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P06621

- CBPG_PSES6

UniProt

P06621 - CBPG_PSES6

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Protein
Carboxypeptidase G2
Gene
cpg2
Organism
Pseudomonas sp. (strain RS-16)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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 2
Active sitei114 – 1141 By similarity
Metal bindingi141 – 1411Zinc 1
Metal bindingi141 – 1411Zinc 2
Active sitei175 – 1751Proton acceptor1 Publication
Metal bindingi176 – 1761Zinc 1
Metal bindingi200 – 2001Zinc 2
Metal bindingi385 – 3851Zinc 1

GO - Molecular functioni

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

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 – 2222
Add
BLAST
Chaini23 – 415393Carboxypeptidase G2
PRO_0000026808Add
BLAST

Interactioni

Subunit structurei

Homodimer.

Structurei

Secondary structure

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.

Miscellaneous databases

EvolutionaryTraceiP06621.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M20A family.

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

« Hide

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: May 14, 2014
This is version 88 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

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