A1ANN6 · A1ANN6_PELPD
- ProteinPyruvate carboxylase
- StatusUniProtKB unreviewed (TrEMBL)
- Amino acids1148 (go to sequence)
- Protein existencePredicted
- Annotation score2/5
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
Features
Showing features for binding site, active site.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Binding site | 121 | ATP (UniProtKB | ChEBI) | ||||
Sequence: K | ||||||
Binding site | 205 | ATP (UniProtKB | ChEBI) | ||||
Sequence: E | ||||||
Binding site | 240 | ATP (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Active site | 297 | |||||
Sequence: R | ||||||
Binding site | 545 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: D | ||||||
Binding site | 617 | substrate | ||||
Sequence: R | ||||||
Binding site | 714 | Mn2+ (UniProtKB | ChEBI); via carbamate group | ||||
Sequence: K | ||||||
Binding site | 743 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 745 | Mn2+ (UniProtKB | ChEBI) | ||||
Sequence: H | ||||||
Binding site | 878 | 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
- Ligand
Enzyme and pathway databases
Names & Taxonomy
Protein names
- Recommended namePyruvate carboxylase
- EC number
Gene names
Organism names
- Strain
- Taxonomic lineageBacteria > Thermodesulfobacteriota > Desulfuromonadia > Desulfuromonadales > Desulfuromonadaceae > Pelobacter
Accessions
- Primary accessionA1ANN6
Proteomes
Subcellular Location
UniProt Annotation
GO Annotation
PTM/Processing
Features
Showing features for modified residue.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 714 | N6-carboxylysine | ||||
Sequence: K | ||||||
Modified residue | 1114 | N6-biotinyllysine | ||||
Sequence: K |
Interaction
Protein-protein interaction databases
Structure
Family & Domains
Features
Showing features for domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Domain | 5-458 | Biotin carboxylation | ||||
Sequence: KFKKIMAANRGEISVRIFRACAELGIRMVAIYSEEDKLSLHRYKADEAYLIGKGKAPVEAYLGIDEIIALALKVGVEAIHPGYGFLSENAEFAEKCEANGIVFIGPTGEMQRALGDKVAGRKMATAAGVNVVPGTEDPIEREEDALKFAKQYGYPIIVKAAAGGGGRGMRVAHNQKELLEGLVAAGSEAKAAFGNAAVFLERYLENPKHIEVQVLGDNYGNLVHFFERDCSVQRRHQKVVEFAPSLCITPELREELCDAALKIARQVNYRNAGTVEFLVDQQGRYYFMEMNPRIQVEHTVTEMITGRNLVQNQILVAGGYALSDPEINIPSQGAINMRGYAIQCRVTTEDPANNFAPDFGMLTTYRSAAGCGVRLDAGNATTGARITPHYDSLLVKVGTWGLTFPEAAHIMDRALREFRIRGVKTNIAFLENVVTHPVFLEGKCDTSFIDKHPE | ||||||
Domain | 125-322 | ATP-grasp | ||||
Sequence: RKMATAAGVNVVPGTEDPIEREEDALKFAKQYGYPIIVKAAAGGGGRGMRVAHNQKELLEGLVAAGSEAKAAFGNAAVFLERYLENPKHIEVQVLGDNYGNLVHFFERDCSVQRRHQKVVEFAPSLCITPELREELCDAALKIARQVNYRNAGTVEFLVDQQGRYYFMEMNPRIQVEHTVTEMITGRNLVQNQILVAG | ||||||
Domain | 536-804 | Pyruvate carboxyltransferase | ||||
Sequence: LFLTDTSMRDAHQSNLATRVRSYDLLKIAEPTSYLGAELFSLECWGGATFDVSMRFLKEDPWQRLHALSEKVPNVLLQMLLRGSNAVGYTNYPDNVVERFVDEAARSGIDVFRVFDSLNWTTGMQVAMEAVRKTGKICEAAICYTGDITDPKRDKYPLEYYVNLAKELEKMGAHILAIKDMAGLLKPFAAYRLIKALKENIGIPVHLHTHDTSSNGGATLLKASEAGVDIVDAALSALSGLTAQPSLNAIASALEGSERDPLVNGRGLQ | ||||||
Domain | 1073-1148 | Lipoyl-binding | ||||
Sequence: KADRDNPSHIGAPMPGKVFKVNVKPGFEVKAGDVLMVTEAMKMETNIKAKVDGRVMEVKFKEGDKVEKDDLLIVMG |
Phylogenomic databases
Family and domain databases
Sequence
- Sequence statusComplete
- Length1,148
- Mass (Da)127,256
- Last updated2007-01-23 v1
- ChecksumD5E58F273A29B9DC
Keywords
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
CP000482 EMBL· GenBank· DDBJ | ABK98956.1 EMBL· GenBank· DDBJ | Genomic DNA |