | AIHSVFLFHA | ISNGLTMGIV |
| NAGLLEI |