C8NRH0 (C8NRH0_COREF) Unreviewed, UniProtKB/TrEMBL
Last modified
May 1, 2013.
Version 27.
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-Rule MF_00446 EC=4.1.1.11 HAMAP-Rule MF_00446 Alternative name(s): Aspartate alpha-decarboxylase HAMAP-Rule MF_00446 | ||||
| Gene names |
| ||||
| Organism | Corynebacterium efficiens (strain DSM 44549 / YS-314 / AJ 12310 / JCM 11189 / NBRC 100395) EMBL EEW48818.1 | ||||
| Taxonomic identifier | 196164 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Corynebacterineae › Corynebacteriaceae › Corynebacterium › ![]() |
Protein attributes
| Sequence length | 136 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-Rule MF_00446 SAAS SAAS003190 |
| Catalytic activity | L-aspartate = beta-alanine + CO2. HAMAP-Rule MF_00446 SAAS SAAS003190 |
| Cofactor | Pyruvoyl group By similarity. PIRSR PIRSR006246-1 HAMAP-Rule MF_00446 SAAS SAAS003190 |
| Pathway | Cofactor biosynthesis; (R)-pantothenate biosynthesis; beta-alanine from L-aspartate: step 1/1. HAMAP-Rule MF_00446 SAAS SAAS003190 |
| Subunit structure | Heterooctamer of four alpha and four beta subunits By similarity. HAMAP-Rule MF_00446 SAAS SAAS003190 |
| Subcellular location | Cytoplasm By similarity HAMAP-Rule 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-Rule MF_00446 |
| Sequence similarities | Belongs to the PanD family. HAMAP-Rule MF_00446 |
Ontologies
| Keywords | |
|---|---|
| Biological process | Pantothenate biosynthesis HAMAP-Rule MF_00446 SAAS SAAS003190 |
| Cellular component | Cytoplasm HAMAP-Rule MF_00446 SAAS SAAS003190 |
| Ligand | Pyruvate PIRSR PIRSR006246-1 HAMAP-Rule MF_00446 SAAS SAAS003190 Schiff base PIRSR PIRSR006246-1 HAMAP-Rule MF_00446 SAAS SAAS003190 |
| Molecular function | Decarboxylase HAMAP-Rule MF_00446 SAAS SAAS003190 Lyase |
| PTM | Autocatalytic cleavage HAMAP-Rule MF_00446 Zymogen HAMAP-Rule MF_00446 |
| 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 |
| 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-Rule MF_00446 | ||||||
Sites | |||||||||
| Active site | 25 | 1 | Schiff-base intermediate with substrate; via pyruvic acid By similarity PIRSR PIRSR006246-1 HAMAP-Rule MF_00446 | ||||||
| Active site | 58 | 1 | Proton donor By similarity PIRSR PIRSR006246-1 HAMAP-Rule MF_00446 | ||||||
| Binding site | 57 | 1 | Substrate By similarity PIRSR PIRSR006246-2 HAMAP-Rule MF_00446 | ||||||
Amino acid modifications | |||||||||
| Modified residue | 25 | 1 | Pyruvic acid (Ser) By similarity PIRSR PIRSR006246-3 HAMAP-Rule MF_00446 | ||||||
Sequences
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References
| [1] | Muzny D., Qin X., Deng J., Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M., Korchina V., Kovar C., Mata R., Mathew T., Ngo R. Gibbs R.Submitted (AUG-2009) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE. Strain: YS-314 EMBL EEW48818.1. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | ACLI01000106 Genomic DNA. Translation: EEW48818.1. |
| RefSeq | NP_736745.1. NC_004369.1. |
3D structure databases | |
| ProteinModelPortal | C8NRH0. |
| SMR | C8NRH0. Positions 1-113. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Genome annotation databases | |
| GeneID | 1031997. |
| KEGG | cef:CE0135. |
| PATRIC | 21486458. VBICorEff9312_0183. |
Phylogenomic databases | |
| eggNOG | COG0853. |
| KO | K01579. |
| OMA | LYSKIHR. |
| ProtClustDB | PRK05449. |
Enzyme and pathway databases | |
| BioCyc | CEFF196164:GJW8-138-MONOMER. |
| UniPathway | UPA00028; UER00002. |
Family and domain databases | |
| Gene3D | 2.40.40.20. 1 hit. |
| HAMAP | MF_00446. PanD. |
| InterPro | IPR009010. Asp_de-COase-like_dom. IPR003190. Asp_decarbox. [Graphical view] |
| PANTHER | PTHR21012. PTHR21012. 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 | C8NRH0_COREF | ||||||||
| Accession | Primary (citable) accession number: C8NRH0 | ||||||||
| Entry history |
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| Entry status | Unreviewed (UniProtKB/TrEMBL) | ||||||||

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