Q8RHX7
Gene name |
FN1863 |
Protein name |
Lysine 5,6-aminomutase alpha subunit |
Names |
5,6-LAM, D-lysine 5,6-aminomutase alpha subunit, L-beta-lysine 5,6-aminomutase alpha subunit |
Species |
Fusobacterium nucleatum subsp. nucleatum (strain ATCC 25586 / DSM 15643 / BCRC 10681 / CIP 101130 / JCM 8532 / KCTC 2640 / LMG 13131 / VPI 4355) |
KEGG Pathway |
fnu:FN1863 |
EC number |
5.4.3.3: Transferring amino groups |
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 Q8RHX7
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q8RHX7-F1 | Predicted | AlphaFoldDB |
No variants for Q8RHX7
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for Q8RHX7 | |||||
No associated diseases with Q8RHX7
6 regional properties for Q8RHX7
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Rho GTPase-activating protein domain | 481 - 671 | IPR000198 |
| domain | FCH domain | 22 - 121 | IPR001060 |
| domain | SH3 domain | 720 - 779 | IPR001452 |
| domain | F-BAR domain | 19 - 314 | IPR031160 |
| domain | srGAP1/2/3, SH3 domain | 724 - 776 | IPR035648 |
| domain | SLIT-ROBO Rho GTPase-activating protein 1, F-BAR domain | 26 - 278 | IPR037451 |
Functions
| Description | ||
|---|---|---|
| EC Number | 5.4.3.3 | Transferring amino groups |
| 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 |
|---|---|
| beta-lysine 5,6-aminomutase activity | Catalysis of the reaction: (3S)-3,6-diaminohexanoate = (3S,5S)-3,5-diaminohexanoate. |
| cobalamin binding | Binding to cobalamin (vitamin B12), a water-soluble vitamin characterized by possession of a corrin nucleus containing a cobalt atom. |
| D-lysine 5,6-aminomutase activity | Catalysis of the reaction: D-lysine = 2,5-diaminohexanoate. |
1 GO annotations of biological process
| Name | Definition |
|---|---|
| L-lysine catabolic process to acetate | The chemical reactions and pathways resulting in the breakdown of L-lysine into other compounds, including acetate. |
No homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| No homologous proteins | ||||
| 10 | 20 | 30 | 40 | 50 | 60 |
| MGKLDLDWGL | VKEARESAKK | IAADAQVFID | AHSTVTVERT | ICRLLGIDGV | DEFGVPLPNV |
| 70 | 80 | 90 | 100 | 110 | 120 |
| IVDFIKDNGN | ISLGVAKYIG | NAMIETKLQP | QEIAEKVAKK | ELDITKMQWH | DDFDIQLALK |
| 130 | 140 | 150 | 160 | 170 | 180 |
| DITHSTVERI | KANRKAREDY | LEQFGGDKKG | PYIYVIVATG | NIYEDVTQAV | AAARQGADVV |
| 190 | 200 | 210 | 220 | 230 | 240 |
| AVIRTTGQSL | LDFVPFGATT | EGFGGTMATQ | ENFRIMRKAL | DDVGVELGRY | IRLCNYCSGL |
| 250 | 260 | 270 | 280 | 290 | 300 |
| CMPEIAAMGA | LERLDMMLND | ALYGILFRDI | NMKRTLVDQF | FSRIINGFAG | VIINTGEDNY |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LTTADAIEEA | HTVLASQFIN | EQFALVAGLP | EEQMGLGHAF | EMEPGTENGF | LLELAQAQMA |
| 370 | 380 | 390 | 400 | 410 | 420 |
| REIFPKAPLK | YMPPTKFMTG | NIFKGHIQDA | LFNIVTITTG | QKVHLLGMLT | EAIHTPFMSD |
| 430 | 440 | 450 | 460 | 470 | 480 |
| RALSIENARY | IFNNLKDFGN | DIEFKKGGIM | NTRAQEVLKK | AAELLKTIET | MGIFKTIEKG |
| 490 | 500 | 510 | |||
| VFGGVRRPID | GGKGLAGVFE | KDNTYFNPFI | PLMLGGDR |