P14882
Gene name |
Pcca |
Protein name |
Propionyl-CoA carboxylase alpha chain, mitochondrial |
Names |
PCCase subunit alpha, Propanoyl-CoA:carbon dioxide ligase subunit alpha |
Species |
Rattus norvegicus (Rat) |
KEGG Pathway |
rno:687008 |
EC number |
|
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 P14882
| Entry ID | Method | Resolution | Chain | Position | Source |
|---|---|---|---|---|---|
| AF-P14882-F1 | Predicted | AlphaFoldDB |
No variants for P14882
| Variant ID(s) | Position | Change | Description | Diseaes Association | Provenance |
|---|---|---|---|---|---|
| No variants for P14882 | |||||
1 associated diseases with P14882
Without disease ID
8 regional properties for P14882
| Type | Name | Position | InterPro Accession |
|---|---|---|---|
| domain | Biotin/lipoyl attachment | 658 - 737 | IPR000089 |
| binding_site | Biotin-binding site | 693 - 710 | IPR001882 |
| domain | Carbamoyl-phosphate synthetase large subunit-like, ATP-binding domain | 185 - 393 | IPR005479 |
| domain | Biotin carboxylase-like, N-terminal domain | 72 - 180 | IPR005481 |
| domain | Biotin carboxylase, C-terminal | 406 - 514 | IPR005482 |
| domain | ATP-grasp fold | 190 - 387 | IPR011761 |
| domain | Biotin carboxylation domain | 71 - 518 | IPR011764 |
| domain | Propionyl-coenzyme A carboxylase, BT domain | 534 - 662 | IPR041265 |
3 GO annotations of cellular component
| Name | Definition |
|---|---|
| catalytic complex | A protein complex which is capable of catalytic activity. |
| 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. |
4 GO annotations of molecular function
| Name | Definition |
|---|---|
| ATP binding | Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator. |
| enzyme binding | Binding to an enzyme, a protein with catalytic activity. |
| metal ion binding | Binding to a metal ion. |
| propionyl-CoA carboxylase activity | Catalysis of the reaction: ATP + propanoyl-CoA + HCO3- = ADP + phosphate + (S)-methylmalonyl-CoA. |
2 GO annotations of biological process
| Name | Definition |
|---|---|
| cellular amino acid catabolic process | The chemical reactions and pathways resulting in the breakdown of amino acids, organic acids containing one or more amino substituents. |
| fatty acid catabolic process | The chemical reactions and pathways resulting in the breakdown 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. |
1 homologous proteins in AiPD
| UniProt AC | Gene Name | Protein Name | Species | Evidence Code |
|---|---|---|---|---|
| Q19842 | pcca-1 | Propionyl-CoA carboxylase alpha chain, mitochondrial | Caenorhabditis elegans | PR |
| 10 | 20 | 30 | 40 | 50 | 60 |
| MAGLWVRTVA | LLAARRHWRR | SSQQLLWTLK | RAPRSSQQLL | WTLKRAPVYS | QQCLVVSRSL |
| 70 | 80 | 90 | 100 | 110 | 120 |
| SSVEYEPKEK | TFDKILIANR | GEIACRVIKT | CRKMGIRTVA | IHSDVDASSV | HVKMADEAVC |
| 130 | 140 | 150 | 160 | 170 | 180 |
| VGPAPTSKSY | LNMDAIMEAI | KKTGAQAVHP | GYGFLSENKE | FAKCLAAEDV | TFIGPDTHAI |
| 190 | 200 | 210 | 220 | 230 | 240 |
| QAMGDKIESK | LLAKRAKVNT | IPGFDGVLKD | ADEAVRIARE | IGYPVMIKAS | AGGGGKGMRI |
| 250 | 260 | 270 | 280 | 290 | 300 |
| PWDDEETRDG | FRFSSQEAAS | SFGDDRLLIE | KFIDNPRHIE | IQVLGDKHGN | ALWLNERECS |
| 310 | 320 | 330 | 340 | 350 | 360 |
| IQRRNQKVVE | EAPSIFLDPE | TRRAMGEQAV | AWPKAVKYSS | AGTVEFLVDS | QKNFYFLEMN |
| 370 | 380 | 390 | 400 | 410 | 420 |
| TRLQVEHPVT | ECITGLDLVQ | EMILVAKGYP | LRHKQEDIPI | SGWAVECRVY | AEDPYKSFGL |
| 430 | 440 | 450 | 460 | 470 | 480 |
| PSIGRLSQYQ | EPIHLPGVRV | DSGIQPGSDI | SIYHDPMISK | LVTYGSDRAE | ALKRMEDALD |
| 490 | 500 | 510 | 520 | 530 | 540 |
| SYVIRGVTHN | IPLLREVIIN | TRFVKGDIST | KFLSDVYPDG | FKGHMLTPSE | RDQLLAIASS |
| 550 | 560 | 570 | 580 | 590 | 600 |
| LFVASQLRAQ | RFQEHSRVPV | IRPDVAKWEL | SVKLHDEDHT | VVASNNGPTF | NVEVDGSKLN |
| 610 | 620 | 630 | 640 | 650 | 660 |
| VTSTWNLASP | LLSVNVDGTQ | RTVQCLSPDA | GGNMSIQFLG | TVYKVHILTK | LAAELNKFML |
| 670 | 680 | 690 | 700 | 710 | 720 |
| EKVPKDTSSV | LRSPKPGVVV | AVSVKPGDMV | AEGQEICVIE | AMKMQNSMTA | GKMGKVKLVH |
| 730 | |||||
| CKAGDTVGEG | DLLVELE |