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P06621 (CBPG_PSES6) Reviewed, UniProtKB/Swiss-Prot

Last modified April 3, 2013. Version 85. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Carboxypeptidase G2
Short name=CPDG2
EC=3.4.17.11
Alternative name(s):
Folate hydrolase G2
Glutamate carboxypeptidase
Pteroylmonoglutamic acid hydrolase G2
INN=Glucarpidase
Gene names
Name:cpg2
OrganismPseudomonas sp. (strain RS-16)
Taxonomic identifier312 [NCBI]
Taxonomic lineageBacteria › Proteobacteria ›

Protein attributes

Sequence length415 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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

Catalytic activity

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

Cofactor

Binds 2 zinc ions per subunit. Ref.4

Subunit structure

Homodimer.

Pharmaceutical use

Used clinically as a folate-depleting, antitumor agent.

Sequence similarities

Belongs to the peptidase M20A family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2222
Chain23 – 415393Carboxypeptidase G2
PRO_0000026808

Sites

Active site1141 By similarity
Active site1751Proton acceptor Ref.4
Metal binding1121Zinc 2
Metal binding1411Zinc 1
Metal binding1411Zinc 2
Metal binding1761Zinc 1
Metal binding2001Zinc 2
Metal binding3851Zinc 1

Secondary structure

1 ............................................................ 415
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P06621 [UniParc].

Last modified January 1, 1988. Version 1.
Checksum: 8483A52202CE9C5E

FASTA41543,932
        10         20         30         40         50         60 
MRPSIHRTAI AAVLATAFVA GTALAQKRDN VLFQAATDEQ PAVIKTLEKL VNIETGTGDA 

        70         80         90        100        110        120 
EGIAAAGNFL EAELKNLGFT VTRSKSAGLV VGDNIVGKIK GRGGKNLLLM SHMDTVYLKG 

       130        140        150        160        170        180 
ILAKAPFRVE GDKAYGPGIA DDKGGNAVIL HTLKLLKEYG VRDYGTITVL FNTDEEKGSF 

       190        200        210        220        230        240 
GSRDLIQEEA KLADYVLSFE PTSAGDEKLS LGTSGIAYVQ VNITGKASHA GAAPELGVNA 

       250        260        270        280        290        300 
LVEASDLVLR TMNIDDKAKN LRFNWTIAKA GNVSNIIPAS ATLNADVRYA RNEDFDAAMK 

       310        320        330        340        350        360 
TLEERAQQKK LPEADVKVIV TRGRPAFNAG EGGKKLVDKA VAYYKEAGGT LGVEERTGGG 

       370        380        390        400        410 
TDAAYAALSG KPVIESLGLP GFGYHSDKAE YVDISAIPRR LYMAARLIMD LGAGK

« Hide

References

[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.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		M12599 Genomic DNA. Translation: AAA62842.1.
PIRYXPSF2. A24955.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1CG2X-ray2.50A/B/C/D23-415[»]
ProteinModelPortalP06621.
SMRP06621. Positions 26-414.
ModBaseSearch...

Protein family/group databases

MEROPSM20.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Enzyme and pathway databases

SABIO-RKP06621.

Family and domain databases

InterProIPR001261. ArgE/DapE_CS.
IPR017150. Pept_M20_glutamate_carboxypep.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view]
PfamPF07687. M20_dimer. 1 hit.
PF01546. Peptidase_M20. 1 hit.
[Graphical view]
PIRSFPIRSF037238. Carboxypeptidase_G2. 1 hit.
SUPFAMSSF55031. Peptidase_M20_dimer. 1 hit.
PROSITEPS00758. ARGE_DAPE_CPG2_1. 1 hit.
PS00759. ARGE_DAPE_CPG2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceP06621.

Entry information

Entry nameCBPG_PSES6
AccessionPrimary (citable) accession number: P06621
Entry history
Integrated into UniProtKB/Swiss-Prot: January 1, 1988
Last sequence update: January 1, 1988
Last modified: April 3, 2013
This is version 85 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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