A0A849GNP1 · A0A849GNP1_9GAMM
- ProteinPyruvate carboxylase
- Genepyc
- StatusUniProtKB unreviewed (TrEMBL)
- Organism
- Amino acids1148 (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
- hydrogencarbonate + pyruvate + ATP = oxaloacetate + ADP + phosphate + H+
Cofactor
Pathway
Carbohydrate biosynthesis; gluconeogenesis.
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 119 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 203 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Active site | 296 | |||||
Sequence: R | ||||||
Binding site | 543 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 615 | substrate | ||||
Sequence: R | ||||||
Binding site | 712 | Mn2+ (UniProtKB | ChEBI); via carbamate group | ||||
Sequence: K | ||||||
Binding site | 741 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 743 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 876 | substrate | ||||
Sequence: T |
GO annotations
Aspect | Term | |
---|---|---|
Cellular Component | cytoplasm | |
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 > Gammaproteobacteria > Woeseiales > Woeseiaceae
Accessions
- Primary accessionA0A849GNP1
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 712 | N6-carboxylysine | ||||
Sequence: K | ||||||
Modified residue | 1113 | N6-biotinyllysine | ||||
Sequence: K |
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 3-456 | Biotin carboxylation | ||||
Sequence: EFNKILVANRGEIAIRVMRAANELGKKTVAVYAEEDKLGLHRFKSDQAYRIGEGMGPVAAYLSIEEIIRVAIHSGADAIHPGYGLLSENPMFVDACDAAGIKFIGPKAETMRQLGDKASARRVAIEAGVPVVPASDILPDDPAEIRRMAAEVGYPLMLKASWGGGGRGMRAIMSADELQEKVLEGRREAEAAFGNGEGYVERLVQRARHVEVQILGDRHGDIYHLWERDCSVQRRNQKVVERAPAPYLSQSQRDYICSLGIKVCAHVGYECAGTVEFLMDMDTDEFFFIEVNPRVQVEHTVTEEITGIDIVSAQIRIAEGATLAEATGANTQQDVPLNGHALQCRITTEDPQNNFIPDYGRLLAYRAATGMGIRLDGGTAYNGATITRYYDSLLEKVTAWAPTEKAAIARMDRALREFRIRGVSTNIAFVENLLRHPTFLNNTYSTKFIDNTPE | ||||||
Domain | 123-321 | ATP-grasp | ||||
Sequence: RRVAIEAGVPVVPASDILPDDPAEIRRMAAEVGYPLMLKASWGGGGRGMRAIMSADELQEKVLEGRREAEAAFGNGEGYVERLVQRARHVEVQILGDRHGDIYHLWERDCSVQRRNQKVVERAPAPYLSQSQRDYICSLGIKVCAHVGYECAGTVEFLMDMDTDEFFFIEVNPRVQVEHTVTEEITGIDIVSAQIRIAE | ||||||
Domain | 534-802 | Pyruvate carboxyltransferase | ||||
Sequence: LLITDTTMRDAHQSLLATRMRSLDMINIAETYAHNLPQLFSIECWGGATFDVAYRFLQECPWQRLRDLREKIPNIMTQMLLRASNGVGYTNYPDNVVQEFVRQAAVSGVDVFRVFDSLNWVENMRVAMDAVIANDKLCEGTICYTGDILDPNRAKYNLKYYVDMAKQLEAAGAHVLGLKDMAGLLKPAAATVLIKALKEEIGLPIHFHTHDTSGIAGATILAASAAGVDAADVAMDAFSGGTSQACMGSVVEALRNTERDTGLDIKAIR | ||||||
Domain | 1072-1147 | Lipoyl-binding | ||||
Sequence: KAQENNPAHVGAPMPGVITSVLVTPGQQVKAGDLLLTMEAMKMETGVHAEHDAIVKQVHAPSGSQVDAKDLLLEFD |
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,148
- Mass (Da)126,278
- Last updated2021-09-29 v1
- Checksum16183DFE206743EA