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Protein

Xaa-Pro dipeptidase

Gene

pepQ

Organism
Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Splits dipeptides with a prolyl in the C-terminal position and a nonpolar amino acid at the N-terminal position.1 Publication

Catalytic activityi

Hydrolysis of Xaa-|-Pro dipeptides; also acts on aminoacyl-hydroxyproline analogs. No action on Pro-|-Pro.

Cofactori

Co2+1 Publication, Mn2+1 PublicationNote: Binds 2 cobalt ions per subunit. Co2+ can be replaced by Mn2+, resulting in a 25% decrease in activity, but not by Mg2+, Ca2+, Fe2+, Zn2+, Cu2+, or Ni2+.1 Publication

Kineticsi

  1. KM=2.8 mM for Met-Pro1 Publication
  2. KM=3 mM for Leu-Pro1 Publication
  3. KM=4.2 mM for Val-Pro1 Publication
  4. KM=8.3 mM for Ala-Pro1 Publication
  5. KM=20 mM for Phe-Pro1 Publication
  1. Vmax=645 µmol/min/mg enzyme with Met-Pro as substrate1 Publication
  2. Vmax=645 µmol/min/mg enzyme with Leu-Pro as substrate1 Publication
  3. Vmax=175 µmol/min/mg enzyme with Val-Pro as substrate1 Publication
  4. Vmax=250 µmol/min/mg enzyme with Ala-Pro as substrate1 Publication
  5. Vmax=1000 µmol/min/mg enzyme with Phe-Pro as substrate1 Publication

pH dependencei

Optimum pH is 7.0.1 Publication

Temperature dependencei

Optimum temperature is 100 degrees Celsius. Highly thermostable.1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi209 – 2091Cobalt 2
Metal bindingi220 – 2201Cobalt 1
Metal bindingi220 – 2201Cobalt 2
Metal bindingi284 – 2841Cobalt 1
Metal bindingi313 – 3131Cobalt 1
Metal bindingi327 – 3271Cobalt 1
Metal bindingi327 – 3271Cobalt 2

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Dipeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Cobalt, Metal-binding

Enzyme and pathway databases

BRENDAi3.4.13.9. 5243.

Protein family/group databases

MEROPSiM24.008.

Names & Taxonomyi

Protein namesi
Recommended name:
Xaa-Pro dipeptidase (EC:3.4.13.9)
Short name:
X-Pro dipeptidase
Alternative name(s):
Imidodipeptidase
Proline dipeptidase
Short name:
Prolidase
Gene namesi
Name:pepQ
Ordered Locus Names:PF1343
OrganismiPyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)
Taxonomic identifieri186497 [NCBI]
Taxonomic lineageiArchaeaEuryarchaeotaThermococciThermococcalesThermococcaceaePyrococcus
Proteomesi
  • UP000001013 Componenti: Chromosome

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi209 – 2091D → A: 1300-fold reduction in activity. 1 Publication
Mutagenesisi284 – 2841H → A or L: 2000-fold reduction in activity. 1 Publication
Mutagenesisi327 – 3271E → L: Loss of activity. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 348348Xaa-Pro dipeptidasePRO_0000185093Add
BLAST

Proteomic databases

PRIDEiP81535.

Interactioni

Subunit structurei

Homodimer.2 Publications

Protein-protein interaction databases

STRINGi186497.PF1343.

Structurei

Secondary structure

1
348
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi9 – 146Combined sources
Beta strandi19 – 224Combined sources
Helixi25 – 328Combined sources
Beta strandi41 – 455Combined sources
Beta strandi48 – 547Combined sources
Helixi55 – 573Combined sources
Helixi58 – 647Combined sources
Beta strandi69 – 746Combined sources
Helixi77 – 815Combined sources
Turni82 – 843Combined sources
Beta strandi86 – 905Combined sources
Helixi96 – 1049Combined sources
Beta strandi110 – 1134Combined sources
Helixi115 – 1228Combined sources
Helixi127 – 15024Combined sources
Helixi157 – 17014Combined sources
Beta strandi174 – 1785Combined sources
Beta strandi181 – 1844Combined sources
Helixi185 – 1895Combined sources
Beta strandi205 – 2106Combined sources
Beta strandi212 – 2143Combined sources
Beta strandi221 – 2299Combined sources
Helixi232 – 25120Combined sources
Helixi258 – 27114Combined sources
Helixi275 – 2773Combined sources
Beta strandi282 – 2854Combined sources
Beta strandi287 – 29711Combined sources
Beta strandi309 – 3124Combined sources
Beta strandi315 – 3184Combined sources
Turni319 – 3213Combined sources
Beta strandi322 – 3254Combined sources
Beta strandi327 – 3326Combined sources
Beta strandi334 – 3407Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PV9X-ray2.00A/B1-348[»]
ProteinModelPortaliP81535.
SMRiP81535. Positions 8-345.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP81535.

Family & Domainsi

Sequence similaritiesi

Phylogenomic databases

eggNOGiarCOG01000. Archaea.
COG0006. LUCA.
HOGENOMiHOG000008760.
KOiK01271.
OMAiPNFSMLI.

