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Q5RFB0

- ACY1_PONAB

UniProt

Q5RFB0 - ACY1_PONAB

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Protein
Aminoacylase-1
Gene
ACY1
Organism
Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Status
Reviewed - Annotation score: 3 out of 5 - Experimental evidence at transcript leveli

Functioni

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

Catalytic activityi

An N-acyl-aliphatic-L-amino acid + H2O = an aliphatic L-amino acid + a carboxylate.
An N-acetyl-L-cysteine-S-conjugate + H2O = an L-cysteine-S-conjugate + acetate.

Cofactori

Binds 2 zinc ions per subunit By similarity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi80 – 801Zinc 1 By similarity
Active sitei82 – 821 By similarity
Metal bindingi113 – 1131Zinc 1 By similarity
Metal bindingi113 – 1131Zinc 2 By similarity
Active sitei147 – 1471Proton acceptor By similarity
Metal bindingi148 – 1481Zinc 2 By similarity
Metal bindingi175 – 1751Zinc 1 By similarity
Metal bindingi373 – 3731Zinc 2 By similarity

GO - Molecular functioni

  1. aminoacylase activity Source: UniProtKB-EC
  2. metal ion binding Source: UniProtKB-KW
  3. metallopeptidase activity Source: InterPro

GO - Biological processi

  1. cellular amino acid metabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Aminoacylase-1 (EC:3.5.1.14)
Short name:
ACY-1
Alternative name(s):
N-acyl-L-amino-acid amidohydrolase
Gene namesi
Name:ACY1
OrganismiPongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii)
Taxonomic identifieri9601 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo
ProteomesiUP000001595: Unplaced

Subcellular locationi

Cytoplasm By similarity

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed By similarity
Chaini2 – 408407Aminoacylase-1
PRO_0000274008Add
BLAST

Interactioni

Subunit structurei

Homodimer By similarity. Interacts with SPHK1 By similarity.

Structurei

3D structure databases

ProteinModelPortaliQ5RFB0.
SMRiQ5RFB0. Positions 7-198, 321-408.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M20A family.

Phylogenomic databases

HOVERGENiHBG000982.
InParanoidiQ5RFB0.
KOiK14677.

Family and domain databases

Gene3Di3.30.70.360. 1 hit.
InterProiIPR001261. ArgE/DapE_CS.
IPR010159. N-acyl_aa_amidohydrolase.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view]
PfamiPF07687. M20_dimer. 1 hit.
PF01546. Peptidase_M20. 1 hit.
[Graphical view]
PIRSFiPIRSF036696. ACY-1. 1 hit.
SUPFAMiSSF55031. SSF55031. 1 hit.
TIGRFAMsiTIGR01880. Ac-peptdase-euk. 1 hit.
PROSITEiPS00758. ARGE_DAPE_CPG2_1. 1 hit.
PS00759. ARGE_DAPE_CPG2_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

Q5RFB0-1 [UniParc]FASTAAdd to Basket

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MTSKGPEEEH PSVTLFRQYL RIRTVQPKPD YGAAVAFFEE RARQLGLGCQ    50
KVEVAPGYVV TVLTWPGTNP TLSSILLNSH TDVVPVFKEH WSHDPFEAFK 100
DSEGYIYARG AQDMKCISIQ YLEAVRRLKV EGHRFPRTIH MTFVPDEEVG 150
GHQGMELFVQ RPEFHALRAG FALDEGIANP TDAFTVFYSE RSPWWVRVTS 200
TGRPGHASRF MEDTAAEKLH KVVSSILAFR EKEWQRLQSN PHLKEGSVTS 250
VNLTKLEGGV AYNVIPATMS ASFDFRVAPD VDFKAFEEQL QSWCQAAGEG 300
VTLEFAQKWM HPQVTPTDDS NPWWAAFSRV CKDMKLTLEP EIMPAATDNR 350
YIRAVGIPAL GFSPMNRTPV LLHDHDERLH EAVFLRGVDI YTRLLPALAS 400
VPALPSES 408
Length:408
Mass (Da):45,969
Last modified:January 23, 2007 - v2
Checksum:iDA5F3D6468261C84
GO

Sequence cautioni

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

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR857251 mRNA. Translation: CAH89547.1. Different initiation.
RefSeqiNP_001124673.1. NM_001131201.2.

Genome annotation databases

GeneIDi100171519.
KEGGipon:100171519.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
CR857251 mRNA. Translation: CAH89547.1 . Different initiation.
RefSeqi NP_001124673.1. NM_001131201.2.

3D structure databases

ProteinModelPortali Q5RFB0.
SMRi Q5RFB0. Positions 7-198, 321-408.
ModBasei Search...
MobiDBi Search...

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

GeneIDi 100171519.
KEGGi pon:100171519.

Organism-specific databases

CTDi 95.

Phylogenomic databases

HOVERGENi HBG000982.
InParanoidi Q5RFB0.
KOi K14677.

Family and domain databases

Gene3Di 3.30.70.360. 1 hit.
InterProi IPR001261. ArgE/DapE_CS.
IPR010159. N-acyl_aa_amidohydrolase.
IPR002933. Peptidase_M20.
IPR011650. Peptidase_M20_dimer.
[Graphical view ]
Pfami PF07687. M20_dimer. 1 hit.
PF01546. Peptidase_M20. 1 hit.
[Graphical view ]
PIRSFi PIRSF036696. ACY-1. 1 hit.
SUPFAMi SSF55031. SSF55031. 1 hit.
TIGRFAMsi TIGR01880. Ac-peptdase-euk. 1 hit.
PROSITEi PS00758. ARGE_DAPE_CPG2_1. 1 hit.
PS00759. ARGE_DAPE_CPG2_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

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

Entry informationi

Entry nameiACY1_PONAB
AccessioniPrimary (citable) accession number: Q5RFB0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: January 23, 2007
Last modified: May 14, 2014
This is version 54 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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