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Q5RFB0 (ACY1_PONAB) Reviewed, UniProtKB/Swiss-Prot

Last modified March 6, 2013. Version 50. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
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Names and origin

Protein namesRecommended name:
Aminoacylase-1
Short name=ACY-1
EC=3.5.1.14
Alternative name(s):
N-acyl-L-amino-acid amidohydrolase
Gene names
Name:ACY1
OrganismPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii) [Reference proteome]
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Pongo

Protein attributes

Sequence length408 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript level

General annotation (Comments)

Function

Involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate) By similarity.

Catalytic activity

An N-acyl-L-amino acid + H2O = a carboxylate + an L-amino acid.

Cofactor

Binds 2 zinc ions per subunit By similarity.

Subunit structure

Homodimer By similarity. Interacts with SPHK1 By similarity.

Subcellular location

Cytoplasm By similarity.

Sequence similarities

Belongs to the peptidase M20A family.

Sequence caution

The sequence CAH89547.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentCytoplasm
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular amino acid metabolic process

Inferred from electronic annotation. Source: InterPro

proteolysis

Inferred from electronic annotation. Source: InterPro

   Cellular_componentcytoplasm

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionaminoacylase activity

Inferred from electronic annotation. Source: EC

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

metallopeptidase activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 408407Aminoacylase-1
PRO_0000274008

Sites

Active site821 By similarity
Active site1471Proton acceptor By similarity
Metal binding801Zinc 1 By similarity
Metal binding1131Zinc 1 By similarity
Metal binding1131Zinc 2 By similarity
Metal binding1481Zinc 2 By similarity
Metal binding1751Zinc 1 By similarity
Metal binding3731Zinc 2 By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5RFB0 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: DA5F3D6468261C84

FASTA40845,969
        10         20         30         40         50         60 
MTSKGPEEEH PSVTLFRQYL RIRTVQPKPD YGAAVAFFEE RARQLGLGCQ KVEVAPGYVV 

        70         80         90        100        110        120 
TVLTWPGTNP TLSSILLNSH TDVVPVFKEH WSHDPFEAFK DSEGYIYARG AQDMKCISIQ 

       130        140        150        160        170        180 
YLEAVRRLKV EGHRFPRTIH MTFVPDEEVG GHQGMELFVQ RPEFHALRAG FALDEGIANP 

       190        200        210        220        230        240 
TDAFTVFYSE RSPWWVRVTS TGRPGHASRF MEDTAAEKLH KVVSSILAFR EKEWQRLQSN 

       250        260        270        280        290        300 
PHLKEGSVTS VNLTKLEGGV AYNVIPATMS ASFDFRVAPD VDFKAFEEQL QSWCQAAGEG 

       310        320        330        340        350        360 
VTLEFAQKWM HPQVTPTDDS NPWWAAFSRV CKDMKLTLEP EIMPAATDNR YIRAVGIPAL 

       370        380        390        400 
GFSPMNRTPV LLHDHDERLH EAVFLRGVDI YTRLLPALAS VPALPSES

« Hide

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		CR857251 mRNA. Translation: CAH89547.1. Different initiation.
RefSeqNP_001124673.1. NM_001131201.2.
UniGenePab.19502.

3D structure databases

HSSPHSSP built from PDB template 1Q7L based on UniProtKB Q03154.
ProteinModelPortalQ5RFB0.
SMRQ5RFB0. Positions 7-198, 321-408.
ModBaseSearch...

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

GeneID100171519.
KEGGpon:100171519.

Organism-specific databases

CTD95.

Phylogenomic databases

HOVERGENHBG000982.
InParanoidQ5RFB0.
KOK14677.

Family and domain databases

InterProIPR001261. ArgE/DapE_CS.
IPR010159. N-acyl_aa_amidohydrolase.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view]
PfamPF07687. M20_dimer. 1 hit.
PF01546. Peptidase_M20. 1 hit.
[Graphical view]
PIRSFPIRSF036696. ACY-1. 1 hit.
SUPFAMSSF55031. Peptidase_M20_dimer. 1 hit.
TIGRFAMsTIGR01880. Ac-peptdase-euk. 1 hit.
PROSITEPS00758. ARGE_DAPE_CPG2_1. 1 hit.
PS00759. ARGE_DAPE_CPG2_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Entry information

Entry nameACY1_PONAB
AccessionPrimary (citable) accession number: Q5RFB0
Entry history
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: January 23, 2007
Last modified: March 6, 2013
This is version 50 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

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