A0A1V8RN46 · A0A1V8RN46_9HYPH
- ProteinPyruvate carboxylase
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1152 (go to sequence)
- Protein existencePredicted
- Annotation score3/5
Function
function
Catalyzes a 2-step reaction, involving the ATP-dependent carboxylation of the covalently attached biotin in the first step and the transfer of the carboxyl group to pyruvate in the second.
Catalytic activity
- ATP + hydrogencarbonate + pyruvate = ADP + H+ + oxaloacetate + phosphate
Cofactor
Pathway
Carbohydrate biosynthesis; gluconeogenesis.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 124 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 208 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 301 | |||||
Sequence: R | ||||||
Binding site | 548 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 620 | substrate | ||||
Sequence: R | ||||||
Binding site | 717 | Mn2+ (UniProtKB | ChEBI); via carbamate group | ||||
Sequence: K | ||||||
Binding site | 746 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 748 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 881 | substrate | ||||
Sequence: T |
GO annotations
Aspect | Term | |
---|---|---|
Molecular Function | ATP binding | |
Molecular Function | metal ion binding | |
Molecular Function | pyruvate carboxylase activity | |
Biological Process | gluconeogenesis | |
Biological Process | pyruvate metabolic process |
Keywords
- Molecular function
- Biological process
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePyruvate carboxylase
- EC number
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageBacteria > Pseudomonadota > Alphaproteobacteria > Hyphomicrobiales > Phyllobacteriaceae > Pseudaminobacter
Accessions
- Primary accessionA0A1V8RN46
Proteomes
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 717 | N6-carboxylysine | ||||
Sequence: K | ||||||
Modified residue | 1118 | N6-biotinyllysine | ||||
Sequence: K |
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain, compositional bias, region.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 2-462 | Biotin carboxylation | ||||
Sequence: PISKILVANRSEIAIRVFRAANELGLKTVAIWAEEDKYSLHRFKADESYQVGRGPWLTKDMGPIESYLSIEEVLRVAKLSGADAIHPGYGLLSESPEFADACAKAGITFIGPAPKTMRRLGNKVAARNLAIEVGVPVVPATEPLPDDMEAVKKLAAQIGYPVMLKASWGGGGRGMRAIRSEADLAREVIEGKREAKAAFGKDEVYLEKLIERARHVEVQVLGDKHGNVVHLYERDCSIQRRNQKVVERAPAPYLDAAQREELCGYALRIARETSYVGAGTVEFLMDADSGKFYFIEVNPRIQVEHTVTEEVTGIDIVKAQIHILDGHAIGTPQSGVPAQMDIRLNGHALQCRITTEDPEHNFIPDYGRITAYRGATGFGIRLDGGTAYSGAVITRFYDPLLEKVTAWAPTSGETIARMNRALREFRIRGVATNLTFLEAIIRHPDFANNSYTTRFIDNTPE | ||||||
Domain | 128-326 | ATP-grasp | ||||
Sequence: RNLAIEVGVPVVPATEPLPDDMEAVKKLAAQIGYPVMLKASWGGGGRGMRAIRSEADLAREVIEGKREAKAAFGKDEVYLEKLIERARHVEVQVLGDKHGNVVHLYERDCSIQRRNQKVVERAPAPYLDAAQREELCGYALRIARETSYVGAGTVEFLMDADSGKFYFIEVNPRIQVEHTVTEEVTGIDIVKAQIHILD | ||||||
Domain | 539-807 | Pyruvate carboxyltransferase | ||||
Sequence: VLVTDTTMRDGHQSLLATRVRTHDIARIAGTYARALPQLLSLECWGGATFDVAMRFLTEDPWERLAMIRKAAPNILLQMLLRGANGVGYTNYPDNVVRYFVTEAARGGVDLFRVFDCLNWVENMRVAMDAVASEGKLVEAAMCYTGDILDPERAKYDLKYYIGLAKELEAAGAHILAVKDMSGLLKPAAARVLFKALREATDLPIHFHTHDTSGLSAATVLAAVEAGVDAIDAAMDPFSGNTSQPCLGSIIEALKGSDRAPDLDPEWIR | ||||||
Compositional bias | 1063-1082 | Basic and acidic residues | ||||
Sequence: PDRTHGAGAAKARRKAEPGN | ||||||
Region | 1063-1083 | Disordered | ||||
Sequence: PDRTHGAGAAKARRKAEPGND | ||||||
Domain | 1077-1152 | Lipoyl-binding | ||||
Sequence: KAEPGNDAHVAAPMPGVVSAVPVVAGQAVRAGDVLLSIEAMKMETALHAERDGVIAEVLARAGDQIDAKDLLIVYG |
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,152
- Mass (Da)126,367
- Last updated2017-06-07 v1
- ChecksumFC099351A3C9AC2F
Features
Showing features for compositional bias.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1063-1082 | Basic and acidic residues | ||||
Sequence: PDRTHGAGAAKARRKAEPGN |
Keywords
- Technical term