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Protein

Aminoacylase-1B

Gene

Acy1b

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Involved in the hydrolysis of N-acylated or N-acetylated amino acids (except L-aspartate).1 Publication

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

Zn2+By similarityNote: Binds 2 Zn2+ ions per subunit.By similarity

Sites

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

GO - Molecular functioni

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

GO - Biological processi

  1. cellular amino acid metabolic process Source: InterPro
  2. protein catabolic process Source: RGD
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase

Keywords - Ligandi

Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Aminoacylase-1B (EC:3.5.1.14)
Short name:
ACY-1B
Alternative name(s):
ACY IB
N-acyl-L-amino-acid amidohydrolase
Gene namesi
Name:Acy1b
Synonyms:Acy1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
ProteomesiUP000002494 Componenti: Unplaced

Organism-specific databases

RGDi2030. Acy1.

Subcellular locationi

  1. 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
Chaini1 – 408408Aminoacylase-1BPRO_0000274010Add
BLAST

Proteomic databases

PRIDEiQ6PTT0.

Expressioni

Gene expression databases

GenevestigatoriQ6PTT0.

Interactioni

Subunit structurei

Homodimer.By similarity

Structurei

3D structure databases

ProteinModelPortaliQ6PTT0.
SMRiQ6PTT0. Positions 7-198, 321-408.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase M20A family.Curated

Phylogenomic databases

HOVERGENiHBG000982.
PhylomeDBiQ6PTT0.

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.

Q6PTT0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTSKGPEEEH PSVTLFRQYL RIRTVQPKPD YGAAVAFFEE TARQLGLGCQ
60 70 80 90 100
KVEVAPGYVV TVLTWPGTNP TLSSILLNSH TDVVPVFKEH WSHDPFEAFK
110 120 130 140 150
DSEGYIYTRG AQDMKCVSIQ YLEAVKRLKV EGHRFPRTIH MTFVPDEEVG
160 170 180 190 200
GHQGMELFVQ RHEFHALRAG FALDEGLANP TDAFTVFYSE RSPWWVRVTS
210 220 230 240 250
TGRPGHASRF MEDTAAEKLH KVVNSILAFR EKEWQRLQSN PHLKEGSVTS
260 270 280 290 300
VNLTKLEGGV AYNVVPATMS ACFDFRVAPD VDMKAFEEQL QSWCQEAGEG
310 320 330 340 350
VTFEFAQKFT EPRMTPTDDT DPWWAAFSGA CKEMTLTLEP EIFPAATDSR
360 370 380 390 400
YIRAVGIPAL GFSPMNRTPV LLHDHNERLH EAVFLRGVDI YTRLVAALAS

VPALPGES
Length:408
Mass (Da):45,823
Last modified:July 5, 2004 - v1
Checksum:iF335317AF2574927
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY580165 mRNA. Translation: AAS90691.1.
UniGeneiRn.3679.

Genome annotation databases

UCSCiRGD:2030. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY580165 mRNA. Translation: AAS90691.1.
UniGeneiRn.3679.

3D structure databases

ProteinModelPortaliQ6PTT0.
SMRiQ6PTT0. Positions 7-198, 321-408.
ModBaseiSearch...
MobiDBiSearch...

Proteomic databases

PRIDEiQ6PTT0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

UCSCiRGD:2030. rat.

Organism-specific databases

RGDi2030. Acy1.

Phylogenomic databases

HOVERGENiHBG000982.
PhylomeDBiQ6PTT0.

Gene expression databases

GenevestigatoriQ6PTT0.

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]
ProtoNetiSearch...

Publicationsi

  1. "The rat kidney acylase I, characterization and molecular cloning. Differences with other acylases I."
    Giardina T., Perrier J., Puigserver A.
    Eur. J. Biochem. 267:6249-6255(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 161-178, FUNCTION.
    Strain: Wistar.
    Tissue: Kidney.
  2. "The rat kidney acylase 1. Evidence for a new cDNA form and comparisons with the porcine intestinal enzyme."
    Perrier J., Durand A., Giardina T., Puigserver A.
    Comp. Biochem. Physiol. 138B:277-283(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Wistar.

Entry informationi

Entry nameiACY1B_RAT
AccessioniPrimary (citable) accession number: Q6PTT0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 23, 2007
Last sequence update: July 5, 2004
Last modified: April 29, 2015
This is version 68 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.