P65660 (PAND_MYCTU) Reviewed, UniProtKB/Swiss-Prot
Last modified
January 25, 2012.
Version 57.
History...
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
Names·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize orderNames and origin
| Protein names | Recommended name: Aspartate 1-decarboxylase EC=4.1.1.11 Alternative name(s): Aspartate alpha-decarboxylase Cleaved into the following 2 chains: | ||||||
| Gene names |
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| Organism | Mycobacterium tuberculosis | ||||||
| Taxonomic identifier | 1773 [NCBI] | ||||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Mycobacteriaceae › Mycobacterium › Mycobacterium tuberculosis complex |
Protein attributes
| Sequence length | 139 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is further processed into a mature form. |
| Protein existence | Evidence at protein level |
General annotation (Comments)
| Function | Catalyzes the pyruvoyl-dependent decarboxylation of aspartate to produce beta-alanine By similarity. HAMAP MF_00446 |
| Catalytic activity | L-aspartate = beta-alanine + CO2. HAMAP MF_00446 |
| Cofactor | Pyruvoyl group By similarity. HAMAP MF_00446 |
| Pathway | Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1. HAMAP MF_00446 |
| Subunit structure | Heterooctamer of four alpha and four beta subunits By similarity. |
| Subcellular location | Cytoplasm By similarity HAMAP MF_00446. |
| 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. HAMAP MF_00446 |
| Sequence similarities | Belongs to the PanD family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Pantothenate biosynthesis |
| Cellular component | Cytoplasm |
| Ligand | Pyruvate Schiff base |
| Molecular function | Decarboxylase Lyase |
| PTM | Autocatalytic cleavage Zymogen |
| Technical term | 3D-structure Complete proteome Reference proteome |
| Gene Ontology (GO) | |
| Biological process | alanine biosynthetic process Inferred from direct assay. Source: MTBBASE pantothenate biosynthetic processInferred from direct assay. Source: MTBBASE protein homotetramerizationInferred from physical interaction. Source: MTBBASE |
| Cellular component | cell wall Inferred from direct assay. Source: MTBBASE cytosolInferred from direct assay. Source: MTBBASE |
| Molecular function | aspartate 1-decarboxylase activity Inferred from direct assay. Source: MTBBASE bindingInferred 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 – 24 | 24 | Aspartate 1-decarboxylase beta chain By similarity | PRO_0000023121 | |||||||||||||||||||||||||||||||||
| Chain | 25 – 139 | 115 | Aspartate 1-decarboxylase alpha chain By similarity | PRO_0000023122 | |||||||||||||||||||||||||||||||||
Regions | |||||||||||||||||||||||||||||||||||||
| Region | 73 – 75 | 3 | Substrate binding By similarity | ||||||||||||||||||||||||||||||||||
Sites | |||||||||||||||||||||||||||||||||||||
| Active site | 25 | 1 | Schiff-base intermediate with substrate; via pyruvic acid By similarity | ||||||||||||||||||||||||||||||||||
| Active site | 58 | 1 | Proton donor By similarity | ||||||||||||||||||||||||||||||||||
| Binding site | 57 | 1 | Substrate By similarity | ||||||||||||||||||||||||||||||||||
Amino acid modifications | |||||||||||||||||||||||||||||||||||||
| Modified residue | 25 | 1 | Pyruvic acid (Ser) By similarity | ||||||||||||||||||||||||||||||||||
Secondary structure | |||||||||||||||||||||||||||||||||||||
Helix Strand Turn | |||||||||||||||||||||||||||||||||||||
| Beta strand | 2 – 4 | 3 | |||||||||||||||||||||||||||||||||||
| Beta strand | 8 – 14 | 7 | |||||||||||||||||||||||||||||||||||
| Beta strand | 18 – 22 | 5 | |||||||||||||||||||||||||||||||||||
| Beta strand | 25 – 29 | 5 | |||||||||||||||||||||||||||||||||||
| Helix | 30 – 35 | 6 | |||||||||||||||||||||||||||||||||||
| Beta strand | 44 – 48 | 5 | |||||||||||||||||||||||||||||||||||
| Turn | 49 – 51 | 3 | |||||||||||||||||||||||||||||||||||
| Beta strand | 54 – 57 | 4 | |||||||||||||||||||||||||||||||||||
| Beta strand | 59 – 62 | 4 | |||||||||||||||||||||||||||||||||||
| Turn | 64 – 67 | 4 | |||||||||||||||||||||||||||||||||||
| Beta strand | 69 – 74 | 6 | |||||||||||||||||||||||||||||||||||
| Turn | 75 – 78 | 4 | |||||||||||||||||||||||||||||||||||
| Beta strand | 84 – 89 | 6 | |||||||||||||||||||||||||||||||||||
| Beta strand | 92 – 94 | 3 | |||||||||||||||||||||||||||||||||||
| Helix | 95 – 99 | 5 | |||||||||||||||||||||||||||||||||||
| Beta strand | 104 – 107 | 4 | |||||||||||||||||||||||||||||||||||
Sequences
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References
Cross-references
Sequence databases | |||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| EMBL GenBank DDBJ | BX842583 Genomic DNA. Translation: CAB08943.1. AE000516 Genomic DNA. Translation: AAK48064.1. | ||||||||||||
| PIR | B70955. | ||||||||||||
| RefSeq | NP_218118.1. NC_000962.2. NP_338250.1. NC_002755.2. | ||||||||||||
3D structure databases | |||||||||||||
| PDBe RCSB PDB PDBj |
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| ProteinModelPortal | P65660. | ||||||||||||
| SMR | P65660. Positions 1-113. | ||||||||||||
| ModBase | Search... | ||||||||||||
Protocols and materials databases | |||||||||||||
| StructuralBiologyKnowledgebase | Search... | ||||||||||||
Genome annotation databases | |||||||||||||
| EnsemblBacteria | EBMYCT00000002380; EBMYCP00000002380; EBMYCG00000002378. EBMYCT00000072275; EBMYCP00000070334; EBMYCG00000072270. | ||||||||||||
| GeneID | 885596. 922795. | ||||||||||||
| GenomeReviews | Gene locus MT3706.1 in contig AE000516_GR. Gene locus Rv3601c in contig AL123456_GR. | ||||||||||||
| KEGG | mtc:MT3706.1. mtu:Rv3601c. | ||||||||||||
| PATRIC | 18129901. VBIMycTub22151_4045. | ||||||||||||
| TIGR | MT3706.1. | ||||||||||||
Organism-specific databases | |||||||||||||
| TubercuList | Rv3601c. | ||||||||||||
Phylogenomic databases | |||||||||||||
| GeneTree | EBGT00050000017253. | ||||||||||||
| HOGENOM | HBG302821. | ||||||||||||
| OMA | LYSKIHR. | ||||||||||||
| PhylomeDB | P65660. | ||||||||||||
| 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 | PAND_MYCTU | ||||||||
| Accession | Primary (citable) accession number: P65660 Secondary accession number(s): O06281 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Prokaryotic Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with