UniProtKB - O59196 (TET_PYRHO)
Protein
Tetrahedral aminopeptidase
Gene
frvX
Organism
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Status
Functioni
Functions as an aminopeptidase, with a clear preference for leucine as the N-terminal amino acid. However, can also cleave moderately long polypeptide substrates of various compositions in a fairly unspecific manner. Has neither carboxypeptidase nor endoproteolytic activities, and it is devoid of N-terminal deblocking activity. Is involved in protein degradation, performing degradation of oligopeptides produced by the proteasome into single amino acids.3 Publications
Miscellaneous
The hydrolytic mechanism is nonprocessive. Therefore, the enzyme does not process one substrate molecule completely before starting with another one. Instead, the reaction products are generated by multiple rounds of substrate digestion.
Cofactori
Zn2+3 Publications, Co2+3 PublicationsNote: Binds 2 Zn2+ ions per subunit. Can also use Co2+.3 Publications
Activity regulationi
Inhibited by EDTA and bestatin in vitro. Is insensitive to papain, antipain, chymostatin, leupeptin, pepstatin and aprotinin.1 Publication
pH dependencei
Optimum pH is 7.5 with Leu-pNA as substrate. Strong activity is still detectable at pH 6 and 9.1 Publication
Temperature dependencei
Optimum temperature is 100 degrees Celsius over a broad pH array. At temperatures lower than 70 degrees Celsius, less than 10% of the maximum activity is detected. Highly thermostable. Shows half-lives of 24.8 minutes and 10.03 hours when incubated at 100 and 80 degrees Celsius, respectively.1 Publication
Sites
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Metal bindingi | 68 | Zinc 1 | 1 | |
Metal bindingi | 182 | Zinc 1 | 1 | |
Metal bindingi | 182 | Zinc 2 | 1 | |
Active sitei | 212 | Proton acceptor2 Publications | 1 | |
Metal bindingi | 213 | Zinc 2 | 1 | |
Metal bindingi | 235 | Zinc 1 | 1 | |
Metal bindingi | 323 | Zinc 2 | 1 |
GO - Molecular functioni
- aminopeptidase activity Source: UniProtKB-KW
- metal ion binding Source: UniProtKB-KW
- metallopeptidase activity Source: UniProtKB-KW
Keywordsi
Molecular function | Aminopeptidase, Hydrolase, Metalloprotease, Protease |
Ligand | Cobalt, Metal-binding, Zinc |
Enzyme and pathway databases
BRENDAi | 3.4.11.1, 5244 3.4.11.B4, 5244 |
Protein family/group databases
MEROPSi | M42.004 |
Names & Taxonomyi
Protein namesi | Recommended name: Tetrahedral aminopeptidase (EC:3.4.11.-)Short name: TET Short name: TET aminopeptidase Alternative name(s): Leucyl aminopeptidase PhTET2 |
Gene namesi | Name:frvX Ordered Locus Names:PH1527 |
Organismi | Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3) |
Taxonomic identifieri | 70601 [NCBI] |
Taxonomic lineagei | Archaea › Euryarchaeota › Thermococci › Thermococcales › Thermococcaceae › Pyrococcus › |
Proteomesi |
|
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000391012 | 1 – 353 | Tetrahedral aminopeptidaseAdd BLAST | 353 |
Interactioni
Subunit structurei
Homododecamer. The assembly of six dimers results in a tetrahedral-shaped structure; all 12 active sites are located on the inside of the tetrahedron. Substrate access is granted by four pores with a maximal diameter of 18 Angstroms, allowing only small peptides and unfolded proteins access to the active site. Beside the four entry ports, TET contains 12 small product release openings, which are large enough to allow passage of only single amino acid residues.
