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P07662 (G7AC_PSEU7) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 83. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | 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:
Glutaryl-7-aminocephalosporanic-acid acylase

Short name=Glutaryl-7-ACA acylase
EC=3.5.1.93
Alternative name(s):
7-beta-(4-carboxybutanamido)cephalosporanic acid acylase
GL-7-ACA acylase
Short name=GCA

Cleaved into the following 2 chains:

  1. Glutaryl-7-aminocephalosporanic-acid acylase subunit alpha
    Short name=Glutaryl-7-ACA acylase subunit alpha
  2. Glutaryl-7-aminocephalosporanic-acid acylase subunit beta
    Short name=Glutaryl-7-ACA acylase subunit beta
OrganismPseudomonas sp. (strain SY-77)
Taxonomic identifier269086 [NCBI]
Taxonomic lineageBacteriaProteobacteriaGammaproteobacteriaPseudomonadalesPseudomonadaceaePseudomonas

Protein attributes

Sequence length720 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 deacylation of 7 beta-(4-carboxybutanamido)cephalosporanic acid (glutaryl-7-aminocephalosporanic acid or GL-7-ACA) to 7-aminocephalosporanic acid (7-ACA). Ref.2

Catalytic activity

(7R)-7-(4-carboxybutanamido)cephalosporanate + H2O = (7R)-7-aminocephalosporanate + glutarate.

Subunit structure

Heterotetramer of two alpha and two beta subunits processed from the same precursor. Ref.3

Subcellular location

Periplasm Ref.2.

Induction

By glutaric acid. Ref.2

Sequence similarities

Belongs to the peptidase S45 family.

Ontologies

Keywords
   Biological processAntibiotic resistance
   Cellular componentPeriplasm
   DomainSignal
   Molecular functionHydrolase
   PTMZymogen
   Technical term3D-structure
Direct protein sequencing
Gene Ontology (GO)
   Biological_processantibiotic biosynthetic process

Inferred from electronic annotation. Source: InterPro

response to antibiotic

Inferred from electronic annotation. Source: UniProtKB-KW

   Cellular_componentperiplasmic space

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionglutaryl-7-aminocephalosporanic-acid acylase activity

Inferred from electronic annotation. Source: UniProtKB-EC

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2929 Ref.2
Chain30 – 720691Glutaryl-7-aminocephalosporanic-acid acylase
PRO_0000027353
Chain30 – 189160Glutaryl-7-aminocephalosporanic-acid acylase subunit alpha
PRO_0000027354
Propeptide190 – 1989Spacer peptide
PRO_0000253351
Chain199 – 720522Glutaryl-7-aminocephalosporanic-acid acylase subunit beta
PRO_0000027355

Sites

Active site1991Nucleophile
Active site2211 Potential
Active site6531 Potential

Experimental info

Mutagenesis1991S → A: Loss of activity. Lack of autoprocessing. Ref.3
Sequence conflict791H → Q in AAA25826. Ref.2
Sequence conflict1541E → D in AAA25826. Ref.2

Secondary structure

................................................................................................................................ 720
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P07662 [UniParc].

Last modified October 17, 2006. Version 2.
Checksum: 643250675A266C33

FASTA72079,627
        10         20         30         40         50         60 
MLRVLHRAAS ALVMATVIGL APAVAFALAE PTSTPQAPIA AYKPRSNEIL WDGYGVPHIY 

        70         80         90        100        110        120 
GVDAPSAFYG YGWAQARSHG DNILRLYGEA RGKGAEYWGP DYEQTTVWLL TNGVPERAQQ 

       130        140        150        160        170        180 
WYAQQSPDFR ANLDAFAAGI NAYAQQNPDD ISPEVRQVLP VSGADVVAHA HRLMNFLYVA 

       190        200        210        220        230        240 
SPGRTLGEGD PPDLADQGSN SWAVAPGKTA NGNALLLQNP HLSWTTDYFT YYEAHLVTPD 

       250        260        270        280        290        300 
FEIYGATQIG LPVIRFAFNQ RMGITNTVNG MVGATNYRLT LQDGGYLYDG QVRPFERPQA 

