Reviewed,
UniProtKB/Swiss-Prot A0QBE6 (KDC_MYCA1)
Last modified
June 16, 2009.
Version 19.
History...
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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents
Names and origin
| Protein names | Recommended name: Alpha-keto-acid decarboxylase Short name=KDC EC=4.1.1.- | ||||
| Gene names |
| ||||
| Organism | Mycobacterium avium (strain 104) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 243243 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium avium complex (MAC) |
Protein attributes
| Sequence length | 563 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Decarboxylates branched-chain and aromatic alpha-keto acids to aldehydes. |
| Cofactor | Binds 1 metal ion per subunit By similarity. Binds 1 thiamine pyrophosphate per subunit By similarity. |
| Sequence similarities | Belongs to the TPP enzyme family. |
Ontologies
| Keywords | |
|---|---|
| Ligand | Magnesium Metal-binding Thiamine pyrophosphate |
| Molecular function | Decarboxylase Lyase |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Molecular function | carboxy-lyase activity Inferred from electronic annotation. Source: UniProtKB-KW magnesium ion bindingInferred from electronic annotation. Source: UniProtKB-KW thiamin pyrophosphate bindingInferred from electronic annotation. Source: InterPro transferase activityInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 563 | 563 | Alpha-keto-acid decarboxylase | PRO_0000333745 | |||||
Regions | |||||||||
| Region | 394 – 476 | 83 | Thiamine pyrophosphate binding By similarity | ||||||
Sites | |||||||||
| Metal binding | 444 | 1 | Magnesium By similarity | ||||||
| Metal binding | 471 | 1 | Magnesium By similarity | ||||||
| Metal binding | 473 | 1 | Magnesium; via carbonyl oxygen By similarity | ||||||
| Binding site | 59 | 1 | Thiamine pyrophosphate By similarity | ||||||
Sequences
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References
| [1] | Fleischmann R.D., Dodson R.J., Haft D.H., Merkel J.S., Nelson W.C., Fraser C.M. Submitted (OCT-2006) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| CP000479 Genomic DNA. Translation: ABK66465.1. Different initiation. | |
| RefSeq | YP_880234.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 4529569. |
| GenomeReviews | Gene locus MAV_0973 in contig CP000479_GR. |
| KEGG | mav:MAV_0973. |
| TIGR | MAV_0973. |
Family and domain databases | |
| InterPro | IPR000399. TPP_bd_CS. IPR012001. TPP_bd_enzyme_N. IPR011766. TPP_enzyme_bd_C. IPR012000. TPP_enzyme_M. [Graphical view] |
| Pfam | PF02775. TPP_enzyme_C. 1 hit. PF00205. TPP_enzyme_M. 1 hit. PF02776. TPP_enzyme_N. 1 hit. [Graphical view] |
| PROSITE | PS00187. TPP_ENZYMES. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | KDC_MYCA1 | ||||||||
| Accession | Primary (citable) accession number: A0QBE6 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

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