A5WTG9 (A5WTG9_MYCTF) Unreviewed, UniProtKB/TrEMBL
Last modified
December 14, 2011.
Version 20.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry infoCustomize orderNames and origin
| Protein names | Recommended name: Aspartate 1-decarboxylase HAMAP MF_00446 EC=4.1.1.11 HAMAP MF_00446 Alternative name(s): Aspartate alpha-decarboxylase HAMAP MF_00446 | ||||
| Gene names |
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| Organism | Mycobacterium tuberculosis (strain F11) [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 336982 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex |
Protein attributes
| Sequence length | 139 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine By similarity. HAMAP MF_00446 SAAS SAAS003190 |
| Catalytic activity | L-aspartate = beta-alanine + CO2. HAMAP MF_00446 SAAS SAAS003190 |
| Cofactor | Pyruvoyl group By similarity. PIRSR PIRSR006246-1 HAMAP MF_00446 SAAS SAAS003190 |
| Pathway | Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1. HAMAP MF_00446 SAAS SAAS003190 |
| Subunit structure | Heterooctamer of four alpha and four beta subunits By similarity. HAMAP MF_00446 SAAS SAAS003190 |
| Subcellular location | Cytoplasm By similarity HAMAP MF_00446 SAAS SAAS003190. |
| Post-translational modification | Is synthesized initially as an inactive proenzyme, which is activated by self-cleavage at a specific serine bond to produce a beta-subunit with a hydroxyl group at its C-terminus and an alpha-subunit with a pyruvoyl group at its N-terminus By similarity. PIRSR PIRSR006246-3 HAMAP MF_00446 |
| Sequence similarities | Belongs to the PanD family. HAMAP MF_00446 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Pantothenate biosynthesis HAMAP MF_00446 SAAS SAAS003190 |
| Cellular component | Cytoplasm HAMAP MF_00446 SAAS SAAS003190 |
| Ligand | Pyruvate PIRSR PIRSR006246-1 HAMAP MF_00446 SAAS SAAS003190 Schiff base PIRSR PIRSR006246-1 HAMAP MF_00446 SAAS SAAS003190 |
| Molecular function | Decarboxylase HAMAP MF_00446 SAAS SAAS003190 Lyase |
| PTM | Autocatalytic cleavage HAMAP MF_00446 Zymogen HAMAP MF_00446 |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | alanine biosynthetic process Inferred from electronic annotation. Source: InterPro pantothenate biosynthetic processInferred from electronic annotation. Source: HAMAP |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | aspartate 1-decarboxylase activity Inferred from electronic annotation. Source: HAMAP bindingInferred from electronic annotation. Source: InterPro |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Regions | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Region | 73 – 75 | 3 | Substrate binding By similarity PIRSR PIRSR006246-2 HAMAP MF_00446 | ||||||
Sites | |||||||||
| Active site | 25 | 1 | Schiff-base intermediate with substrate; via pyruvic acid By similarity PIRSR PIRSR006246-1 HAMAP MF_00446 | ||||||
| Active site | 58 | 1 | Proton donor By similarity PIRSR PIRSR006246-1 HAMAP MF_00446 | ||||||
| Binding site | 57 | 1 | Substrate By similarity PIRSR PIRSR006246-2 HAMAP MF_00446 | ||||||
Amino acid modifications | |||||||||
| Modified residue | 25 | 1 | Pyruvic acid (Ser) By similarity PIRSR PIRSR006246-3 HAMAP MF_00446 | ||||||
Sequences
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References
| [1] | "The complete genome sequence of Mycobacterium tuberculosis F11." Birren B., Lander E., Galagan J., Devon K., Nusbaum C., Borowsky M.L., Grabherr M., Mauceli E., Brockman W., Young S., LaButti K., Pushparaj V., Sykes S., Baldwin J., Fitzgerald M., Bloom T., Zimmer A., Settipalli S. Murray M.Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | CP000717 Genomic DNA. Translation: ABR07958.1. |
| RefSeq | YP_001289560.1. NC_009565.1. |
3D structure databases | |
| ProteinModelPortal | A5WTG9. |
| SMR | A5WTG9. Positions 1-113. |
| ModBase | Search... |
Protein-protein interaction databases | |
| STRING | A5WTG9. |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 5224322. |
| GenomeReviews | Gene locus TBFG_13633 in contig CP000717_GR. |
| KEGG | mtf:TBFG_13633. |
| PATRIC | 18138807. VBIMycTub9078_4036. |
Organism-specific databases | |
| CMR | Search... |
Phylogenomic databases | |
| OMA | LYSKIHR. |
| ProtClustDB | PRK05449. |
Family and domain databases | |
| HAMAP | MF_00446. PanD. [Tree] |
| InterPro | IPR009010. Asp_de-COase-like_fold. IPR003190. Asp_decarbox. [Graphical view] |
| Gene3D | G3DSA:2.40.40.20. Asp_decarboxylase-like_fold. 1 hit. |
| KO | K01579. |
| PANTHER | PTHR21012. Asp_decarbox. 1 hit. |
| Pfam | PF02261. Asp_decarbox. 1 hit. [Graphical view] |
| PIRSF | PIRSF006246. Asp_decarbox. 1 hit. |
| ProDom | PD009294. Asp_decarbox. 1 hit. [Graphical view] [Entries sharing at least one domain] |
| SUPFAM | SSF50692. Asp_decarb_fold. 1 hit. |
| TIGRFAMs | TIGR00223. PanD. 1 hit. |
| ProtoNet | Search... |
Entry information
| Entry name | A5WTG9_MYCTF | ||||||||
| Accession | Primary (citable) accession number: A5WTG9 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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