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Protein

Beta-Ala-Xaa dipeptidase

Gene

pepV

Organism
Lactobacillus delbrueckii subsp. lactis
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Is a relatively unspecific dipeptidase cleaving a variety of dipeptides, notably those with an N-terminal beta-Ala or D-Ala residue, e.g. carnosine (beta-Ala-His). To a lesser extent, also shows aminopeptidase activity, since it is able to catalyze the removal of the N-terminal amino acid from a few distinct tripeptides.1 Publication

Cofactori

Zn2+1 PublicationNote: Binds 2 Zn2+ ions per subunit. These two catalytic ions are both involved in the stabilization of the tetrahedral intermediate and in the activation of the catalytic water molecule.1 Publication

Enzyme regulationi

Fully inhibited by 1,10-phenanthroline or EDTA.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Metal bindingi87Zinc 21 Publication1
Active sitei89By similarity1
Metal bindingi119Zinc 11 Publication1
Metal bindingi119Zinc 21 Publication1
Active sitei153Proton acceptorCurated1
Metal bindingi154Zinc 11 Publication1
Metal bindingi177Zinc 21 Publication1
Binding sitei350Substrate1
Metal bindingi439Zinc 11 Publication1

GO - Molecular functioni

Complete GO annotation...

Keywords - Molecular functioni

Dipeptidase, Hydrolase, Metalloprotease, Protease

Keywords - Ligandi

Metal-binding, Zinc

Protein family/group databases

MEROPSiM20.004.

Names & Taxonomyi

Protein namesi
Recommended name:
Beta-Ala-Xaa dipeptidase (EC:3.4.13.-)
Alternative name(s):
Beta-Ala-His dipeptidase
Peptidase V
Gene namesi
Name:pepV
OrganismiLactobacillus delbrueckii subsp. lactis
Taxonomic identifieri29397 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesLactobacillaceaeLactobacillus

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001852761 – 470Beta-Ala-Xaa dipeptidaseAdd BLAST470

Structurei

Secondary structure

1470
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi5 – 10Combined sources6
Helixi13 – 24Combined sources12
Helixi32 – 34Combined sources3
Beta strandi37 – 39Combined sources3
Helixi43 – 58Combined sources16
Beta strandi62 – 66Combined sources5
Turni67 – 69Combined sources3
Beta strandi70 – 75Combined sources6
Beta strandi79 – 87Combined sources9
Beta strandi111 – 114Combined sources4
Beta strandi117 – 120Combined sources4
Helixi121 – 137Combined sources17
Beta strandi142 – 151Combined sources10
Turni153 – 156Combined sources4
Helixi158 – 166Combined sources9
Beta strandi171 – 186Combined sources16
Beta strandi188 – 196Combined sources9
Beta strandi204 – 212Combined sources9
Beta strandi221 – 228Combined sources8
Helixi232 – 246Combined sources15
Beta strandi249 – 255Combined sources7
Beta strandi258 – 264Combined sources7
Helixi273 – 275Combined sources3
Helixi279 – 287Combined sources9
Helixi294 – 305Combined sources12
Turni306 – 309Combined sources4
Turni314 – 317Combined sources4
Turni323 – 325Combined sources3
Beta strandi329 – 338Combined sources10
Beta strandi343 – 351Combined sources9
Helixi357 – 368Combined sources12
Turni369 – 371Combined sources3
Beta strandi372 – 375Combined sources4
Helixi390 – 403Combined sources14
Beta strandi409 – 414Combined sources6
Helixi417 – 420Combined sources4
Beta strandi444 – 446Combined sources3
Helixi447 – 465Combined sources19

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LFWX-ray1.80A1-470[»]
ProteinModelPortaliP45494.
SMRiP45494.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP45494.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M20A family.Curated

Family and domain databases

CDDicd03888. M20_PepV. 1 hit.
Gene3Di3.30.70.360. 2 hits.
InterProiIPR001261. ArgE/DapE_CS.
IPR010964. M20A_pepV-rel.
IPR011291. Pept_M20A_peptidaseV.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view]
PfamiPF01546. Peptidase_M20. 1 hit.
[Graphical view]
SUPFAMiSSF55031. SSF55031. 1 hit.
TIGRFAMsiTIGR01886. dipeptidase. 1 hit.
TIGR01887. dipeptidaselike. 1 hit.
PROSITEiPS00758. ARGE_DAPE_CPG2_1. 1 hit.
PS00759. ARGE_DAPE_CPG2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P45494-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDLNFKELAE AKKDAILKDL EELIAIDSSE DLENATEEYP VGKGPVDAMT
60 70 80 90 100
KFLSFAKRDG FDTENFANYA GRVNFGAGDK RLGIIGHMDV VPAGEGWTRD
110 120 130 140 150
PFKMEIDEEG RIYGRGSADD KGPSLTAYYG MLLLKEAGFK PKKKIDFVLG
160 170 180 190 200
TNEETNWVGI DYYLKHEPTP DIVFSPDAEY PIINGEQGIF TLEFSFKNDD
210 220 230 240 250
TKGDYVLDKF KAGIATNVTP QVTRATISGP DLEAVKLAYE SFLADKELDG
260 270 280 290 300
SFEINDESAD IVLIGQGAHA SAPQVGKNSA TFLALFLDQY AFAGRDKNFL
310 320 330 340 350
HFLAEVEHED FYGKKLGIFH HDDLMGDLAS SPSMFDYEHA GKASLLNNVR
360 370 380 390 400
YPQGTDPDTM IKQVLDKFSG ILDVTYNGFE EPHYVPGSDP MVQTLLKVYE
410 420 430 440 450
KQTGKPGHEV VIGGGTYGRL FERGVAFGAQ PENGPMVMHA ANEFMMLDDL
460 470
ILSIAIYAEA IYELTKDEEL
Length:470
Mass (Da):51,990
Last modified:November 1, 1995 - v1
Checksum:i488117B4F33E4AB0
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z31377 Genomic DNA. Translation: CAA83252.1.
PIRiS57902.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
Z31377 Genomic DNA. Translation: CAA83252.1.
PIRiS57902.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1LFWX-ray1.80A1-470[»]
ProteinModelPortaliP45494.
SMRiP45494.
ModBaseiSearch...
MobiDBiSearch...

Protein family/group databases

MEROPSiM20.004.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Miscellaneous databases

EvolutionaryTraceiP45494.

Family and domain databases

CDDicd03888. M20_PepV. 1 hit.
Gene3Di3.30.70.360. 2 hits.
InterProiIPR001261. ArgE/DapE_CS.
IPR010964. M20A_pepV-rel.
IPR011291. Pept_M20A_peptidaseV.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view]
PfamiPF01546. Peptidase_M20. 1 hit.
[Graphical view]
SUPFAMiSSF55031. SSF55031. 1 hit.
TIGRFAMsiTIGR01886. dipeptidase. 1 hit.
TIGR01887. dipeptidaselike. 1 hit.
PROSITEiPS00758. ARGE_DAPE_CPG2_1. 1 hit.
PS00759. ARGE_DAPE_CPG2_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPEPV_LACDL
AccessioniPrimary (citable) accession number: P45494
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: November 2, 2016
This is version 87 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure

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.