Family and domain databases

Gene3Di3.40.350.10. 1 hit.
3.90.230.10. 1 hit.
InterProiIPR029149. Creatin/AminoP/Spt16_NTD.
IPR028980. Creatinase/Aminopeptidase_P_N.
IPR000587. Creatinase_N.
IPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR001131. Peptidase_M24B_aminopep-P_CS.
[Graphical view]
PfamiPF01321. Creatinase_N. 1 hit.
PF00557. Peptidase_M24. 1 hit.
[Graphical view]
PRINTSiPR00599. MAPEPTIDASE.
SUPFAMiSSF53092. SSF53092. 1 hit.
SSF55920. SSF55920. 1 hit.
PROSITEiPS00491. PROLINE_PEPTIDASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P81535-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKERLEKLVK FMDENSIDRV FIAKPVNVYY FSGTSPLGGG YIIVDGDEAT
60 70 80 90 100
LYVPELEYEM AKEESKLPVV KFKKFDEIYE ILKNTETLGI EGTLSYSMVE
110 120 130 140 150
NFKEKSNVKE FKKIDDVIKD LRIIKTKEEI EIIEKACEIA DKAVMAAIEE
160 170 180 190 200
ITEGKREREV AAKVEYLMKM NGAEKPAFDT IIASGHRSAL PHGVASDKRI
210 220 230 240 250
ERGDLVVIDL GALYNHYNSD ITRTIVVGSP NEKQREIYEI VLEAQKRAVE
260 270 280 290 300
AAKPGMTAKE LDSIAREIIK EYGYGDYFIH SLGHGVGLEI HEWPRISQYD
310 320 330 340
ETVLKEGMVI TIEPGIYIPK LGGVRIEDTV LITENGAKRL TKTERELL
Length:348
Mass (Da):39,387
Last modified:November 1, 1998 - v1
Checksum:i6BA956FAA9C18FB5
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF060010 Genomic DNA. Translation: AAC61259.1.
AE009950 Genomic DNA. Translation: AAL81467.1.
PIRiT46973.
RefSeqiWP_011012489.1. NC_003413.1.

Genome annotation databases

EnsemblBacteriaiAAL81467; AAL81467; PF1343.
GeneIDi1469218.
KEGGipfu:PF1343.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF060010 Genomic DNA. Translation: AAC61259.1.
AE009950 Genomic DNA. Translation: AAL81467.1.
PIRiT46973.
RefSeqiWP_011012489.1. NC_003413.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1PV9X-ray2.00A/B1-348[»]
ProteinModelPortaliP81535.
SMRiP81535. Positions 8-345.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi186497.PF1343.

Protein family/group databases

MEROPSiM24.008.

Proteomic databases

PRIDEiP81535.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblBacteriaiAAL81467; AAL81467; PF1343.
GeneIDi1469218.
KEGGipfu:PF1343.

Phylogenomic databases

eggNOGiarCOG01000. Archaea.
COG0006. LUCA.
HOGENOMiHOG000008760.
KOiK01271.
OMAiPNFSMLI.

Enzyme and pathway databases

BRENDAi3.4.13.9. 5243.

Miscellaneous databases

EvolutionaryTraceiP81535.

Family and domain databases

Gene3Di3.40.350.10. 1 hit.
3.90.230.10. 1 hit.
InterProiIPR029149. Creatin/AminoP/Spt16_NTD.
IPR028980. Creatinase/Aminopeptidase_P_N.
IPR000587. Creatinase_N.
IPR001714. Pept_M24_MAP.
IPR000994. Pept_M24_structural-domain.
IPR001131. Peptidase_M24B_aminopep-P_CS.
[Graphical view]
PfamiPF01321. Creatinase_N. 1 hit.
PF00557. Peptidase_M24. 1 hit.
[Graphical view]
PRINTSiPR00599. MAPEPTIDASE.
SUPFAMiSSF53092. SSF53092. 1 hit.
SSF55920. SSF55920. 1 hit.
PROSITEiPS00491. PROLINE_PEPTIDASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of native and recombinant forms of an unusual cobalt-dependent proline dipeptidase (Prolidase) from the hyperthermophilic archaeon Pyrococcus furiosus."
    Ghosh M., Grunden A.M., Dunn D.M., Weiss R., Adams M.W.W.
    J. Bacteriol. 180:4781-4789(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 1-15, FUNCTION, COFACTOR, SUBUNIT, BIOPHYSICOCHEMICAL PROPERTIES.
    Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
  2. "Divergence of the hyperthermophilic archaea Pyrococcus furiosus and P. horikoshii inferred from complete genomic sequences."
    Maeder D.L., Weiss R.B., Dunn D.M., Cherry J.L., Gonzalez J.M., DiRuggiero J., Robb F.T.
    Genetics 152:1299-1305(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
  3. "Crystallization and characterization of the prolidase from Pyrococcus furiosus."
    Willingham K., Maher M.J., Grunden A.M., Ghosh M., Adams M.W.W., Freeman H.C., Guss J.M.
    Acta Crystallogr. D 57:428-430(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: CRYSTALLIZATION.
    Strain: ATCC 43587 / DSM 3638 / JCM 8422 / Vc1.
  4. "Proline dipeptidase from Pyrococcus furiosus."
    Grunden A.M., Ghosh M., Adams M.W.W.
    Methods Enzymol. 330:433-445(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW.
  5. "Characterization of the dinuclear metal center of Pyrococcus furiosus prolidase by analysis of targeted mutants."
    Du X., Tove S., Kast-Hutcheson K., Grunden A.M.
    FEBS Lett. 579:6140-6146(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: MUTAGENESIS OF ASP-209; HIS-284 AND GLU-327.
  6. Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) IN COMPLEX WITH ZINC IONS.

Entry informationi

Entry nameiPEPQ_PYRFU
AccessioniPrimary (citable) accession number: P81535
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 26, 2001
Last sequence update: November 1, 1998
Last modified: May 11, 2016
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Miscellaneous

Cobalt 1 is the tight-binding and cobalt 2 is the loose-binding metal center.

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference 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.