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Reviewed, UniProtKB/Swiss-Prot Q5RFB0 (ACY1_PONAB)

Last modified September 22, 2009. Version 30. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Aminoacylase-1
    EC=3.5.1.14
Alternative name(s):
    N-acyl-L-amino-acid amidohydrolase
    ACY-1
Gene names
Name: ACY1
OrganismPongo abelii (Sumatran orangutan)
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

Protein attributes

Sequence length408 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 408408Aminoacylase-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
Q5RFB0-1 [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

CR857251 mRNA. Translation: CAH89547.1. Different initiation.
RefSeqNP_001124673.1.
UniGenePab.19502

3D structure databases

SMRQ5RFB0. Positions 7-198, 321-408.
ModBaseSearch...

Genome annotation databases

GeneID100171519.

Organism-specific databases

CTD100171519.

Phylogenomic databases

HOVERGENQ5RFB0.

Enzyme and pathway databases

BRENDA3.5.1.14. 269192.

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.
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: September 22, 2009
This is version 30 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Peptidase families

Classification of peptidase families and list of entries

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents