P26046 (ACVS2_PENCH) Reviewed, UniProtKB/Swiss-Prot
Last modified
September 21, 2011.
Version 77.
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: N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase EC=6.3.2.26 Alternative name(s): Delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase Short name=ACV synthetase Short name=ACVS | ||
| Gene names |
| ||
| Organism | Penicillium chrysogenum (Penicillium notatum) | ||
| Taxonomic identifier | 5076 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › mitosporic Trichocomaceae › Penicillium › Penicillium chrysogenum complex |
Protein attributes
| Sequence length | 3791 AA. |
| Sequence status | Complete. |
| Protein existence | Inferred from homology |
General annotation (Comments)
| Function | Each of the constituent amino acids of the tripeptide acv are activated as aminoacyl-adenylates with peptide bonds formed through the participation of amino acid thioester intermediates. |
| Catalytic activity | L-2-aminohexanedioate + L-cysteine + L-valine + 3 ATP + H2O = N-(L-5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine + 3 AMP + 3 diphosphate. |
| Cofactor | Binds 3 phosphopantetheines covalently. |
| Pathway | |
| Sequence similarities | Belongs to the ATP-dependent AMP-binding enzyme family. Contains 3 acyl carrier domains. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Antibiotic biosynthesis |
| Domain | Repeat |
| Ligand | ATP-binding Nucleotide-binding Phosphopantetheine |
| Molecular function | Ligase |
| Technical term | Multifunctional enzyme |
| Gene Ontology (GO) | |
| Biological process | antibiotic biosynthetic process Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | ATP binding Inferred from electronic annotation. Source: UniProtKB-KW N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase activityInferred from electronic annotation. Source: EC acyl carrier activityInferred from electronic annotation. Source: InterPro cofactor bindingInferred from electronic annotation. Source: InterPro hydrolase activity, acting on ester bondsInferred from electronic annotation. Source: InterPro phosphopantetheine 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 – 3791 | 3791 | N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase | PRO_0000193061 | |||||
Regions | |||||||||
| Domain | 853 – 924 | 72 | Acyl carrier 1 | ||||||
| Domain | 1939 – 2008 | 70 | Acyl carrier 2 | ||||||
| Domain | 3028 – 3095 | 68 | Acyl carrier 3 | ||||||
| Region | 307 – 1068 | 762 | Domain 1 (adipate-activating) | ||||||
| Region | 1392 – 2157 | 766 | Domain 2 (cysteine-activating) | ||||||
| Region | 2574 – 3242 | 669 | Domain 3 (valine-activating) | ||||||
Sites | |||||||||
| Active site | 3631 | 1 | For thioesterase activity By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 885 | 1 | O-(pantetheine 4'-phosphoryl)serine By similarity | ||||||
| Modified residue | 1971 | 1 | O-(pantetheine 4'-phosphoryl)serine By similarity | ||||||
| Modified residue | 3058 | 1 | O-(pantetheine 4'-phosphoryl)serine By similarity | ||||||
Sequences
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References
| [1] | "The cluster of penicillin biosynthetic genes. Identification and characterization of the pcbAB gene encoding the alpha-aminoadipyl-cysteinyl-valine synthetase and linkage to the pcbC and penDE genes." Diez B., Gutierrez S., Barredo J.L., van Solingen P., van der Voort L.H.M., Martin J.F. J. Biol. Chem. 265:16358-16365(1990) [PubMed: 2129535] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: AS-P-78. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | M57425 Genomic DNA. Translation: AAA63415.1. |
| PIR | YGPLV8. A37886. |
3D structure databases | |
| ProteinModelPortal | P26046. |
| ModBase | Search... |
Protocols and materials databases | |
| StructuralBiologyKnowledgebase | Search... |
Family and domain databases | |
| InterPro | IPR010071. AA_adenyl_domain. IPR009081. Acyl_carrier_prot-like. IPR020845. AMP-binding_CS. IPR000873. AMP-dep_Synth/Lig. IPR001242. Condensatn. IPR006163. Phsphopanteth-bd. IPR006162. PPantetheine_attach_site. IPR001031. Thioesterase. [Graphical view] |
| Gene3D | G3DSA:1.10.1200.10. ACP_like. 3 hits. |
| Pfam | PF00501. AMP-binding. 3 hits. PF00668. Condensation. 3 hits. PF00550. PP-binding. 3 hits. PF00975. Thioesterase. 1 hit. [Graphical view] |
| SUPFAM | SSF47336. ACP_like. 3 hits. |
| TIGRFAMs | TIGR01733. AA-adenyl-dom. 3 hits. |
| PROSITE | PS50075. ACP_DOMAIN. 3 hits. PS00455. AMP_BINDING. 3 hits. PS00012. PHOSPHOPANTETHEINE. 3 hits. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ACVS2_PENCH | ||||||||
| Accession | Primary (citable) accession number: P26046 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation program | Fungal Protein Annotation Program | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |

Clusters with