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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)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi68 – 681Zinc 1
Metal bindingi182 – 1821Zinc 1
Metal bindingi182 – 1821Zinc 2
Active sitei212 – 2121Proton acceptor2 Publications
Metal bindingi213 – 2131Zinc 2
Metal bindingi235 – 2351Zinc 1
Metal bindingi323 – 3231Zinc 2

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Aminopeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Cobalt, Metal-binding, Zinc

Enzyme and pathway databases

BioCyciPHOR70601:GJWR-1528-MONOMER.
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)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 353353Tetrahedral aminopeptidasePRO_0000391012Add
BLAST

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

1
353
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 179Combined sources
Helixi25 – 273Combined sources
Helixi29 – 379Combined sources
Helixi38 – 403Combined sources
Beta strandi41 – 466Combined sources
Beta strandi52 – 565Combined sources
Beta strandi62 – 687Combined sources
Beta strandi73 – 797Combined sources
Beta strandi85 – 928Combined sources
Helixi95 – 973Combined sources
Turni98 – 1003Combined sources
Beta strandi102 – 1087Combined sources
Beta strandi111 – 1188Combined sources
Helixi136 – 1383Combined sources
Beta strandi140 – 1423Combined sources
Helixi148 – 1536Combined sources
Beta strandi161 – 1644Combined sources
Beta strandi169 – 1713Combined sources
Turni172 – 1743Combined sources
Beta strandi175 – 1784Combined sources
Helixi181 – 19616Combined sources
Beta strandi201 – 21010Combined sources
Turni213 – 2153Combined sources
Helixi217 – 22610Combined sources
Beta strandi229 – 23810Combined sources
Helixi247 – 2493Combined sources
Beta strandi258 – 2647Combined sources
Helixi271 – 28313Combined sources
Beta strandi288 – 2925Combined sources
Helixi300 – 3034Combined sources
Beta strandi312 – 32110Combined sources
Beta strandi323 – 3253Combined sources
Beta strandi327 – 3304Combined sources
Helixi331 – 34717Combined sources
Helixi348 – 3503Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiO59196.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M42 family.Curated

Phylogenomic databases

eggNOGiarCOG01518. Archaea.
COG1363. LUCA.
HOGENOMiHOG000291972.
KOiK01179.
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
EntryMethodResolution (Å)ChainPositionsPDBsum
1XFOX-ray1.96A/B/C/D1-353[»]
1Y0RX-ray1.75A1-353[»]
1Y0YX-ray1.60A1-353[»]
ProteinModelPortaliO59196.
SMRiO59196. Positions 1-353.
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.
KOiK01179.
OMAiICHPTIV.

Enzyme and pathway databases

BioCyciPHOR70601:GJWR-1528-MONOMER.
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...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 700860 / DSM 12428 / JCM 9974 / NBRC 100139 / OT-3.
  2. "Characterization of a TET-like aminopeptidase complex from the hyperthermophilic archaeon Pyrococcus horikoshii."
    Dura M.A., Receveur-Brechot V., Andrieu J.P., Ebel C., Schoehn G., Roussel A., Franzetti B.
    Biochemistry 44:3477-3486(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS AN AMINOPEPTIDASE, CATALYTIC ACTIVITY, COFACTOR, SUBSTRATE SPECIFICITY, ENZYME REGULATION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, REACTION MECHANISM.
  3. "Crystal structure of a dodecameric tetrahedral-shaped aminopeptidase."
    Russo S., Baumann U.
    J. Biol. Chem. 279:51275-51281(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.96 ANGSTROMS) IN COMPLEX WITH ZINC IONS, FUNCTION AS AN AMINOPEPTIDASE, CATALYTIC ACTIVITY, COFACTOR, SUBUNIT, ACTIVE SITE, CATALYTIC MECHANISM.
  4. "Crystal structure of TET protease reveals complementary protein degradation pathways in prokaryotes."
    Borissenko L., Groll M.
    J. Mol. Biol. 346:1207-1219(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.6 ANGSTROMS) IN COMPLEXES WITH ZINC IONS AND THE INHIBITOR AMASTATIN, FUNCTION IN PROTEIN DEGRADATION, COFACTOR, SUBUNIT, ACTIVE SITE, CATALYTIC MECHANISM.

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 11, 2015
This is version 83 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.