       310        320        330        340        350        360 
SYRLRQADGT TVDKPLEIRS SVHGPVFERA DGTAVAVRVA GLDRPGMLEQ YFDMITADSF 

       370        380        390        400        410        420 
DDYEAALARM QVPTFNIVYA DREGTINYSF NGVAPKRAEG DIAFWQGLVP GDSSRYLWTE 

       430        440        450        460        470        480 
THPLDDLPRV TNPPGGFVQN SNDPPWTPTW PVTYTPKDFP SYLAPQTPHS LRAQQSVRLM 

       490        500        510        520        530        540 
SENDDLTLER FMALQLSHRA VMADRTLPDL IPAALIDPDP EVQAAARLLA AWDREFTSDS 

       550        560        570        580        590        600 
RAALLFEEWA RLFAGQNFAG QAGFATPWSL DKPVSTPYGV RDPKAAVDQL RTAIANTKRK 

       610        620        630        640        650        660 
YGAIDRPFGD ASRMILNDVN VPGAAGYGNL GSFRVFTWSD PDENGVRTPV HGETWVAMIE 

       670        680        690        700        710        720 
FSTPVRAYGL MSYGNSRQPG TTHYSDQIER VSRADFRELL LRREQVEAAV QERTPFNFKP 

« Hide

References

[1]"Directed evolution of a glutaryl acylase into an adipyl acylase."
Sio C.F., Riemens A.M., Van Der Laan J.M., Verhaert R.M., Quax W.J.
Eur. J. Biochem. 269:4495-4504(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[2]"Molecular cloning and structure of the gene for 7 beta-(4-carboxybutanamido)cephalosporanic acid acylase from a Pseudomonas strain."
Matsuda A., Komatsu K.
J. Bacteriol. 163:1222-1228(1985) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-311, PROTEIN SEQUENCE OF 30-46 AND 199-215, FUNCTION, SUBCELLULAR LOCATION, INDUCTION.
[3]"Crystal structures of glutaryl 7-aminocephalosporanic acid acylase: insight into autoproteolytic activation."
Kim J.K., Yang I.S., Rhee S., Dauter Z., Lee Y.S., Park S.S., Kim K.H.
Biochemistry 42:4084-4093(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 30-189 AND 199-720 OF WILD-TYPE AND 30-720 OF MUTANT ALA-199, SUBUNIT, MUTAGENESIS OF SER-199, AUTOCATALYTIC PROCESSING MECHANISM.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF458663 Genomic DNA. Translation: AAN39264.1.
M11436 Genomic DNA. Translation: AAA25826.1.
PIRA24928.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1GK0X-ray2.50A/C36-188[»]
B/D199-720[»]
1GK1X-ray2.40A/C36-188[»]
B/D199-720[»]
1OR0X-ray2.00A/C30-189[»]
B/D199-720[»]
2ADVX-ray2.24A30-195[»]
B199-226[»]
C227-720[»]
2AE3X-ray2.40A30-195[»]
B199-720[»]
2AE4X-ray2.30A30-195[»]
B199-720[»]
2AE5X-ray2.24A30-195[»]
B200-720[»]
3S8RX-ray2.50A/B30-720[»]
ProteinModelPortalP07662.
SMRP07662. Positions 35-720.
ModBaseSearch...
MobiDBSearch...

Protein family/group databases

MEROPSS45.002.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Family and domain databases

Gene3D1.10.439.10. 1 hit.
3.60.20.10. 2 hits.
InterProIPR029055. Ntn_hydrolases_N.
IPR014395. Pen/cephalosporin_acylase.
IPR002692. Penicillin_amidase-like.
IPR023343. Penicillin_amidase_dom1.
[Graphical view]
PfamPF01804. Penicil_amidase. 2 hits.
[Graphical view]
PIRSFPIRSF001227. Pen_acylase. 1 hit.
SUPFAMSSF56235. SSF56235. 1 hit.
ProtoNetSearch...

Other

EvolutionaryTraceP07662.

Entry information

Entry nameG7AC_PSEU7
AccessionPrimary (citable) accession number: P07662
Secondary accession number(s): Q84I62
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: October 17, 2006
Last modified: July 9, 2014
This is version 83 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

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references