Q8K0L3
Gene name |
Acsm2 |
Protein name |
Acyl-coenzyme A synthetase ACSM2, mitochondrial |
Names |
Acyl-CoA synthetase medium-chain family member 2, Benzoate--CoA ligase, Butyrate--CoA ligase 2, Butyryl-coenzyme A synthetase 2, Middle-chain acyl-CoA synthetase 2 |
Species |
Mus musculus (Mouse) |
KEGG Pathway |
mmu:233799 |
EC number |
6.2.1.2: Acid--thiol ligases |
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 Q8K0L3
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-Q8K0L3-F1 | Predicted | AlphaFoldDB |
37 variants for Q8K0L3
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| rs228867113 | 21 | R>C | No | EVA | |
| rs3388941652 | 27 | I>N | No | EVA | |
| rs3388939240 | 34 | Q>E | No | EVA | |
| rs243000849 | 57 | V>I | No | EVA | |
| rs231762316 | 84 | R>Q | No | EVA | |
| rs3388899046 | 137 | T>S | No | EVA | |
| rs3388939694 | 167 | V>L | No | EVA | |
| rs3388945798 | 185 | E>G | No | EVA | |
| rs3388915023 | 189 | E>D | No | EVA | |
| rs32561385 | 213 | R>Q | No | EVA | |
| rs3388944974 | 233 | H>L | No | EVA | |
| rs3398553324 | 248 | S>R | No | EVA | |
| rs227696573 | 268 | M>L | No | EVA | |
| rs3388899061 | 276 | E>D | No | EVA | |
| rs213845667 | 288 | L>V | No | EVA | |
| rs3398481993 | 289 | L>* | No | EVA | |
| rs32557893 | 303 | S>R | No | EVA | |
| rs257616574 | 308 | T>S | No | EVA | |
| rs227884249 | 308 | T>S | No | EVA | |
| rs219602722 | 315 | I>V | No | EVA | |
| rs221980725 | 361 | I>F | No | EVA | |
| rs221723292 | 370 | I>T | No | EVA | |
| rs3388945121 | 371 | C>Y | No | EVA | |
| rs32560048 | 389 | A>P | No | EVA | |
| rs32562165 | 418 | I>T | No | EVA | |
| rs219641773 | 445 | M>T | No | EVA | |
| rs228397711 | 448 | R>Q | No | EVA | |
| rs3388941322 | 466 | I>F | No | EVA | |
| rs3388936350 | 477 | S>P | No | EVA | |
| rs3388939302 | 505 | V>G | No | EVA | |
| rs3388945134 | 543 | R>G | No | EVA | |
| rs3388941716 | 551 | L>P | No | EVA | |
| rs3388939262 | 558 | K>N | No | EVA | |
| rs3388945825 | 566 | A>S | No | EVA | |
| rs3388941715 | 568 | E>D | No | EVA | |
| rs579137449 | 574 | R>Q | No | EVA | |
| rs582379148 | 576 | A>Y | No | EVA |
No associated diseases with Q8K0L3
Functions
| Description | ||
|---|---|---|
| EC Number | 6.2.1.2 | Acid--thiol ligases |
| Subcellular Localization |
|
|
| PANTHER Family | ||
| PANTHER Subfamily | ||
| PANTHER Protein Class | ||
| PANTHER Pathway Category | No pathway information available | |
2 GO annotations of cellular component
| Name | Definition |
|---|---|
| mitochondrial matrix | The gel-like material, with considerable fine structure, that lies in the matrix space, or lumen, of a mitochondrion. It contains the enzymes of the tricarboxylic acid cycle and, in some organisms, the enzymes concerned with fatty acid oxidation. |
| mitochondrion | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. |
7 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| benzoate-CoA ligase activity | Catalysis of the reaction: ATP + benzoate + CoA = AMP + benzoyl-CoA + diphosphate. |
| butyrate-CoA ligase activity | Catalysis of the reaction: ATP + an acid + CoA = AMP + diphosphate + an acyl-CoA. |