3 PublicationsProtein-protein interaction databases
STRINGi | 70601.3257954 |
Structurei
Secondary structure
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details3D structure databases
BMRBi | O59196 |
SMRi | O59196 |
ModBasei | Search... |
PDBe-KBi | Search... |
Miscellaneous databases
EvolutionaryTracei | O59196 |
Family & Domainsi
Sequence similaritiesi
Belongs to the peptidase M42 family.Curated
Phylogenomic databases
eggNOGi | arCOG01518, Archaea |
OMAi | GGFMIAE |
Family and domain databases
Gene3Di | 2.40.30.40, 1 hit |
InterProi | View protein in InterPro IPR008007, Peptidase_M42 IPR023367, Peptidase_M42_dom2 |
Pfami | View protein in Pfam PF05343, Peptidase_M42, 1 hit |
PIRSFi | PIRSF001123, PepA_GA, 1 hit |
i Sequence
Sequence statusi: Complete.
O59196-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MEVRNMVDYE LLKKVVEAPG VSGYEFLGIR DVVIEEIKDY VDEVKVDKLG
60 70 80 90 100
NVIAHKKGEG PKVMIAAHMD QIGLMVTHIE KNGFLRVAPI GGVDPKTLIA
110 120 130 140 150
QRFKVWIDKG KFIYGVGASV PPHIQKPEDR KKAPDWDQIF IDIGAESKEE
160 170 180 190 200
AEDMGVKIGT VITWDGRLER LGKHRFVSIA FDDRIAVYTI LEVAKQLKDA
210 220 230 240 250
KADVYFVATV QEEVGLRGAR TSAFGIEPDY GFAIDVTIAA DIPGTPEHKQ
260 270 280 290 300
VTHLGKGTAI KIMDRSVICH PTIVRWLEEL AKKHEIPYQL EILLGGGTDA
310 320 330 340 350
GAIHLTKAGV PTGALSVPAR YIHSNTEVVD ERDVDATVEL MTKALENIHE
LKI
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BA000001 Genomic DNA Translation: BAA30637.1 |
PIRi | E71029 |
Genome annotation databases
EnsemblBacteriai | BAA30637; BAA30637; BAA30637 |
KEGGi | pho:PH1527 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BA000001 Genomic DNA Translation: BAA30637.1 |
PIRi | E71029 |
3D structure databases
Select the link destinations: PDBei RCSB PDBi PDBji Links Updated | PDB entry | Method | Resolution (Å) | Chain | Positions | PDBsum |
1XFO | X-ray | 1.96 | A/B/C/D | 1-353 | [»] | |
1Y0R | X-ray | 1.75 | A | 1-353 | [»] | |
1Y0Y | X-ray | 1.60 | A | 1-353 | [»] | |
6F3K | Other | 4.10 | A | 1-353 | [»] | |
6R8N | Other | 4.10 | A/B/C/D/E/F/G/H/I/J/K/L | 1-353 | [»] | |
BMRBi | O59196 | |||||
SMRi | O59196 | |||||
ModBasei | Search... | |||||
PDBe-KBi | Search... |
Protein-protein interaction databases
STRINGi | 70601.3257954 |
Protein family/group databases
MEROPSi | M42.004 |
Genome annotation databases
EnsemblBacteriai | BAA30637; BAA30637; BAA30637 |
KEGGi | pho:PH1527 |
Phylogenomic databases
eggNOGi | arCOG01518, Archaea |
OMAi | GGFMIAE |
Enzyme and pathway databases
BRENDAi | 3.4.11.1, 5244 3.4.11.B4, 5244 |
Miscellaneous databases
EvolutionaryTracei | O59196 |
Family and domain databases
Gene3Di | 2.40.30.40, 1 hit |
InterProi | View protein in InterPro IPR008007, Peptidase_M42 IPR023367, Peptidase_M42_dom2 |
Pfami | View protein in Pfam PF05343, Peptidase_M42, 1 hit |
PIRSFi | PIRSF001123, PepA_GA, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | TET_PYRHO | |
Accessioni | O59196Primary (citable) accession number: O59196 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | February 9, 2010 |
Last sequence update: | August 1, 1998 | |
Last modified: | December 2, 2020 | |
This is version 104 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Prokaryotic Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
3D-structureDocuments
- PDB cross-references
Index of Protein Data Bank (PDB) cross-references - SIMILARITY comments
Index of protein domains and families - Peptidase families
Classification of peptidase families and list of entries