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UniProtKB - B2KZE7 (TPDA_CORST)

Entry version 35 (23 Feb 2022)
Sequence version 1 (10 Jun 2008)
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Protein

Cysteinylglycine-S-conjugate dipeptidase

Gene

tpdA

Organism
Corynebacterium striatum
Status
Reviewed-Annotation score:

Annotation score:3 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Metallopeptidase that hydrolyzes the Cys-Gly bond of Cys-Gly-S-conjugates (PubMed:18515361).

Involved in the formation of the human body odorant 3-methyl-3-sulfanylhexan-1-ol (3M3SH) from odorless axilla secretions. Catalyzes the hydrolysis of the Cys-Gly bond of the Cys-Gly-S-conjugate of 3M3SH, a key precursor secreted by apocrine glands in human axilla skin. The Cys-S-conjugate obtained is then cleaved by the Cys-S-conjugate beta-lyase MetC, which finally releases 3M3SH (PubMed:18515361).

1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the 'Function' section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Zn2+By similarity

<p>This subsection of the 'Function' section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=0.045 mM for S-(1-hydroxy-3-methylhexan-3-yl)-L-cysteinylglycine1 Publication
  2. KM=0.2 mM for S-benzyl-L-cysteinylglycine1 Publication
  1. Vmax=0.023 mmol/min/mg enzyme with S-(1-hydroxy-3-methylhexan-3-yl)-L-cysteinylglycine as substrate1 Publication
  2. Vmax=0.169 mmol/min/mg enzyme with S-benzyl-L-cysteinylglycine as substrate1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the 'Description' field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi92Zinc 1; via amino nitrogenBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei94By similarity1
Metal bindingi125Zinc 1By similarity1
Metal bindingi125Zinc 2By similarity1
Active sitei158Proton acceptorBy similarity1
Metal bindingi159Zinc 2By similarity1
Metal bindingi163Zinc 2By similarity1
Metal bindingi428Zinc 2; via amino nitrogenBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionAminopeptidase, Dipeptidase, Hydrolase, Protease
LigandCobalt, Metal-binding, Zinc

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...BRENDAi		3.4.13.23, 7918

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Cysteinylglycine-S-conjugate dipeptidase1 Publication (EC:3.4.13.231 Publication)
Alternative name(s):
Thiol precursor dipeptidase1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:tpdA1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiCorynebacterium striatum
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri43770 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiBacteria › Actinobacteria › Corynebacteriales › Corynebacteriaceae › Corynebacterium

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004512111 – 455Cysteinylglycine-S-conjugate dipeptidaseAdd BLAST455

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		B2KZE7

Database of comparative protein structure models

More...ModBasei		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the peptidase M20F family.Curated

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR001261, ArgE/DapE_CS
IPR036264, Bact_exopeptidase_dim_dom
IPR002933, Peptidase_M20
IPR011650, Peptidase_M20_dimer

Pfam protein domain database

More...Pfami		View protein in Pfam
PF07687, M20_dimer, 1 hit
PF01546, Peptidase_M20, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF55031, SSF55031, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00758, ARGE_DAPE_CPG2_1, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

B2KZE7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MSNDKAATST NFNLTPNRER IFQELSELIS HYSPHSMPEH ADTHEEAAKW 
        60         70         80         90        100
VTAKLEELGL DVTRHPTVDD ADTIIGVKEP VGDAPTILLY SHYDVVPAQN 
       110        120        130        140        150
PAVWTNDPLE LDERDGRWYG RGAADCKGNV IMHLEALRMV QENGGTDLGL 
       160        170        180        190        200
KVVMEGSEEL GGEDGLGKLI DANPELFTAD VIFIGDGGNV AVGIPTLTTH 
       210        220        230        240        250
LRGGAQLRFK VDTLEGPVHS GGWGGAAPDA AHALIRIIDS FFDEHGRTTI 
       260        270        280        290        300
EGVDTTAKWE GDPYDRETFR KDARVLDGVQ LLGTVDDEPA DMVWARPAIT 
       310        320        330        340        350
VIGFTSVPVE DATNIVNPTA EAQFNLRVPA PQSAAEVAKK VEEQIRARAP 
       360        370        380        390        400
WGAKVEVSIT GVNEPFSTDP NGPAVQHFGK CLQDAYGAEH LTVVGTGGSI 
       410        420        430        440        450
PLTVTLQKHF PDAEFALYGV ADPAANIHGV DESVDPTEIE HVAIAEAEFL 

LTYGK
Length:455
Mass (Da):49,000
Last modified:June 10, 2008 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i9035C5B7483BC161
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
EU311559 Genomic DNA Translation: ACA03770.1

Genome annotation databases

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		ag:ACA03770

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
EU311559 Genomic DNA Translation: ACA03770.1

3D structure databases

SMRiB2KZE7
ModBaseiSearch...

Genome annotation databases

KEGGiag:ACA03770

Enzyme and pathway databases

BRENDAi3.4.13.23, 7918

Family and domain databases

InterProiView protein in InterPro
IPR001261, ArgE/DapE_CS
IPR036264, Bact_exopeptidase_dim_dom
IPR002933, Peptidase_M20
IPR011650, Peptidase_M20_dimer
PfamiView protein in Pfam
PF07687, M20_dimer, 1 hit
PF01546, Peptidase_M20, 1 hit
SUPFAMiSSF55031, SSF55031, 1 hit
PROSITEiView protein in PROSITE
PS00758, ARGE_DAPE_CPG2_1, 1 hit

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiTPDA_CORST
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: B2KZE7
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 7, 2020
Last sequence update: June 10, 2008
Last modified: February 23, 2022
This is version 35 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
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