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P15557 (PAC1_PSES3) Reviewed, UniProtKB/Swiss-Prot

Last modified October 19, 2011. Version 55. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (1) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Acylase ACY 1

Cleaved into the following 2 chains:

  1. Acylase ACY 1 large subunit
  2. Acylase ACY 1 small subunit

Including the following 2 domains:

  1. Cephalosporin acylase
    EC=3.5.1.-
    Alternative name(s):
    GL-7ACA acylase
  2. Gamma-glutamyltranspeptidase
    Short name=GGT
    EC=2.3.2.2
Gene names
Name:acyI
OrganismPseudomonas sp. (strain SE83)
Taxonomic identifier309 [NCBI]
Taxonomic lineageBacteriaProteobacteria

Protein attributes

Sequence length558 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Besides the cephalosporin acylase I activity which converts GL-7ACA into 7-ACA; this enzyme displays some gamma glutamyltranspeptidase activity.

Catalytic activity

7-beta-(4-carboxybutanamido)-cephalosporanic acid + H2O = 7-aminocephalosporanic acid + glutaric acid.

(5-L-glutamyl)-peptide + an amino acid = peptide + 5-L-glutamyl amino acid.

Glutathione + H2O = L-cysteinylglycine + L-glutamate.

Subunit structure

Dimer of two non-identical chains processed from the same precursor.

Sequence similarities

Belongs to the gamma-glutamyltransferase family.

Ontologies

Keywords
   Biological processAntibiotic resistance
   Molecular functionAcyltransferase
Hydrolase
Transferase
   PTMZymogen
   Technical termDirect protein sequencing
Gene Ontology (GO)
   Biological processresponse to antibiotic

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functiongamma-glutamyltransferase activity

Inferred from electronic annotation. Source: EC

hydrolase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.1
Chain2 – ?367366Acylase ACY 1 large subunit
PRO_0000011080
Chain368 – 558191Acylase ACY 1 small subunit
PRO_0000011081

Sequences

Sequence LengthMass (Da)Tools
P15557 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 9659691DE0DC528B

FASTA55858,095
        10         20         30         40         50         60 
MNAPVPVPRV ADFTCEKKPA SGSRGMVVTN HPLASAAGAQ ILLAGGNAID AAVASLFALT 

        70         80         90        100        110        120 
VAEPMMVGIL GGGLSHIRLA DGRHVVIDNL STAPGKATAE MYECLSDEIG KQRDTRDRQN 

       130        140        150        160        170        180 
VVGAKAVAVP GALKGWCEAL ARFGTLPLAE VLQPAIGLAE RGFVVTPYLS NCITDNAGDL 

       190        200        210        220        230        240 
ARDPGLAAML LPGGKPLQPG MRLVQSDYAA SLKLIAAEGP DALYGGKLGR ALTDYMAANG 

       250        260        270        280        290        300 
GLIDQADLAN YRIELREPIR GSYRGYEIIG PPPPSSSGVH ITQMLNILEG YDIGSLGFGS 

       310        320        330        340        350        360 
TDAVHLLAEA LKIAFADRAV ATADPAFVKV PVARLIDKAY ADERRALIEM EQAKSWTAGL 

       370        380        390        400        410        420 
SGGESADTTH VTVADAMGNV VSATQTINGL FGACVQIPGT GMIANNYMYN FDPHPGRALS 

       430        440        450        460        470        480 
IAPGKRVFTS MAPMMALKEG RIAFALGLPG ALRIFPSALQ AIVNLIDHRM SLQEAVEAPR 

       490        500        510        520        530        540 
VWTEGGVLEL EEAIPEAVAQ ALIARGHKVV RSPRVAGGMN AIAFNPDGTL TGAACWRADG 

       550 
TPVAISGGLA RAGARFTI 

« Hide

References

[1]"Nucleotide sequences of the genes for two distinct cephalosporin acylases from a Pseudomonas strain."
Matsuda A., Toma K., Komatsu K.
J. Bacteriol. 169:5821-5826(1987) [PubMed: 3680178] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], PROTEIN SEQUENCE OF 2-22 AND 368-388.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M18279 Genomic DNA. Translation: AAA88424.1.
PIRB28392.

3D structure databases

ProteinModelPortalP15557.
ModBaseSearch...

Protein family/group databases

MEROPST03.001.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

InterProIPR000101. GGT_peptidase.
[Graphical view]
PANTHERPTHR11686. GGT_peptidase. 1 hit.
PfamPF01019. G_glu_transpept. 1 hit.
[Graphical view]
PRINTSPR01210. GGTRANSPTASE.
TIGRFAMsTIGR00066. G_glut_trans. 1 hit.
PROSITEPS00462. G_GLU_TRANSPEPTIDASE. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry namePAC1_PSES3
AccessionPrimary (citable) accession number: P15557
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1990
Last sequence update: January 23, 2007
Last modified: October 19, 2011
This is version 55 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families