| decanoate-CoA ligase activity | Catalysis of the reaction: ATP + decanoate + CoA = AMP + diphosphate + decanoyl-CoA. |
| fatty acid ligase activity | Catalysis of the ligation of a fatty acid to an acceptor, coupled to the hydrolysis of ATP. |
| fatty-acyl-CoA synthase activity | Catalysis of the reaction: acetyl-CoA + n malonyl-CoA + 2n NADH + 2n NADPH + 4n H+ = a long-chain acyl-CoA + n CoA + n CO2 + 2n NAD+ + 2n NADP+. |
| metal ion binding | Binding to a metal ion. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| acyl-CoA metabolic process | The chemical reactions and pathways involving acyl-CoA, any derivative of coenzyme A in which the sulfhydryl group is in thiolester linkage with an acyl group. |
| fatty acid biosynthetic process | The chemical reactions and pathways resulting in the formation of a fatty acid, any of the aliphatic monocarboxylic acids that can be liberated by hydrolysis from naturally occurring fats and oils. Fatty acids are predominantly straight-chain acids of 4 to 24 carbon atoms, which may be saturated or unsaturated; branched fatty acids and hydroxy fatty acids also occur, and very long chain acids of over 30 carbons are found in waxes. |
8 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q9NR19 | ACSS2 | Acetyl-coenzyme A synthetase, cytoplasmic | Homo sapiens (Human) | PR |
| Q08AH3 | ACSM2A | Acyl-coenzyme A synthetase ACSM2A, mitochondrial | Homo sapiens (Human) | PR |
| Q68CK6 | ACSM2B | Acyl-coenzyme A synthetase ACSM2B, mitochondrial | Homo sapiens (Human) | PR |
| Q9QXG4 | Acss2 | Acetyl-coenzyme A synthetase, cytoplasmic | Mus musculus (Mouse) | PR |
| Q9D2R0 | Aacs | Acetoacetyl-CoA synthetase | Mus musculus (Mouse) | PR |
| Q9JMI1 | Aacs | Acetoacetyl-CoA synthetase | Rattus norvegicus (Rat) | PR |
| O70490 | Acsm2 | Acyl-coenzyme A synthetase ACSM2, mitochondrial | Rattus norvegicus (Rat) | PR |
| Q84P17 | AAE18 | Probable acyl-activating enzyme 18, peroxisomal | Arabidopsis thaliana (Mouse-ear cress) | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MHHLWKIPRL | FTLWGNEISC | RTFHMNIKKL | IPIQWGHQEA | PAKFNFASDV | IDHWASVEKA |
| 70 | 80 | 90 | 100 | 110 | 120 |
| GKRSSGPALW | WMNGSGKEIK | WSFRELSEAS | KQTANVLSGA | CGLHRGDRVA | VVLPRIPEWW |
| 130 | 140 | 150 | 160 | 170 | 180 |
| LMILGCMRTG | LVFMPGTIQM | RSSDILYRLQ | ASKARAIVAG | DEVAQEVDAV | APDCSFLKIK |
| 190 | 200 | 210 | 220 | 230 | 240 |
| LLVSENSREG | WLNFKALLKE | ASTIHQCVET | ESRESAAIYF | TSGTSGPPKM | AEHSHCSLGI |
| 250 | 260 | 270 | 280 | 290 | 300 |
| KAKMDAASWT | GLSTSDIIWT | ISDTAWIMNI | LGAFLEPWVL | GACIFVHLLP | KFDSQTVLKV |
| 310 | 320 | 330 | 340 | 350 | 360 |
| LSSYPINTLV | GAPIIYRMLL | QQDLSSYKFP | HLHSCFSGGE | TLLPETLENW | KAKTGLEIRE |
| 370 | 380 | 390 | 400 | 410 | 420 |
| IYGQTETGLI | CRVSRTMKVK | PGYLGTAFAH | YDVQVIDEQG | NVLPPGKEGD | IAIRVKPIWP |
| 430 | 440 | 450 | 460 | 470 | 480 |
| IGMFSGYVDN | PKKTQDNIRG | DFWLMGDRGI | KDPEGYFHFI | GRSDDIINSS | GYRIGPSEVE |
| 490 | 500 | 510 | 520 | 530 | 540 |
| NALMEHPAVS | ETAVISSPDP | SRGEVVKAFV | VLAPEFLSHD | RDQLTKVLQE | HVKSVTAPYK |
| 550 | 560 | 570 | |||
| YPRKVEFVLD | LPKTVTGKIE | RAKLRAKEWK | TSGRA |