Reviewed,
UniProtKB/Swiss-Prot Q05053 (PAC1_PSESV)
Last modified
February 9, 2010.
Version 48.
History...
Clusters with 100%,
90%,
50% identity |
Documents (1) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Acylase ACY 1 Cleaved into the following 2 chains: 1- Recommended name: Acylase ACY 1 large subunit 2- Recommended name: Acylase ACY 1 small subunit Including the following 2 domains: 1- Recommended name: Cephalosporin acylase EC=3.5.1.- Alternative name(s): GL-7ACA acylase 2- Recommended name: Gamma-glutamyltranspeptidase Short name=GGT EC=2.3.2.2 | ||
| Gene names |
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| Organism | Pseudomonas sp. (strain V22) | ||
| Taxonomic identifier | 33068 [NCBI] | ||
| Taxonomic lineage | Bacteria › Proteobacteria |
Protein attributes
| Sequence length | 558 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 | Besides the cephalosporin acylase I activity which converts GL-7ACA into 7-ACA; this enzyme displays some gamma glutamyltranspeptidase activity. |
| Catalytic activity | 7-beta-(4-carboxybutanamido)-cephalosporanic acid + H2O = 7-aminocephalosporanic acid + glutaric acid. (5-L-glutamyl)-peptide + an amino acid = peptide + 5-L-glutamyl amino acid. |
| Subunit structure | Dimer of two non-identical chains processed from the same precursor. |
| Sequence similarities | Belongs to the gamma-glutamyltransferase family. |
Ontologies
| Keywords | |
|---|---|
| Biological process | Antibiotic resistance |
| Molecular function | Acyltransferase Hydrolase Transferase |
| PTM | Zymogen |
| Technical term | Direct protein sequencing |
| Gene Ontology (GO) | |
| Biological process | response to antibiotic Inferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | acyltransferase activity Inferred from electronic annotation. Source: UniProtKB-KW gamma-glutamyltransferase activityInferred from electronic annotation. Source: EC hydrolase activityInferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Sequence annotation (Features)
Sequences
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References
| [1] | "Nucleotide sequence and expression in Escherichia coli of the cephalosporin acylase gene of a Pseudomonas strain." Ishiye M., Niwa M. Biochim. Biophys. Acta 1132:233-239(1992) [PubMed: 1358202] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-13 AND 368-381. |
Cross-references
Sequence databases | |
|---|---|
| EMBL GenBank DDBJ | X69020 Genomic DNA. Translation: CAA48785.1. |
| PIR | S27199. |
3D structure databases | |
| SMR | Q05053. Positions 16-375. |
| ModBase | Search... |
Protein family/group databases | |
| MEROPS | T03.001. |
Family and domain databases | |
| InterPro | IPR000101. GGT_peptidase. [Graphical view] |
| PANTHER | PTHR11686. GGT_peptidase. 1 hit. |
| Pfam | PF01019. G_glu_transpept. 1 hit. [Graphical view] |
| PRINTS | PR01210. GGTRANSPTASE. |
| TIGRFAMs | TIGR00066. g_glut_trans. 1 hit. |
| PROSITE | PS00462. G_GLU_TRANSPEPTIDASE. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | PAC1_PSESV | ||||||||
| Accession | Primary (citable) accession number: Q05053 | ||||||||
| Entry history |
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| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||

Clusters with


