Reviewed,
UniProtKB/Swiss-Prot P27742 (ACVS_EMENI)
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June 16, 2009.
Version 67.
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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: 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 | Emericella nidulans (Aspergillus nidulans) | ||||
| Taxonomic identifier | 162425 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Fungi › Dikarya › Ascomycota › Pezizomycotina › Eurotiomycetes › Eurotiomycetidae › Eurotiales › Trichocomaceae › Emericella |
Protein attributes
| Sequence length | 3770 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
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 Potential. |
| Pathway | |
| Post-translational modification | The N-terminus is blocked. Glycosylated. |
| 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 |
| PTM | Glycoprotein |
| Technical term | Direct protein sequencing 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 – 3770 | 3770 | N-(5-amino-5-carboxypentanoyl)-L-cysteinyl-D-valine synthase | PRO_0000193057 | |||||
Regions | |||||||||
| Domain | 850 – 919 | 70 | Acyl carrier 1 | ||||||
| Domain | 1929 – 2002 | 74 | Acyl carrier 2 | ||||||
| Domain | 3020 – 3087 | 68 | Acyl carrier 3 | ||||||
| Region | 321 – 910 | 590 | Domain 1 (adipate-activating) | ||||||
| Region | 1413 – 1993 | 581 | Domain 2 (cysteine-activating) | ||||||
| Region | 2494 – 3078 | 585 | Domain 3 (valine-activating) | ||||||
Sites | |||||||||
| Active site | 3623 | 1 | For thioesterase activity By similarity | ||||||
Amino acid modifications | |||||||||
| Modified residue | 882 | 1 | O-(pantetheine 4'-phosphoryl)serine By similarity | ||||||
| Modified residue | 1965 | 1 | O-(pantetheine 4'-phosphoryl)serine By similarity | ||||||
| Modified residue | 3050 | 1 | O-(pantetheine 4'-phosphoryl)serine By similarity | ||||||
| Glycosylation | 88 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 309 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 570 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 596 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 638 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 639 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 655 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 787 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1256 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1402 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1545 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 1735 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 2410 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 3130 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 3298 | 1 | N-linked (GlcNAc...) Potential | ||||||
| Glycosylation | 3332 | 1 | N-linked (GlcNAc...) Potential | ||||||
Experimental info | |||||||||
| Sequence conflict | 1941 | 1 | W → S AAA03914/CAA38631/AA sequence Ref.1 | ||||||
| Sequence conflict | 2177 – 2178 | 2 | NE → KQ in AAA03914. Ref.1 | ||||||
| Sequence conflict | 2177 – 2178 | 2 | NE → KQ in CAA38631. Ref.1 | ||||||
| Sequence conflict | 2335 | 1 | A → P in AAA03914. Ref.1 | ||||||
| Sequence conflict | 2335 | 1 | A → P in CAA38631. Ref.1 | ||||||
| Sequence conflict | 2869 | 1 | S → C in AAA03914. Ref.1 | ||||||
| Sequence conflict | 2869 | 1 | S → C in CAA38631. Ref.1 | ||||||
| Sequence conflict | 3116 | 1 | T → I AAA03914/CAA38631/AA sequence Ref.1 | ||||||
| Sequence conflict | 3139 | 1 | E → D in CAA38631. Ref.1 | ||||||
Sequences
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References
| « Hide 'large scale' references | |
| [1] | "Delta-(L-alpha-aminoadipyl)-L-cysteinyl-D-valine synthetase from Aspergillus nidulans. Molecular characterization of the acvA gene encoding the first enzyme of the penicillin biosynthetic pathway." Maccabe A.P., van Liempt H., Pallissa H., Unkles S.E., Riach M.B.R., Pfeifer E., von Doehren H., Kinghorn J.R. J. Biol. Chem. 266:12646-12654(1991) [PubMed: 2061333] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 547-561; 944-979; 1928-1944; 2396-2419 AND 3102-3118, GLYCOSYLATION. Strain: G191. |
| [2] | "Sequencing of Aspergillus nidulans and comparative analysis with A. fumigatus and A. oryzae." Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S., Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V., Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S., Braus G.H.  Birren B.W.Nature 438:1105-1115(2005) [PubMed: 16372000] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: FGSC 4. |
Cross-references
Sequence databases | |
|---|---|
| S40212 Genomic DNA. Translation: AAA03914.1. X54853 Genomic DNA. Translation: CAA38631.1. AACD01000045 Genomic DNA. Translation: EAA62968.1. | |
| PIR | A40889. |
3D structure databases | |
| HSSP | HSSP built from PDB template 1AMU based on UniProtKB P14687. |
| ModBase | Search... |
Enzyme and pathway databases | |
| BRENDA | 6.3.2.26. 3859. |
Family and domain databases | |
| PROSITE | PS50075. ACP_DOMAIN. 3 hits. PS00455. AMP_BINDING. 3 hits. PS00012. PHOSPHOPANTETHEINE. 3 hits. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | ACVS_EMENI | ||||||||
| Accession | Primary (citable) accession number: P27742 Secondary accession number(s): Q4J6A8, Q5BA09 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | FPAP (Fungal Proteome Annotation Project) | ||||||||
Relevant documents
| PATHWAY comments Index of metabolic and biosynthesis pathways |
| SIMILARITY comments Index of protein domains and families |
