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Protein

Tetrahedral aminopeptidase

Gene

frvX

Organism
Pyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

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

Cofactori

Zn2+3 Publications, Co2+3 PublicationsNote: Binds 2 Zn2+ ions per subunit. Can also use Co2+.3 Publications

Enzyme 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 keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi68Zinc 11
Metal bindingi182Zinc 11
Metal bindingi182Zinc 21
Active sitei212Proton acceptor2 Publications1
Metal bindingi213Zinc 21
Metal bindingi235Zinc 11
Metal bindingi323Zinc 21

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Cobalt, Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi3.4.11.1. 5244.
3.4.11.B4. 5244.

Protein family/group databases

MEROPSiM42.004.

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
OrganismiPyrococcus horikoshii (strain ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3)
Taxonomic identifieri70601 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
Proteomesi
  • UP000000752 Componenti: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00003910121 – 353Tetrahedral aminopeptidaseAdd BLAST353

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 Publications

Protein-protein interaction databases

STRINGi70601.PH1527.

Structurei

Secondary structure

1353
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi9 – 17Combined sources9
Helixi25 – 27Combined sources3
Helixi29 – 37Combined sources9
Helixi38 – 40Combined sources3
Beta strandi41 – 46Combined sources6
Beta strandi52 – 56Combined sources5
Beta strandi62 – 68Combined sources7
Beta strandi73 – 79Combined sources7
Beta strandi85 – 92Combined sources8
Helixi95 – 97Combined sources3
Turni98 – 100Combined sources3
Beta strandi102 – 108Combined sources7
Beta strandi111 – 118Combined sources8
Helixi136 – 138Combined sources3
Beta strandi140 – 142Combined sources3
Helixi148 – 153Combined sources6
Beta strandi161 – 164Combined sources4
Beta strandi169 – 171Combined sources3
Turni172 – 174Combined sources3
Beta strandi175 – 178Combined sources4
Helixi181 – 196Combined sources16
Beta strandi201 – 210Combined sources10
Turni213 – 215Combined sources3
Helixi217 – 226Combined sources10
Beta strandi229 – 238Combined sources10
Helixi247 – 249Combined sources3
Beta strandi258 – 264Combined sources7
Helixi271 – 283Combined sources13
Beta strandi288 – 292Combined sources5
Helixi300 – 303Combined sources4
Beta strandi312 – 321Combined sources10
Beta strandi323 – 325Combined sources3
Beta strandi327 – 330Combined sources4
Helixi331 – 347Combined sources17
Helixi348 – 350Combined sources3

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XFOX-ray1.96A/B/C/D1-353[»]
1Y0RX-ray1.75A1-353[»]
1Y0YX-ray1.60A1-353[»]
ProteinModelPortaliO59196.
SMRiO59196.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO59196.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M42 family.Curated

Phylogenomic databases

eggNOGiarCOG01518. Archaea.
COG1363. LUCA.
HOGENOMiHOG000291972.
KOiK20608.
OMAiICHPTIV.

Family and domain databases

Gene3Di2.40.30.40. 1 hit.
InterProiIPR008007. Peptidase_M42.
IPR023367. Peptidase_M42_dom2.
[Graphical view]
PfamiPF05343. Peptidase_M42. 1 hit.
[Graphical view]
PIRSFiPIRSF001123. PepA_GA. 1 hit.

Sequencei

Sequence statusi: Complete.

O59196-1 [UniParc]FASTAAdd to basket

« Hide

        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
Length:353
Mass (Da):39,014
Last modified:August 1, 1998 - v1
Checksum:iA6AE25809C8B2041
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA30637.1.
PIRiE71029.

Genome annotation databases

EnsemblBacteriaiBAA30637; BAA30637; BAA30637.
KEGGipho:PH1527.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
BA000001 Genomic DNA. Translation: BAA30637.1.
PIRiE71029.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1XFOX-ray1.96A/B/C/D1-353[»]
1Y0RX-ray1.75A1-353[»]
1Y0YX-ray1.60A1-353[»]
ProteinModelPortaliO59196.
SMRiO59196.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi70601.PH1527.

Protein family/group databases

MEROPSiM42.004.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiBAA30637; BAA30637; BAA30637.
KEGGipho:PH1527.

Phylogenomic databases

eggNOGiarCOG01518. Archaea.
COG1363. LUCA.
HOGENOMiHOG000291972.
KOiK20608.
OMAiICHPTIV.

Enzyme and pathway databases

BRENDAi3.4.11.1. 5244.
3.4.11.B4. 5244.

Miscellaneous databases

EvolutionaryTraceiO59196.

Family and domain databases

Gene3Di2.40.30.40. 1 hit.
InterProiIPR008007. Peptidase_M42.
IPR023367. Peptidase_M42_dom2.
[Graphical view]
PfamiPF05343. Peptidase_M42. 1 hit.
[Graphical view]
PIRSFiPIRSF001123. PepA_GA. 1 hit.
ProtoNetiSearch...

Entry informationi

Entry nameiTET_PYRHO
AccessioniPrimary (citable) accession number: O59196
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 9, 2010
Last sequence update: August 1, 1998
Last modified: November 2, 2016
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

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.

Keywords - Technical termi

3D-structure, Complete proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. Peptidase families
    Classification of peptidase families and list of entries
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.