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P06621

- CBPG_PSES6

UniProt

P06621 - CBPG_PSES6

Protein

Carboxypeptidase G2

Gene

cpg2

Organism
Pseudomonas sp. (strain RS-16)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 89 (01 Oct 2014)
      Sequence version 1 (01 Jan 1988)
      Previous versions | rss
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    Functioni

    Catalyzes the hydrolysis of reduced and non-reduced folates to pteroates and L-glutamate. This enzyme has a broad specificity.

    Catalytic activityi

    Release of C-terminal glutamate residues from a wide range of N-acylating moieties, including peptidyl, aminoacyl, benzoyl, benzyloxycarbonyl, folyl and pteroyl groups.

    Cofactori

    Binds 2 zinc ions per subunit.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi112 – 1121Zinc 21 Publication
    Active sitei114 – 1141By similarity
    Metal bindingi141 – 1411Zinc 11 Publication
    Metal bindingi141 – 1411Zinc 21 Publication
    Active sitei175 – 1751Proton acceptor1 Publication
    Metal bindingi176 – 1761Zinc 11 Publication
    Metal bindingi200 – 2001Zinc 21 Publication
    Metal bindingi385 – 3851Zinc 11 Publication

    GO - Molecular functioni

    1. carboxypeptidase activity Source: UniProtKB-KW
    2. metal ion binding Source: UniProtKB-KW
    3. metallopeptidase activity Source: UniProtKB-KW

    Keywords - Molecular functioni

    Carboxypeptidase, Hydrolase, Metalloprotease, Protease

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    SABIO-RKP06621.

    Protein family/group databases

    MEROPSiM20.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Carboxypeptidase G2 (EC:3.4.17.11)
    Short name:
    CPDG2
    Alternative name(s):
    Folate hydrolase G2
    Glutamate carboxypeptidase
    Pteroylmonoglutamic acid hydrolase G2
    INN: Glucarpidase
    Gene namesi
    Name:cpg2
    OrganismiPseudomonas sp. (strain RS-16)
    Taxonomic identifieri312 [NCBI]
    Taxonomic lineageiBacteriaProteobacteria

    Pathology & Biotechi

    Pharmaceutical usei

    Used clinically as a folate-depleting, antitumor agent.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2222Add
    BLAST
    Chaini23 – 415393Carboxypeptidase G2PRO_0000026808Add
    BLAST

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Structurei

    Secondary structure

    1
    415
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi30 – 5122
    Helixi60 – 7617
    Beta strandi80 – 856
    Beta strandi92 – 1009
    Beta strandi107 – 1126
    Helixi121 – 1244
    Beta strandi128 – 1303
    Beta strandi133 – 1353
    Turni137 – 1426
    Helixi143 – 15816
    Beta strandi164 – 17310
    Helixi175 – 1773
    Turni178 – 1825
    Helixi183 – 19210
    Beta strandi194 – 1985
    Beta strandi208 – 2136
    Beta strandi215 – 22410
    Helixi234 – 2363
    Helixi240 – 25112
    Helixi252 – 2543
    Turni257 – 2604
    Beta strandi261 – 27010
    Beta strandi279 – 29113
    Helixi292 – 30615
    Beta strandi315 – 3228
    Helixi330 – 34617
    Beta strandi352 – 3554
    Helixi363 – 3664
    Helixi367 – 3693
    Beta strandi380 – 3823
    Beta strandi386 – 3883
    Beta strandi391 – 3933
    Helixi394 – 3963
    Helixi397 – 41216

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1CG2X-ray2.50A/B/C/D23-415[»]
    ProteinModelPortaliP06621.
    SMRiP06621. Positions 26-414.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP06621.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the peptidase M20A family.Curated

    Keywords - Domaini

    Signal

    Family and domain databases

    Gene3Di3.30.70.360. 1 hit.
    InterProiIPR001261. ArgE/DapE_CS.
    IPR017150. Pept_M20_glutamate_carboxypep.
    IPR002933. Peptidase_M20.
    IPR011650. Peptidase_M20_dimer.
    [Graphical view]
    PfamiPF07687. M20_dimer. 1 hit.
    PF01546. Peptidase_M20. 1 hit.
    [Graphical view]
    PIRSFiPIRSF037238. Carboxypeptidase_G2. 1 hit.
    SUPFAMiSSF55031. SSF55031. 1 hit.
    PROSITEiPS00758. ARGE_DAPE_CPG2_1. 1 hit.
    PS00759. ARGE_DAPE_CPG2_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    P06621-1 [UniParc]FASTAAdd to Basket

