Reviewed,
UniProtKB/Swiss-Prot P45334 (AMPA_HAEIN)
Last modified
November 24, 2009.
Version 71.
History...
Clusters with 100%,
90%,
50% identity |
Documents (4) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Cytosol aminopeptidase EC=3.4.11.1 Alternative name(s): Leucine aminopeptidase Short name=LAP Leucyl aminopeptidase | ||||
| Gene names |
| ||||
| Organism | Haemophilus influenzae [Complete proteome] [HAMAP] | ||||
| Taxonomic identifier | 727 [NCBI] | ||||
| Taxonomic lineage | Bacteria › Proteobacteria › Gammaproteobacteria › Pasteurellales › Pasteurellaceae › Haemophilus |
Protein attributes
| Sequence length | 491 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Inferred from homology. |
General annotation (Comments)
| Function | Presumably involved in the processing and regular turnover of intracellular proteins. Catalyzes the removal of unsubstituted N-terminal amino acids from various peptides By similarity. |
| Catalytic activity | Release of an N-terminal amino acid, Xaa-|-Yaa-, in which Xaa is preferably Leu, but may be other amino acids including Pro although not Arg or Lys, and Yaa may be Pro. Amino acid amides and methyl esters are also readily hydrolyzed, but rates on arylamides are exceedingly low. HAMAP MF_00181 |
| Cofactor | Binds 2 manganese ions per subunit By similarity. |
| Subcellular location | Cytoplasm By similarity. |
| Sequence similarities | Belongs to the peptidase M17 family. |
Ontologies
| Keywords | |
|---|---|
| Cellular component | Cytoplasm |
| Ligand | Manganese Metal-binding |
| Molecular function | Aminopeptidase Hydrolase Protease |
| Technical term | Complete proteome |
| Gene Ontology (GO) | |
| Biological process | proteolysis Inferred from electronic annotation. Source: InterPro |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell |
| Molecular function | aminopeptidase activity Inferred from electronic annotation. Source: HAMAP manganese ion bindingInferred from electronic annotation. Source: HAMAP metalloexopeptidase activityInferred from electronic annotation. Source: HAMAP |
| Complete GO annotation... | |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 491 | 491 | Cytosol aminopeptidase HAMAP MF_00181 | PRO_0000165758 | |||||
Sites | |||||||||
| Active site | 275 | 1 | Potential | ||||||
| Active site | 349 | 1 | Potential | ||||||
| Metal binding | 263 | 1 | Manganese 2 By similarity | ||||||
| Metal binding | 268 | 1 | Manganese 1 By similarity | ||||||
| Metal binding | 268 | 1 | Manganese 2 By similarity | ||||||
| Metal binding | 286 | 1 | Manganese 2 By similarity | ||||||
| Metal binding | 345 | 1 | Manganese 1 By similarity | ||||||
| Metal binding | 347 | 1 | Manganese 1 By similarity | ||||||
| Metal binding | 347 | 1 | Manganese 2 By similarity | ||||||
Sequences
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References
| [1] | "Whole-genome random sequencing and assembly of Haemophilus influenzae Rd." Fleischmann R.D., Adams M.D., White O., Clayton R.A., Kirkness E.F., Kerlavage A.R., Bult C.J., Tomb J.-F., Dougherty B.A., Merrick J.M., McKenney K., Sutton G.G., FitzHugh W., Fields C.A., Gocayne J.D., Scott J.D., Shirley R., Liu L.-I. Venter J.C.Science 269:496-512(1995) [PubMed: 7542800] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC 51907 / DSM 11121 / KW20 / Rd. |
Cross-references
Sequence databases | |
|---|---|
| L42023 Genomic DNA. Translation: AAC23351.1. | |
| PIR | C64137. |
| RefSeq | NP_439847.1. |
3D structure databases | |
| ModBase | Search... |
Genome annotation databases | |
| GeneID | 949712. |
| GenomeReviews | Gene locus HI1705 in contig L42023_GR. |
| KEGG | hin:HI1705. |
| NMPDR | fig|71421.1.peg.1618. |
| TIGR | HI1705. |
Phylogenomic databases | |
| HOGENOM | P45334. |
| OMA | LGHHISG |
Enzyme and pathway databases | |
| BioCyc | HINF71421:HI_1705-MON. |
| BRENDA | 3.4.11.1. 109. |
Family and domain databases | |
| HAMAP | MF_00181. [Tree] |
| InterPro | IPR011356. Peptidase_M17. IPR000819. Peptidase_M17_C. IPR008283. Peptidase_M17_N. [Graphical view] |
| PANTHER | PTHR11963:SF3. Peptidase_M17. 1 hit. |
| Pfam | PF00883. Peptidase_M17. 1 hit. PF02789. Peptidase_M17_N. 1 hit. [Graphical view] |
| PRINTS | PR00481. LAMNOPPTDASE. |
| PROSITE | PS00631. CYTOSOL_AP. 1 hit. [Graphical view] |
| ProtoNet | Search... |
Entry information
| Entry name | AMPA_HAEIN | ||||||||
| Accession | Primary (citable) accession number: P45334 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HAMAP (High-quality Automated and Manual Annotation of microbial Proteomes) | ||||||||
Relevant documents
| UniProtKB/Swiss-Prot annotation A primer on UniProtKB/Swiss-Prot annotation |
| Haemophilus influenzae Haemophilus influenzae (strain Rd): entries and gene names |
| Peptidase families Classification of peptidase families and list of entries |
| SIMILARITY comments Index of protein domains and families |

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