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    MRPSIHRTAI AAVLATAFVA GTALAQKRDN VLFQAATDEQ PAVIKTLEKL    50
    VNIETGTGDA EGIAAAGNFL EAELKNLGFT VTRSKSAGLV VGDNIVGKIK 100
    GRGGKNLLLM SHMDTVYLKG ILAKAPFRVE GDKAYGPGIA DDKGGNAVIL 150
    HTLKLLKEYG VRDYGTITVL FNTDEEKGSF GSRDLIQEEA KLADYVLSFE 200
    PTSAGDEKLS LGTSGIAYVQ VNITGKASHA GAAPELGVNA LVEASDLVLR 250
    TMNIDDKAKN LRFNWTIAKA GNVSNIIPAS ATLNADVRYA RNEDFDAAMK 300
    TLEERAQQKK LPEADVKVIV TRGRPAFNAG EGGKKLVDKA VAYYKEAGGT 350
    LGVEERTGGG TDAAYAALSG KPVIESLGLP GFGYHSDKAE YVDISAIPRR 400
    LYMAARLIMD LGAGK 415
    Length:415
    Mass (Da):43,932
    Last modified:January 1, 1988 - v1
    Checksum:i8483A52202CE9C5E
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12599 Genomic DNA. Translation: AAA62842.1.
    PIRiA24955. YXPSF2.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12599 Genomic DNA. Translation: AAA62842.1 .
    PIRi A24955. YXPSF2.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1CG2 X-ray 2.50 A/B/C/D 23-415 [» ]
    ProteinModelPortali P06621.
    SMRi P06621. Positions 26-414.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

    MEROPSi M20.001.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Enzyme and pathway databases

    SABIO-RK P06621.

    Miscellaneous databases

    EvolutionaryTracei P06621.

    Family and domain databases

    Gene3Di 3.30.70.360. 1 hit.
    InterProi IPR001261. ArgE/DapE_CS.
    IPR017150. Pept_M20_glutamate_carboxypep.
    IPR002933. Peptidase_M20.
    IPR011650. Peptidase_M20_dimer.
    [Graphical view ]
    Pfami PF07687. M20_dimer. 1 hit.
    PF01546. Peptidase_M20. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF037238. Carboxypeptidase_G2. 1 hit.
    SUPFAMi SSF55031. SSF55031. 1 hit.
    PROSITEi PS00758. ARGE_DAPE_CPG2_1. 1 hit.
    PS00759. ARGE_DAPE_CPG2_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The complete nucleotide sequence of the Pseudomonas gene coding for carboxypeptidase G2."
      Minton N.P., Atkinson T., Bruton C.J., Sherwood R.F.
      Gene 31:31-38(1984) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PARTIAL PROTEIN SEQUENCE.
    2. Erratum
      Minton N.P., Atkinson T., Bruton C.J., Sherwood R.F.
      Gene 42:353-353(1986)
    3. "Purification and properties of carboxypeptidase G2 from Pseudomonas sp. strain RS-16. Use of a novel triazine dye affinity method."
      Sherwood R.F., Melton R.G., Alwan S.M., Hughes P.
      Eur. J. Biochem. 148:447-453(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    4. "Crystal structure of carboxypeptidase G2, a bacterial enzyme with applications in cancer therapy."
      Rowsell S., Pauptit R.A., Tucker A.D., Melton R.G., Blow D.M., Brick P.
      Structure 5:337-347(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS) OF 23-415 IN COMPLEX WITH ZINC, COFACTOR, ACTIVE SITE.

    Entry informationi

    Entry nameiCBPG_PSES6
    AccessioniPrimary (citable) accession number: P06621
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: January 1, 1988
    Last sequence update: January 1, 1988
    Last modified: October 1, 2014
    This is version 89 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, Direct protein sequencing, Pharmaceutical

    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

    External Data

    Dasty 3